We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for L-Leucine (HMDB00687)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-03-10 14:54:30
Accession Number HMDB00687
Secondary Accession Numbers Not Available
Common Name L-Leucine
Description Branched chain amino acids (BCAA) are essential amino acids whose carbon structure is marked by a branch point. These three amino acids are critical to human life and are particularly involved in stress, energy and muscle metabolism. BCAA supplementation as therapy, both oral and intravenous, in human health and disease holds great promise. 'BCAA' denotes valine, isoleucine and leucine which are branched chain essential amino acids. Despite their structural similarities, the branched amino acids have different metabolic routes, with valine going solely to carbohydrates, leucine solely to fats and isoleucine to both. The different metabolism accounts for different requirements for these essential amino acids in humans: 12 mg/kg, 14 mg/kg and 16 mg/kg of valine, leucine and isoleucine respectively. Furthermore, these amino acids have different deficiency symptoms. Valine deficiency is marked by neurological defects in the brain, while isoleucine deficiency is marked by muscle tremors. Many types of inborn errors of BCAA metabolism exist, and are marked by various abnormalities. The most common form is the maple syrup urine disease, marked by a characteristic urinary odor. Other abnormalities are associated with a wide range of symptoms, such as mental retardation, ataxia, hypoglycemia, spinal muscle atrophy, rash, vomiting and excessive muscle movement. Most forms of BCAA metabolism errors are corrected by dietary restriction of BCAA and at least one form is correctable by supplementation with 10 mg of biotin daily. BCAA are useful because they are metabolized primarily by muscle. Stress state- e.g surgery, trauma, cirrhosis, infections, fever and starvation--require proportionately more BCAA than other amino acids and probably proportionately more leucine than either valine or isoleucine. BCAA and other amino acids are frequently fed intravenously (TPN) to malnourished surgical patients and in some cases of severe trauma. BCAA, particularly leucine, stimulate protein synthesis, increase reutilization of amino acids in many organs and reduce protein breakdown. Furthermore, leucine can be an important source of calories, and is superior as fuel to the ubiquitous intravenous glucose (dextrose). Leucine also stimulates insulin release, which in turn stimulates protein synthesis and inhibits protein breakdown. These effects are particularly useful in athletic training. BCAA should also replace the use of steroids as commonly used by weightlifters. Huntington's chorea and anorexic disorders both are characterized by low serum BCAA. These diseases, as well as forms of Parkinson's, may respond to BCAA therapy. BCAA, and particularly leucine, are among the amino acids most essential for muscle health. (http://www.dcnutrition.com)
Synonyms
  1. (2S)-2-Amino-4-methylpentanoate
  2. (2S)-2-Amino-4-methylpentanoic acid
  3. (S)-(+)-Leucine
  4. (S)-2-Amino-4-methylpentanoate
  5. (S)-2-Amino-4-methylpentanoic acid
  6. (S)-2-Amino-4-methylvalerate
  7. (S)-2-Amino-4-methylvaleric acid
  8. (S)-Leucine
  9. 4-methyl-L-Norvaline
  10. L-(+)-Leucine
  11. L-a-Aminoisocaproate
  12. L-a-Aminoisocaproic acid
  13. Leu
  14. L-alpha-Aminoisocaproate
  15. L-alpha-Aminoisocaproic acid
  16. Leucine
Chemical IUPAC Name (2S)-2-amino-4-methyl-pentanoic acid
Chemical Formula C6H13NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Essential amino acids
  • Protein component
Application
—
Source
  • Exogenous
Average Molecular Weight 131.173
Monoisotopic Molecular Weight 131.094635
Isomeric SMILES CC(C)C[C@H](N)C(O)=O
Canonical SMILES CC(C)CC(N)C(O)=O
KEGG Compound ID C00123 Link Image
BioCyc ID LEU Link Image
BiGG ID 33942 Link Image
Wikipedia Link Leucine Link Image
NuGOwiki Link HMDB00687 Link Image
Metagene Link HMDB00687 Link Image
METLIN ID 24 Link Image
PubChem Compound 6106 Link Image
PubChem Substance 832925 Link Image
ChEBI ID 15603 Link Image
CAS Registry Number 61-90-5
InChI Identifier InChI=1/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1
Synthesis Reference Leuchtenberger, Wolfgang; Karrenbauer, Michael; Ploecker, Ulf. Scale-up of an enzyme membrane reactor process for the manufacture of L-enantiomeric compounds. Annals of the New York Academy of Sciences (1984), 434(Enzyme Eng.), 78-86.
Melting Point (Experimental) 268-288
Experimental Water Solubility 21.5 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 69.8 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.52 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.82 [Predicted by ALOGPS]; -1.4 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1F2O Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Adrenal Medulla —
Bladder —
Epidermis —
Fibroblasts —
Intestine —
Kidney —
Muscle —
Nerve Cells —
Neuron —
Placenta —
Platelet —
Skeletal Muscle —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 123 (98-148) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 70.0 +/- 25.0 uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 134.0 +/- 20.0 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 160.0 +/- 27.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 157.0 +/- 30.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 93. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 251 +/- 5 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid CSF
Value 10.1 +/- 2.1 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 14.5 +/- 3.7 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 18.6 +/- 4.1 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 11.2 +/- 3.5 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 16 +/- 9 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 7.58 +/- 4.10 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 4.868 (1.842-8.421) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 0.1 (0.0-0.2) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 2.5 +/- 1.0 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 3.0+/- 1.5 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 2.5 +/- 1.3 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 3.5 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 95.3 (89.3-100.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Refractory localization-related epilepsy (RLE)
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 103.0 (97.8-108.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 643.0 +/- 667.0 uM
Age Newborn:0-30 days old
Sex Both
Condition Maple syrup urine disease
Comments Not Available
References
  • Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed Link Image]
Biofluid Blood
Value 273.0 +/- 10.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments Non-diabetic patients with chronic heart failure
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid Blood
Value 66.0 +/- 161.0 uM
Age Newborn:0-30 days old
Sex Both
Condition Phenylketonuria
Comments Not Available
References
  • Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed Link Image]
Biofluid CSF
Value 16.5 +/- 7.0 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Acute Lymphoblastic Leukemia (ALL) with Central Nervous System (CNS) disease
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 13.1 +/- 5.6 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 11.5 +/- 1.5 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 0.91 +/- 0.11 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Epilepsy
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Heart failure
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Maple syrup urine disease
  • Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed Link Image]
Phenylketonuria
  • Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Transcription/Translation SMP00019 Link Image
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed Link Image]
  2. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  3. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  4. Yoshimasa T, Nakao K, Ohtsuki H, Li S, Imura H: Methionine-enkephalin and leucine-enkephalin in human sympathoadrenal system and pheochromocytoma. J Clin Invest. 1982 Mar;69(3):643-50. [PubMed Link Image]
  5. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
  6. Jansson T, Scholtbach V, Powell TL: Placental transport of leucine and lysine is reduced in intrauterine growth restriction. Pediatr Res. 1998 Oct;44(4):532-7. [PubMed Link Image]
  7. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed Link Image]
  8. Lichtenstein AH, Hachey DL, Millar JS, Jenner JL, Booth L, Ordovas J, Schaefer EJ: Measurement of human apolipoprotein B-48 and B-100 kinetics in triglyceride-rich lipoproteins using [5,5,5-2H3]leucine. J Lipid Res. 1992 Jun;33(6):907-14. [PubMed Link Image]
  9. Mero A: Leucine supplementation and intensive training. Sports Med. 1999 Jun;27(6):347-58. [PubMed Link Image]
  10. Sakamoto M, Nakao K, Yoshimasa T, Ikeda Y, Suda M, Takasu K, Shimbo S, Yanaihara N, Imura H: Occurrence of methionine-enkephalin-Arg6-Gly7-Leu8 with methionine-enkephalin, leucine-enkephalin and methionine-enkephalin-Arg6-Phe7 in human gastric antrum. J Clin Endocrinol Metab. 1983 Jan;56(1):202-4. [PubMed Link Image]
  11. Yudkoff M, Daikhin Y, Nissim I, Horyn O, Luhovyy B, Lazarow A, Nissim I: Brain amino acid requirements and toxicity: the example of leucine. J Nutr. 2005 Jun;135(6 Suppl):1531S-8S. [PubMed Link Image]
  12. Iannoli P, Miller JH, Wang HT, Bode B, Souba WW, Avissar NE, Sax HC: Characterization of L-leucine transport system in brush border membranes from human and rabbit small intestine. Metabolism. 1999 Nov;48(11):1432-6. [PubMed Link Image]
  13. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Branched-chain-amino-acid aminotransferase, cytosolic
  2. Branched-chain-amino-acid aminotransferase, mitochondrial precursor
  3. Probable leucyl-tRNA synthetase, mitochondrial precursor
  4. Leucyl-tRNA synthetase, cytoplasmic
  5. Large neutral amino acids transporter small subunit 2
  6. 4F2 cell-surface antigen heavy chain
  7. Leucine carboxyl methyltransferase 2
  8. LARS protein (Leucyl-tRNA synthetase, isoform CRA_a) (Leucyl-tRNA synthetase)
  9. cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
  10. Leucine carboxyl methyltransferase 1
Enzyme 1 [top]
Enzyme 1 ID 5536
Enzyme 1 Name Branched-chain-amino-acid aminotransferase, cytosolic
Enzyme 1 Synonyms
  1. BCAT(c
  2. ECA39 protein
Enzyme 1 Gene Name BCAT1
Enzyme 1 Protein Sequence >Branched-chain-amino-acid aminotransferase, cytosolic 
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLSTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
Enzyme 1 Number of Residues 386
Enzyme 1 Molecular Weight 42953
Enzyme 1 Theoretical pI 4.95
Enzyme 1 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • branched chain family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine
Enzyme 1 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1036780 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P54687 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name BCAT1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1155 bp 
ATGGATTGCAGTAACGGATCGGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAGGTGGTG
GGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAAAAACCA
GACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTGGAGTGG
TCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCATTGCAC
CCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCATTTCGA
GGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATGTATCGC
TCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGTATTCAA
CAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTGTATATT
CGTCCTGCATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAAGCCCTG
CTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAATCCAGTG
TCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGACTGCAAG
ATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGACGTAGATAATGGGTGT
CAGCAGGTCCTGTGGCTCTATGGCAGAGACCATCAGATCACTGAAGTGGGAACTATGAAT
CTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCACTAGAT
GGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAGTGGGGT
GAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTGGAGGGG
AACAGAGTGAGAGAGATGTTTAGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTTTCTGAT
ATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAGCTGGCA
AGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGACTGGACA
ATTGTGCTATCCTGA
Enzyme 1 GenBank Gene ID U21551 Link Image
Enzyme 1 GeneCard ID BCAT1 Link Image
Enzyme 1 GenAtlas ID BCAT1 Link Image
Enzyme 1 HGNC ID HGNC:976 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12pter-q12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5763
Enzyme 2 Name Branched-chain-amino-acid aminotransferase, mitochondrial precursor
Enzyme 2 Synonyms
  1. BCAT(m
  2. Placental protein 18
  3. PP18
Enzyme 2 Gene Name BCAT2
Enzyme 2 Protein Sequence >Branched-chain-amino-acid aminotransferase, mitochondrial precursor 
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
Enzyme 2 Number of Residues 392
Enzyme 2 Molecular Weight 44288
Enzyme 2 Theoretical pI 8.82
Enzyme 2 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • branched chain family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids
Enzyme 2 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 2 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-29
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2342862 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O15382 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name BCAT2_HUMAN Link Image
Enzyme 2 PDB ID 1KTA Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1179 bp 
ATGGCCGCAGCCGCTCTGGGGCAGATCTGGGCACGAAAGCTTCTCTCTGTCCCTTGGCTT
CTGTGTGGTCCCAGAAGATATGCCTCCTCCAGTTTCAAGGCTGCAGACCTGCAGCTGGAA
ATGACACAGAAGCCTCATAAGAAGCCTGGCCCCGGCGAGCCCCTGGTGTTTGGGAAGACA
TTTACCGACCACATGCTGATGGTGGAATGGAATGACAAGGGCTGGGGCCAGCCCCGAATC
CAGCCCTTCCAGAACCTCACGCTGCACCCAGCCTCCTCCAGCCTCCACTACTCCCTGCAG
CTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGACCAGCAGGTGCGCCTCTTCCGCCCC
TGGCTCAACATGGACCGGATGCTGCGCTCAGCCATGCGCCTGTGCCTGCCGAGTTTCGAC
AAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATCGAAGTGGACAAGGACTGGGTCCCC
GATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTGCTCATTGGGAACGAGCCCTCGCTG
GGTGTCAGCCAGCCCAGGCGCGCGCTCCTGTTCGTCATTCTCTGCCCAGTGGGTGCCTAC
TTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTGGCCGACCCAGCCTTCATCCGGGCC
TGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGGAATTATGGGCCCACCGTGTTAGTG
CAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTCCTCTGGCTGTATGGGCCCGACCAC
CAGCTCACCGAGGTGGGAACCATGAACATCTTTGTCTACTGGACCCACGAAGATGGGGTG
CTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATCCTGCCTGGAGTGGTCAGACAGAGT
CTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGGGTGGTGGAGCGCACGATCACCATG
AAGCAGTTGCTGCGGGCCTTGGAGGAGGGCCGCGTGCGGGAAGTCTTTGGCTCGGGCACC
GCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTACAAAGACAGGAACCTCCATATTCCC
ACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTCCAGAAGGAGCTGAAGGAGATCCAG
TACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTGTGA
Enzyme 2 GenBank Gene ID U68418 Link Image
Enzyme 2 GeneCard ID BCAT2 Link Image
Enzyme 2 GenAtlas ID BCAT2 Link Image
Enzyme 2 HGNC ID HGNC:977 Link Image
Enzyme 2 Chromosome Location 19
Enzyme 2 Locus 19q13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [PubMed Link Image]
  2. Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [PubMed Link Image]
  3. Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [PubMed Link Image]
  4. Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [PubMed Link Image]
  5. Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5868
Enzyme 3 Name Probable leucyl-tRNA synthetase, mitochondrial precursor
Enzyme 3 Synonyms
  1. Leucine--tRNA ligase
  2. LeuRS
Enzyme 3 Gene Name LARS2
Enzyme 3 Protein Sequence >Probable leucyl-tRNA synthetase, mitochondrial precursor 
MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVE
KWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGM
QVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPD
YYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQ
WFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYT
ATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVI
LAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQ
DAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVT
LPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPH
SPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIK
GQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGID
TIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNK
EKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDA
LCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQ
MAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFL
VQD
Enzyme 3 Number of Residues 903
Enzyme 3 Molecular Weight 101977
Enzyme 3 Theoretical pI 8.32
Enzyme 3 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • leucine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • leucyl-tRNA aminoacylation
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
—
Enzyme 3 General Function Translation, ribosomal structure and biogenesis
Enzyme 3 Specific Function ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 40788954 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q15031 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SYLM_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2715 bp 
AGAATGGCTTCTGTTTGGCAGAGATTGGGTTTTTATGCCTCTCTTCTGAAAAGACAGCTA
AATGGTGGGCCAGATGTCATCAAGTGGGAAAGGAGAGTAATTCCCGGATGTACCAGAAGC
ATCTACAGTGCCACGGGAAAGTGGACAAAAGAGTATACATTGCAGACAAGAAAGGATGTT
GAGAAATGGTGGCATCAACGAATAAAAGAACAGGCCTCCAAAATTTCAGAAGCTGATAAA
TCGAAGCCAAAATTTTACGTGCTTTCCATGTTCCCTTATCCTTCTGGTAAGCTGCACATG
GGCCATGTGCGTGTCTACACCATCAGCGACACCATAGCACGGTTCCAGAAGATGAGAGGG
ATGCAGGTCATCAACCCCATGGGATGGGATGCTTTTGGATTGCCTGCTGAAAATGCCGCA
GTCGAGAGGAATCTACATCCACAAAGTTGGACACAAAGTAATATTAAACACATGAGGAAA
CAGCTTGATCGTCTGGGCCTGTGTTTCAGCTGGGATAGGGAAATAACTACGTGTTTGCCA
GATTACTACAAGTGGACTCAGTATCTCTTTATTAAACTGTATGAGGCTGGGCTGGCCTAT
CAAAAGGAGGCCCTGGTTAACTGGGACCCAGTGGATCAAACAGTGCTTGCCAATGAGCAG
GTGGATGAACATGGCTGTTCATGGCGTTCTGGAGCAAAGGTGGAACAGAAGTACCTCAGA
CAATGGTTTATTAAGACAACCGCTTATGCAAAGGCCATGCAGGACGCGTTGGCAGACCTT
CCAGAATGGTATGGAATAAAAGGCATGCAAGCCCACTGGATTGGGGACTGTGTGGGCTGC
CACCTGGACTTCACATTAAAGGTTCATGGGCAAGCCACGGGCGAAAAGCTGACTGCCTAT
ACGGCCACCCCTGAAGCCATTTATGGCACCTCCCACGTGGCCATCTCGCCCAGCCACAGA
CTCCTACATGGGCACAGCTCTCTGAAGGAAGCCTTGAGGATGGCCCTTGTCCCTGGCAAA
GATTGCCTCACGCCTGTAATGGCTGTGAACATGCTTACCCAGCAGGAGGTCCCTGTCGTT
ATTTTGGCCAAAGCTGACTTGGAAGGCTCTCTGGATTCAAAAATAGGAATTCCCAGTACT
AGCTCAGAGGACACCATCTTAGCCCAAACCCTGGGCCTGGCCTACTCTGAAGTCATTGAA
ACTTTGCCAGATGGCACAGAGAGACTGAGCAGCTCTGCTGAGTTCACAGGTATGACCCGG
CAGGATGCTTTTCTAGCCCTGACTCAGAAAGCCCGGGGGAAGAGAGTGGGTGGAGACGTG
ACAAGTGATAAACTGAAAGACTGGCTGATTTCACGGCAGCGGTACTGGGGCACACCAATC
CCCATTGTCCACTGCCCAGTCTGTGGCCCCACACCTGTGCCCCTGGAGGACTTGCCTGTG
ACCCTGCCCAACATCGCGTCTTTCACTGGCAAGGGAGGCCCCCCACTGGCCATGGCTTCA
GAGTGGGTGAACTGCTCCTGCCCAAGGTGCAAGGGAGCAGCCAAGAGAGAGACAGACACG
ATGGATACCTTTGTTGATTCTGCTTGGTACTACTTCAGATACACTGACCCTCATAATCCA
CACAGCCCTTTTAACACAGCAGTGGCCGATTACTGGATGCCTGTGGATTTGTACATTGGA
GGGAAAGAACATGCCGTCATGCACTTGTTCTATGCAAGATTCTTTAGTCATTTTTGCCAT
GATCAAAAAATGGTTAAACATAGGGAGCCTTTTCATAAGCTGCTGGCCCAAGGCCTTATC
AAGGGGCAGACATTCCGCCTACCATCTGGACAGTATCTACAGAGAGAGGAAGTGGATCTC
ACAGGTTCCGTTCCTGTTCATGCAAAAACGAAAGAGAAGTTAGAGGTGACGTGGGAGAAG
ATGAGTAAGTCCAAACACAACGGGGTGGACCCAGAGGAAGTTGTGGAGCAGTATGGGATC
GACACGATTCGGCTCTACATCCTTTTTGCTGCCCCTCCTGAGAAGGATATCTTGTGGGAT
GTGAAAACTGATGCTCTCCCTGGGGTGCTGAGATGGCAACAACGACTGTGGACCTTGACA
ACTCGGTTTATTGAGGCCAGGGCTTCTGGGAAGTCTCCCCAGCCTCAGCTGCTGAGTAAC
AAGGAGAAAGCTGAGGCCAGGAAGCTCTGGGAGTACAAGAACTCCGTCATCTCTCAGGTG
ACCACCCATTTCACAGAGGACTTCTCACTGAATTCTGCAATTTCTCAGCTGATGGGACTC
AGCAATGCCCTCTCGCAAGCCTCTCAGAGCGTCATTCTCCACAGCCCCGAGTTTGAGGAT
GCTTTGTGTGCCCTGATGGTAATGGCTGCTCCACTGGCCCCTCATGTAACCTCAGAGATC
TGGGCAGGCCTGGCGCTGGTGCCGAGGAAGCTCTGTGCCCACTACACTTGGGATGCCAGT
GTGCTGCTCCAGGCATGGCCTGCTGTGGACCCGGAGTTCCTGCAGCAGCCTGAGGTTGTC
CAGATGGCAGTTCTGATCAACAATAAAGCTTGTGGCAAAATTCCTGTGCCCCAACAAGTT
GCCCGGGACCAGGACAAAGTCCACGAATTTGTTCTTCAAAGCGAGCTGGGTGTCAGGCTT
TTGCAAGGACGAAGCATCAAGAAGTCCTTCCTTTCCCCGAGAACTGCCCTCATCAACTTC
CTGGTGCAAGATTGA
Enzyme 3 GenBank Gene ID D21851 Link Image
Enzyme 3 GeneCard ID LARS2 Link Image
Enzyme 3 GenAtlas ID LARS2 Link Image
Enzyme 3 HGNC ID HGNC:17095 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5920
Enzyme 4 Name Leucyl-tRNA synthetase, cytoplasmic
Enzyme 4 Synonyms
  1. Leucine--tRNA ligase
  2. LeuRS
Enzyme 4 Gene Name LARS
Enzyme 4 Protein Sequence >Leucyl-tRNA synthetase, cytoplasmic 
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLH
LGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDE
EEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHW
LDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIY
SPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMF
GQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGA
SLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRD
DMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVD
GFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWK
KQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIY
MAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQ
EFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKS
TGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVAN
WDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAV
EGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQ
YLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFE
ANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVL
MENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGH
FSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTP
ISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
Enzyme 4 Number of Residues 1176
Enzyme 4 Molecular Weight 134468
Enzyme 4 Theoretical pI 7.31
Enzyme 4 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • leucine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • protein biosynthesis
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 4 General Function Translation, ribosomal structure and biogenesis
Enzyme 4 Specific Function ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 7804450 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9P2J5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SYLC_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3531 bp 
ATGGCGGAAAGAAAAGGAACAGCCAAAGTGGACTTTTTGAAGAAGATTGAGAAAGAAATC
CAACAGAAATGGGATACTGAGAGAGTGTTTGAGGTCAATGCATCTAATTTAGAGAAACAG
ACCAGCAAGGGCAAGTATTTTGTAACCTTCCCATATCCATATATGAATGGACGCCTTCAT
TTGGGACACACGTTTTCTTTATCCAAATGTGAGTTTGCTGTAGGGTACCAGCGATTGAAA
GGAAAATGTTGTCTGTTTCCCTTTGGCCTGCACTGTACTGGAATGCCTATTAAGGCATGT
GCTGATAAGTTGAAAAGAGAAATAGAGCTGTATGGTTGCCCCCCTGATTTTCCAGATGAA
GAAGAGGAAGAGGAAGAAACCAGTGTTAAAACAGAAGATATAATAATTAAGGATAAAGCT
AAAGGAAAAAAGAGTAAAGCTGCTGCTAAAGCTGGATCTTCTAAATACCAGTGGGGCATT
ATGAAATCCCTTGGCCTGTCTGATGAAGAGATAGTAAAATTTTCTGAAGCAGAACATTGG
CTTGATTATTTCCCGCCACTGGCTATTCAGGATTTAAAAAGAATGGGTTTGAAGGTAGAC
TGGCGTCGTTCCTTCATCACCACTGATGTTAATCCTTACTATGATTCATTTGTCAGATGG
CAATTTTTAACATTAAGAGAAAGAAACAAAATTAAATTTGGGAAGCGGTATACAATTTAC
TCTCCGAAAGATGGACAGCCTTGCATGGATCATGATAGACAAACTGGAGAGGGTGTTGGA
CCTCAGGAATATACTTTACTCAAATTGAAGGCGCTTGAGCCATACCCATCTAAATTAAGT
GGCCTGAAAGGTAAAAATATTTTCTTGGTGGCTGCTACTCTCAGACCTGAGACCATGTTT
GGGCAGACAAATTGTTGGGTTCGTCCTGATATGAAGTACATTGGATTTGAGACGGTGAAT
GGTGATATATTCATCTGTACCCAAAAAGCAGCCAGGAATATGTCATACCAGGGCTTTACC
AAAGACAATGGCGTGGTGCCTGTTGTTAAGGAATTAATGGGGGAGGAAATTCTTGGTGCA
TCACTTTCTGCACCTTTAACATCATACAAGGTGATCTATGTTCTCCCAATGCTAACTATT
AAGGAGGATAAAGGCACTGGTGTGGTTACAAGTGTTCCTTCCGACTCCCCTGATGATATT
GCTGCCCTCAGAGACTTGAAGAAAAAGCAAGCCTTACGAGCAAAATATGGAATTAGAGAT
GACATGGTCTTGCCATTTGAGCCGGTGCCAGTCATTGAAATCCCAGGTTTTGGAAATCTT
TCTGCTGTAACCATTTGTGATGAGTTGAAAATTCAGAGCCAGAATGACCGGGAAAAACTT
GCAGAAGCAAAGGAGAAGATATATCTAAAAGGATTTTATGAGGGTATCATGTTGGTGGAT
GGATTTAAAGGACAGAAGGTTCAAGATGTAAAGAAGACTATTCAGAAAAAGATGATTGAC
GCTGGAGATGCACTTATTTACATGGAACCAGAGAAACAAGTGATGTCCAGGTCGTCAGAT
GAATGTGTTGTGGCTCTGTGTGACCAGTGGTACTTGGATTATGGAGAAGAGAATTGGAAG
AAACAGACATCTCAGTGCTTGAAGAACCTGGAAACATTCTGTGAGGAGACCAGGAGGAAT
TTTGAAGCCACCTTAGGTTGGCTACAAGAACATGCTTGCTCAAGAACTTATGGTCTAGGC
ACTCACCTGCCTTGGGATGAGCAGTGGCTGATTGAATCACTTTCTGACTCCACTATTTAC
ATGGCATTTTACACAGTTGCACACCTATTGCAGGGGGGTAACTTGCATGGACAGGCAGAG
TCTCCGCTGGGCATTAGACCGCAACAGATGACCAAGGAAGTTTGGGATTATGTTTTCTTC
AAGGAGGCTCCATTTCCTAAGACTCAGATTGCAAAGGAAAAATTAGATCAGTTAAAGCAG
GAGTTTGAATTCTGGTATCCTGTTGATCTTCGCGTCTCTGGCAAGGATCTTGTTCCAAAT
CATCTTTCATATTACCTTTATAATCATGTGGCTATGTGGCCGGAACAAAGTGATAAATGG
CCTACAGCTGTGAGAGCAAATGGACATCTCCTCCTGAACTCTGAGAAGATGTCAAAATCC
ACAGGCAACTTCCTCACTTTGACCCAAGCTATTGACAAATTTTCAGCAGATGGAATGCGT
TTGGCTCTGGCTGATGCTGGTGACACTGTAGAAGATGCCAACTTTGTGGAAGCCATGGCA
GATGCAGGTATTCTCCGTCTGTACACCTGGGTAGAGTGGGTGAAAGAAATGGTTGCCAAC
TGGGACAGCCTAAGAAGTGGTCCTGCCAGCACTTTCAATGATAGAGTTTTTGCCAGTGAA
TTGAATGCAGGAATTATAAAAACAGATCAAAACTATGAAAAGATGATGTTTAAAGAAGCT
TTGAAAACAGGGTTTTTTGAGTTTCAGGCCGCAAAAGATAAGTACCGTGAATTGGCTGTG
GAAGGGATGCACAGAGAACTTGTGTTCCGGTTTATTGAAGTTCAGACACTTCTCCTCGCT
CCATTCTGTCCACATTTGTGTGAGCACATCTGGACACTCCTGGGAAAGCCTGACTCAATT
ATGAATGCTTCATGGCCTGTGGCAGGTCCTGTGGATGAAGTTTTAATACACTCCTCACAG
TATCTTATGGAAGTAACACATGACCTTAGACTACGACTCAAGAACTATATGATGCCAGCT
AAAGGGAAGAAGACCGACAAACAACCCCTGCAGAAGCCCTCACATTGCACCATCTATGTG
GCAAAGAACTATCCACCTTGGCAACATACCACCCTGTCTGTTCTACGTAAACACTTTGAG
GCCAATAACGGAAAACTGCCTGACAACAAAGTCATTGCTAGTGAACTAGGCAGTATGCCA
GAACTGAAGAAATACATGAAGAAAGTCATGCCATTTGTTGCCATGATTAAGGAAAATCTG
GAGAAGATGGGGCCTCGTATTCTGGATTTGCAATTAGAATTTGATGAAAAGGCTGTGCTT
ATGGAGAATATAGTCTATCTGACTAATTCGCTTGAGCTAGAACACATAGAAGTCAAGTTT
GCCTCCGAAGCAGAAGATAAAATCAGGGAAGACTGCTGTCCTGGGAAACCACTTAATGTT
TTTAGAATAGAACCTGGTGTGTCCGTTTCTCTGGTGAATCCCCAGCCATCCAATGGCCAC
TTCTCAACCAAAATTGAAATCAAGCAAGGAGATAACTGTGATTCCATAATCAGGCGTTTA
ATGAAAATGAATCGAGGAATTAAAGACCTTTCCAAAGTGAAACTGATGAGATTTGATGAT
CCACTGTTGGGGCCTCGACGAGTTCCTGTCCTGGGAAAGGAGTACACCGAGAAGACCCCC
ATTTCTGAGCATGCTGTTTTCAATGTGGACCTCATGAGCAAGAAAATTCATCTGACTGAG
AATGGGATAAGGGTGGATATTGGCGATACAATAATCTATCTGGTTCATTAA
Enzyme 4 GenBank Gene ID D84223 Link Image
Enzyme 4 GeneCard ID LARS Link Image
Enzyme 4 GenAtlas ID LARS Link Image
Enzyme 4 HGNC ID HGNC:6512 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5q32
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7884
Enzyme 5 Name Large neutral amino acids transporter small subunit 2
Enzyme 5 Synonyms
  1. L-type amino acid transporter 2
  2. hLAT2
Enzyme 5 Gene Name SLC7A8
Enzyme 5 Protein Sequence >Large neutral amino acids transporter small subunit 2 
MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP
Enzyme 5 Number of Residues 535
Enzyme 5 Molecular Weight 58382
Enzyme 5 Theoretical pI 5.75
Enzyme 5 GO Classification
Function
  • amine transporter activity
  • amino acid permease activity
  • amino acid transporter activity
  • amino acid-polyamine transporter activity
  • transporter activity
Process
  • amine transport
  • amino acid transport
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function Sodium-independent, high-affinity transport of large neutral amino acids. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 40-60 72-92 113-133 155-175 189-209 231-251 268-288 310-330 362-382 388-408 424-444 447-467
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 6642960 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9UHI5 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name LAT2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1608 bp 
ATGGAAGAAGGAGCCAGGCACCGAAACAACACCGAAAAGAAACACCCAGGTGGGGGCGAG
TCGGACGCCAGCCCCGAGGCTGGTTCCGGAGGGGGCGGAGTAGCCCTGAAGAAAGAGATC
GGATTGGTCAGTGCCTGTGGTATCATCGTAGGGAACATCATCGGCTCTGGAATCTTTGTC
TCGCCAAAGGGAGTGCTGGAGAATGCTGGTTCTGTGGGCCTTGCTCTCATCGTCTGGATT
GTGACGGGCTTCATCACAGTTGTGGGAGCCCTCTGCTATGCTGAACTCGGGGTCACCATC
CCCAAATCTGGAGGTGACTACTCCTATGTCAAGGACATCTTCGGAGGACTGGCTGGGTTC
CTGAGGCTGTGGATTGCTGTGCTGGTGATCTACCCCACCAACCAGGCTGTCATCGCCCTC
ACCTTCTCCAACTACGTGCTGCAGCCGCTCTTCCCCACCTGCTTCCCCCCAGAGTCTGGC
CTTCGGCTCCTGGCTGCCATCTGCTTATTGCTCCTCACATGGGTCAACTGTTCCAGTGTG
CGGTGGGCCACCCGGGTTCAAGACATCTTCACAGCTGGGAAGCTCCTGGCCTTGGCCCTG
ATTATCATCATGGGGATTGTACAGATATGCAAAGGAGAGTACTTCTGGCTGGAGCCAAAG
AATGCATTTGAGAATTTCCAGGAACCTGACATCGGCCTCGTCGCACTGGCTTTCCTTCAG
GGCTCCTTTGCCTATGGAGGCTGGAACTTTCTGAATTACGTGACTGAGGAGCTTGTTGAT
CCCTACAAGAACCTTCCCAGAGCCATCTTCATCTCCATCCCACTGGTCACATTTGTGTAT
GTCTTTGCCAATGTCGCTTATGTCACTGCAATGTCCCCCCAGGAGCTGCTGGCATCCAAC
GCCGTCGCTGTGACTTTTGGAGAGAAGCTCCTAGGAGTCATGGCCTGGATCATGCCCATT
TCTGTTGCCCTGTCCACATTTGGAGGAGTTAATGGGTCTCTCTTCACCTCCTCTCGGCTG
TTCTTCGCTGGAGCCCGAGAGGGCCACCTTCCCAGTGTGTTGGCCATGATCCACGTGAAG
CGCTGCACCCCAATCCCAGCCCTGCTCTTCACATGCATCTCCACCCTGCTGATGCTGGTC
ACCAGCGACATGTACACACTCATCAACTACGTGGGCTTCATCAACTACCTCTTCTATGGG
GTCACGGTTGCTGGACAGATAGTCCTTCGCTGGAAGAAGCCTGATATCCCCCGCCCCATC
AAGATCAACCTGCTGTTCCCCATCATCTACTTGCTGTTCTGGGCCTTCCTGCTGGTCTTC
AGCCTGTGGTCAGAGCCGGTGGTGTGTGGCATTGGCCTGGCCATCATGCTGACAGGAGTG
CCTGTCTATTTCCTGGGTGTTTACTGGCAACACAAGCCCAAGTGTTTCAGTGACTTCATT
GAGCTGCTAACCCTGGTGAGCCAGAAGATGTGTGTGGTCGTGTACCCCGAGGTGGAGCGG
GGCTCAGGGACAGAGGAGGCTAATGAGGACATGGAGGAGCAGCAGCAGCCCATGTACCAA
CCCACTCCCACGAAGGACAAGGACGTGGCGGGGCAGCCCCAGCCCTGA
Enzyme 5 GenBank Gene ID AF171669 Link Image
Enzyme 5 GeneCard ID SLC7A8 Link Image
Enzyme 5 GenAtlas ID SLC7A8 Link Image
Enzyme 5 HGNC ID HGNC:11066 Link Image
Enzyme 5 Chromosome Location 14
Enzyme 5 Locus 14q11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Rossier G, Meier C, Bauch C, Summa V, Sordat B, Verrey F, Kuhn LC: LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J Biol Chem. 1999 Dec 3;274(49):34948-54. [PubMed Link Image]
  2. Borsani G, Bassi MT, Sperandeo MP, De Grandi A, Buoninconti A, Riboni M, Manzoni M, Incerti B, Pepe A, Andria G, Ballabio A, Sebastio G: SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance. Nat Genet. 1999 Mar;21(3):297-301. [PubMed Link Image]
  3. Pineda M, Fernandez E, Torrents D, Estevez R, Lopez C, Camps M, Lloberas J, Zorzano A, Palacin M: Identification of a membrane protein, LAT-2, that Co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids. J Biol Chem. 1999 Jul 9;274(28):19738-44. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 8627
Enzyme 6 Name 4F2 cell-surface antigen heavy chain
Enzyme 6 Synonyms
  1. 4F2hc
  2. Lymphocyte activation antigen 4F2 large subunit
  3. 4F2 heavy chain antigen
  4. CD98 antigen
Enzyme 6 Gene Name SLC3A2
Enzyme 6 Protein Sequence >4F2 cell-surface antigen heavy chain 
MSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKF
TGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHT
GALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQID
PNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAG
VDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLT
SSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLP
GTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLS
LFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQAS
DLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
Enzyme 6 Number of Residues 529
Enzyme 6 Molecular Weight 57945
Enzyme 6 Theoretical pI 4.99
Enzyme 6 GO Classification
Function
  • alpha-amylase activity
  • amylase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function Involved in sodium-independent, high-affinity transport of large neutral amino acids. Required for normal and neoplastic cell growth
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-98
Enzyme 6 Transmembrane Regions
  • 82-104
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 182865 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P08195 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name 4F2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1590 bp 
ATGAGCCAGGACACCGAGGTGGATATGAAGGAGGTGGAGCTGAATGAGTTAGAGCCCGAG
AAGCAGCCGATGAACGCGGCGTCTGGGGCGGCCATGTCCCTGGCGGGAGCCGAGAAGAAT
GGTCTGGTGAAGATCAAGGTGGCGGAAGACGAGGCGGAGGCGGCAGCCGCGGCTAAGTTC
ACGGGCCTGTCCAAGGAGGAGCTGCTGAAGGTGGCAGGCAGCCCCGGCTGGGTACGCACC
CGCTGGGCACTGCTGCTGCTCTTCTGGCTCGGCTGGCTCGGCATGCTTGCTGGTGCCGTG
GTCATAATCGTGCGAGCGCCGCGTTGTCGCGAGCTACCGGCGCAGAAGTGGTGGCACACG
GGCGCCCTCTACCGCATCGGCGACCTTCAGGCCTTCCAGGGCCACGGCGCGGGCAACCTG
GCGGGTCTGAAGGGGCGTCTCGATTACCTGAGCTCTCTGAAGGTGAAGGGCCTTGTGCTG
GGTCCAATTCACAAGAACCAGAAGGATGATGTCGCTCAGACTGACTTGCTGCAGATCGAC
CCCAATTTTGGCTCCAAGGAAGATTTTGACAGTCTCTTGCAATCGGCTAAAAAAAAGAGC
ATCCGTGTCATTCTGGACCTTACTCCCAACTACCGGGGTGAGAACTCGTGGTTCTCCACT
CAGGTTGACACTGTGGCCACCAAGGTGAAGGATGCTCTGGAGTTTTGGCTGCAAGCTGGC
GTGGATGGGTTCCAGGTTCGGGACATAGAGAATCTGAAGGATGCATCCTCATTCTTGGCT
GAGTGGCAAAATATCACCAAGGGCTTCAGTGAAGACAGGCTCTTGATTGCGGGGACTAAC
TCCTCCGACCTTCAGCAGATCCTGAGCCTACTCGAATCCAACAAAGACTTGCTGTTGACT
AGCTCATACCTGTCTGATTCTGGTTCTACTGGGGAGCATACAAAATCCCTAGTCACACAG
TATTTGAATGCCACTGGCAATCGCTGGTGCAGCTGGAGTTTGTCTCAGGCAAGGCTCCTG
ACTTCCTTCTTGCCGGCTCAACTTCTCCGACTCTACCAGCTGATGCTCTTCACCCTGCCA
GGGACCCCTGTTTTCAGCTACGGGGATGAGATTGGCCTGGATGCAGCTGCCCTTCCTGGA
CAGCCTATGGAGGCTCCAGTCATGCTGTGGGATGAGTCCAGCTTCCCTGACATCCCAGGG
GCTGTAAGTGCCAACATGACTGTGAAGGGCCAGAGTGAAGACCCTGGCTCCCTCCTTTCC
TTGTTCCGGCGGCTGAGTGACCAGCGGAGTAAGGAGCGCTCCCTACTGCATGGGGACTTC
CACGCGTTCTCCGCTGGGCCTGGACTCTTCTCCTATATCCGCCACTGGGACCAGAATGAG
CGTTTTCTGGTAGTGCTTAACTTTGGGGATGTGGGCCTCTCGGCTGGACTGCAGGCCTCC
GACCTGCCTGCCAGCGCCAGCCTCCCAGCCAAGGCTGACCTCCTGCTCAGCACCCAGCCA
GGCCGTGAGGAGGGCTCCCCTCTTGAGCTGGAACGCCTGAAACTGGAGCCTCACGAAGGG
CTGCTGCTCCGCTTCCCCTACGCGGCCTGA
Enzyme 6 GenBank Gene ID J02939 Link Image
Enzyme 6 GeneCard ID SLC3A2 Link Image
Enzyme 6 GenAtlas ID SLC3A2 Link Image
Enzyme 6 HGNC ID HGNC:11026 Link Image
Enzyme 6 Chromosome Location 11
Enzyme 6 Locus 11q13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Quackenbush E, Clabby M, Gottesdiener KM, Barbosa J, Jones NH, Strominger JL, Speck S, Leiden JM: Molecular cloning of complementary DNAs encoding the heavy chain of the human 4F2 cell-surface antigen: a type II membrane glycoprotein involved in normal and neoplastic cell growth. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6526-30. [PubMed Link Image]
  2. Teixeira S, Di Grandi S, Kuhn LC: Primary structure of the human 4F2 antigen heavy chain predicts a transmembrane protein with a cytoplasmic NH2 terminus. J Biol Chem. 1987 Jul 15;262(20):9574-80. [PubMed Link Image]
  3. Lumadue JA, Glick AB, Ruddle FH: Cloning, sequence analysis, and expression of the large subunit of the human lymphocyte activation antigen 4F2. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9204-8. [PubMed Link Image]
  4. Gottesdiener KM, Karpinski BA, Lindsten T, Strominger JL, Jones NH, Thompson CB, Leiden JM: Isolation and structural characterization of the human 4F2 heavy-chain gene, an inducible gene involved in T-lymphocyte activation. Mol Cell Biol. 1988 Sep;8(9):3809-19. [PubMed Link Image]
  5. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  6. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed Link Image]
  7. He X, Di Y, Li J, Xie Y, Tang Y, Zhang F, Wei L, Zhang Y, Qin W, Huo K, Li Y, Wan D, Gu J: Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism. Biochem Biophys Res Commun. 2002 Sep 27;297(3):528-36. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 14756
Enzyme 7 Name Leucine carboxyl methyltransferase 2
Enzyme 7 Synonyms
  1. p21WAF1/CIP1 promoter-interacting protein
  2. tRNA wybutosine-synthesizing protein 4 homolog
Enzyme 7 Gene Name LCMT2
Enzyme 7 Protein Sequence >Leucine carboxyl methyltransferase 2 
MGPRSRERRAGAVQNTNDSSALSKRSLAARGYVQDPFAALLVPGAARRAPLIHRGYYVRA
RAVRHCVRAFLEQIGAPQAALRAQILSLGAGFDSLYFRLKTAGRLARAAVWEVDFPDVAR
RKAERIGETPELCALTGPFERGEPASALCFESADYCILGLDLRQLQRVEEALGAAGLDAA
SPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRPQDAFGQFMLQHFRQLNS
PLHGLERFPDVEAQRRRFLQAGWTACGAVDMNEFYHCFLPAEERRRVENIEPFDEFEEWH
LKCAHYFILAASRGDTLSHTLVFPSSEAFPRVNPASPSGVFPASVVSSEGQVPNLKRYGH
ASVFLSPDVILSAGGFGEQEGRHCRVSQFHLLSRDCDSEWKGSQIGSCGTGVQWDGRLYH
TMTRLSESRVLVLGGRLSPVSPALGVLQLHFFKSEDNNTEDLKVTITKAGRKDDSTLCCW
RHSTTEVSCQNQEYLFVYGGRSVVEPVLSDWHFLHVGTMAWVRIPVEGEVPEARHSHSAC
TWQGGALIAGGLGASEEPLNSVLFLRPISCGFLWESVDIQPPITPRYSHTAHVLNGKLLL
VGGIWIHSSSFPGVTVINLTTGLSSEYQIDTTYVPWPLMLHNHTSILLPEEQQLLLLGGG
GNCFSFGTYFNPHTVTLDLSSLSAGQ
Enzyme 7 Number of Residues 686
Enzyme 7 Molecular Weight 75603
Enzyme 7 Theoretical pI 6.71
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha- leucine ester residues
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 40788285 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O60294 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name LCMT2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2091 bp 
CAGACTGCCATTCCTGAGTCTCTTCTGGCCATGGGCCCCCGGAGCCGTGAGCGTCGGGCA
GGCGCGGTACAGAACACCAACGACAGCAGCGCCCTCAGCAAGCGTTCCCTGGCCGCGCGC
GGGTACGTGCAGGACCCCTTTGCCGCGTTGCTGGTTCCGGGCGCGGCGCGCCGCGCACCG
CTCATTCACCGAGGCTACTACGTCCGCGCACGCGCCGTGAGGCACTGCGTGCGCGCTTTT
TTGGAGCAGATTGGCGCGCCCCAGGCCGCGCTTCGCGCGCAGATCTTGTCTCTCGGCGCT
GGCTTCGACTCGCTCTATTTTCGCTTAAAAACCGCGGGCCGCCTGGCCCGGGCTGCAGTC
TGGGAGGTGGATTTTCCGGACGTGGCGCGGCGCAAAGCAGAAAGGATTGGAGAGACGCCA
GAGCTGTGCGCGTTAACCGGGCCTTTCGAGAGGGGGGAGCCCGCGTCCGCGCTGTGCTTT
GAGAGCGCAGACTACTGCATCCTGGGTCTGGACTTGCGGCAGCTCCAGCGAGTGGAGGAG
GCCCTGGGCGCCGCGGGGCTCGACGCAGCCTCACCCACTCTGCTCCTGGCCGAGGCGGTG
CTGACCTACCTCGAGCCGGAGAGTGCCGCGGCCCTCATCGCCTGGGCAGCCCAGCGTTTT
CCTAATGCCCTTTTCGTGGTCTATGAGCAGATGAGGCCTCAAGACGCCTTTGGCCAGTTC
ATGCTGCAACATTTTCGGCAGCTAAACTCCCCCCTGCATGGCCTGGAGCGTTTTCCTGAC
GTGGAGGCGCAGCGGCGCCGCTTCCTTCAAGCTGGCTGGACCGCCTGCGGTGCCGTGGAC
ATAAATGAATTCTATCACTGCTTTCTTCCCGCAGAAGAACGCCGGCGGGTGGAAAATATT
GAACCCTTTGACGAATTTGAGGAGTGGCATCTGAAGTGCGCCCATTATTTCATTCTGGCA
GCTTCTAGGGGAGACACCCTCTCCCACACCCTAGTGTTTCCATCCTCAGAGGCATTTCCT
CGCGTAAATCCTGCTTCGCCTTCAGGGGTATTCCCTGCCAGCGTAGTCAGTAGCGAGGGC
CAGGTCCCAAACCTGAAGAGATATGGCCACGCCTCTGTCTTCTTGAGCCCAGACGTTATT
CTCAGTGCAGGAGGATTTGGAGAGCAGGAGGGGCGGCACTGCCGAGTGAGCCAGTTTCAC
TTGCTCTCAAGAGATTGTGACTCTGAATGGAAAGGCAGCCAAATAGGCAGTTGTGGGACT
GGAGTTCAGTGGGATGGACGCCTTTATCACACCATGACAAGACTCTCAGAGAGTCGGGTT
CTGGTTCTGGGAGGGAGACTGTCCCCAGTAAGTCCAGCCTTGGGGGTTCTCCAGCTTCAT
TTTTTTAAGAGTGAGGATAATAACACTGAGGACCTGAAAGTGACAATAACAAAGGCTGGC
CGAAAGGATGATTCCACTTTGTGTTGTTGGCGGCATTCAACAACAGAAGTGTCCTGTCAG
AATCAGGAATATTTGTTTGTGTATGGGGGTCGAAGCGTGGTGGAACCTGTACTAAGTGAC
TGGCATTTCCTCCATGTAGGGACAATGGCTTGGGTCAGGATCCCAGTGGAGGGAGAAGTA
CCTGAAGCCCGGCATTCTCACAGTGCCTGCACTTGGCAAGGGGGAGCCCTTATTGCTGGA
GGTCTCGGGGCTTCTGAGGAGCCATTGAACTCTGTGCTCTTTCTGAGACCAATCTCTTGT
GGATTCCTCTGGGAGTCAGTAGACATCCAGCCTCCCATTACCCCAAGGTACTCCCACACA
GCTCATGTGCTCAATGGAAAGCTGTTACTGGTTGGAGGGATCTGGATTCATTCCTCCTCA
TTTCCTGGAGTGACTGTGATCAATTTGACTACAGGATTGAGCTCTGAGTATCAGATTGAC
ACAACATATGTGCCATGGCCATTAATGTTACACAACCATACTAGTATCCTTCTTCCTGAA
GAGCAACAGCTCCTGCTCCTTGGAGGTGGTGGGAACTGCTTTTCCTTTGGTACCTACTTC
AACCCCCATACAGTCACATTAGACCTTTCTTCCTTAAGTGCTGGGCAGTAA
Enzyme 7 GenBank Gene ID AB011119 Link Image
Enzyme 7 GeneCard ID O60294 Link Image
Enzyme 7 GenAtlas ID LCMT2 Link Image
Enzyme 7 HGNC ID HGNC:17558 Link Image
Enzyme 7 Chromosome Location 15
Enzyme 7 Locus 15q15.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  2. De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J: Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. [PubMed Link Image]
  3. Ng CC, Arakawa H, Fukuda S, Kondoh H, Nakamura Y: p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1. Oncogene. 2003 Jul 10;22(28):4449-58. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 15076
Enzyme 8 Name LARS protein (Leucyl-tRNA synthetase, isoform CRA_a) (Leucyl-tRNA synthetase)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name LARS
Enzyme 8 Protein Sequence >LARS protein (Leucyl-tRNA synthetase, isoform CRA_a) (Leucyl-tRNA synthetase) 
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLH
LGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDE
EEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHW
LDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIY
SPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMF
GQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGA
SLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRD
DMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVD
GFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWK
KQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIY
MAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQ
EFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKS
TGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVAN
WDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAV
EGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQ
YLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFE
ANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVL
MENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGH
FSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTP
ISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
Enzyme 8 Number of Residues 1176
Enzyme 8 Molecular Weight 134468
Enzyme 8 Theoretical pI 7.31
Enzyme 8 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • leucine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • protein biosynthesis
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 8 General Function Translation, ribosomal structure and biogenesis
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 152013023 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A7E266 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A7E266_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >3531 bp 
ATGGCGGAAAGAAAAGGAACAGCCAAAGTGGACTTTTTGAAGAAGATTGAGAAAGAAATC
CAACAGAAATGGGATACTGAGAGAGTGTTTGAGGTCAATGCATCTAATTTAGAGAAACAG
ACCAGCAAGGGCAAGTATTTTGTAACCTTCCCATATCCATATATGAATGGACGCCTTCAT
TTGGGACACACGTTTTCTTTATCCAAATGTGAGTTTGCTGTAGGGTACCAGCGATTGAAA
GGAAAATGTTGTCTGTTTCCCTTTGGCCTGCACTGTACTGGAATGCCTATTAAGGCATGT
GCTGATAAGTTGAAAAGAGAAATAGAGCTGTATGGTTGCCCCCCTGATTTTCCAGATGAA
GAAGAGGAAGAGGAAGAAACCAGTGTTAAAACAGAAGATATAATAATTAAGGATAAAGCT
AAAGGAAAAAAGAGTAAAGCTGCTGCTAAAGCTGGATCTTCTAAATACCAGTGGGGCATT
ATGAAATCCCTTGGCCTGTCTGATGAAGAGATAGTAAAATTTTCTGAAGCAGAACATTGG
CTTGATTATTTCCCGCCACTGGCTATTCAGGATTTAAAAAGAATGGGTTTGAAGGTAGAC
TGGCGTCGTTCCTTCATCACCACTGATGTTAATCCTTACTATGATTCATTTGTCAGATGG
CAATTTTTAACATTAAGAGAAAGAAACAAAATTAAATTTGGGAAGCGGTATACAATTTAC
TCTCCGAAAGATGGACAGCCTTGCATGGATCATGATAGACAAACTGGAGAGGGTGTTGGA
CCTCAGGAATATACTTTACTCAAATTGAAGGTGCTTGAGCCATACCCATCTAAATTAAGT
GGCCTGAAAGGTAAAAATATTTTCTTGGTGGCTGCTACTCTCAGACCTGAGACCATGTTT
GGGCAGACAAATTGTTGGGTTCGTCCTGATATGAAGTACATTGGATTTGAGACGGTGAAT
GGTGATATATTCATCTGTACCCAAAAAGCAGCCAGGAATATGTCATACCAGGGCTTTACC
AAAGACAATGGCGTGGTGCCTGTTGTTAAGGAATTAATGGGGGAGGAAATTCTTGGTGCA
TCACTTTCTGCACCTTTAACATCATACAAGGTGATCTATGTTCTCCCAATGCTAACTATT
AAGGAGGATAAAGGCACTGGTGTGGTTACAAGTGTTCCTTCCGACTCCCCTGATGATATT
GCTGCCCTCAGAGACTTGAAGAAAAAGCAAGCCTTACGAGCAAAATATGGAATTAGAGAT
GACATGGTCTTGCCATTTGAGCCGGTGCCAGTCATTGAAATCCCAGGTTTTGGAAATCTT
TCTGCTGTAACCATTTGTGATGAGTTGAAAATTCAGAGCCAGAATGACCGGGAAAAACTT
GCAGAAGCAAAGGAGAAGATATATCTAAAAGGATTTTATGAGGGTATCATGTTGGTGGAT
GGATTTAAAGGACAGAAGGTTCAAGATGTAAAGAAGACTATTCAGAAAAAGATGATTGAC
GCTGGAGATGCACTTATTTACATGGAACCAGAGAAACAAGTGATGTCCAGGTCGTCAGAT
GAATGTGTTGTGGCTCTGTGTGACCAGTGGTACTTGGATTATGGAGAAGAGAATTGGAAG
AAACAGACATCTCAGTGCTTGAAGAACCTGGAAACATTCTGTGAGGAGACCAGGAGGAAT
TTTGAAGCCACCTTAGGTTGGCTACAAGAACATGCTTGCTCAAGAACTTATGGTCTAGGC
ACTCACCTGCCTTGGGATGAGCAGTGGCTGATTGAATCACTTTCTGACTCCACTATTTAC
ATGGCATTTTACACAGTTGCACACCTATTGCAGGGGGGTAACTTGCATGGACAGGCAGAG
TCTCCGCTGGGCATTAGACCGCAACAGATGACCAAGGAAGTTTGGGATTATGTTTTCTTC
AAGGAGGCTCCATTTCCTAAGACTCAGATTGCAAAGGAAAAATTAGATCAGTTAAAGCAG
GAGTTTGAATTCTGGTATCCTGTTGATCTTCGCGTCTCTGGCAAGGATCTTGTTCCAAAT
CATCTTTCATATTACCTTTATAATCATGTGGCTATGTGGCCGGAACAAAGTGACAAATGG
CCTACAGCTGTGAGAGCAAATGGACATCTCCTCCTGAACTCTGAGAAGATGTCAAAATCC
ACAGGCAACTTCCTCACTTTGACCCAAGCTATTGACAAATTTTCAGCAGATGGAATGCGT
TTGGCTCTGGCTGATGCTGGTGACACTGTAGAAGATGCCAACTTTGTGGAAGCCATGGCA
GATGCAGGTATTCTCCGTCTGTACACCTGGGTAGAGTGGGTGAAAGAAATGGTTGCCAAC
TGGGACAGCCTAAGAAGTGGTCCTGCCAGCACTTTCAATGATAGAGTTTTTGCCAGTGAA
TTGAATGCAGGAATTATAAAAACAGATCAAAACTATGAAAAGATGATGTTTAAAGAAGCT
TTGAAAACAGGGTTTTTTGAGTTTCAGGCCGCAAAAGATAAGTACCGTGAATTGGCTGTG
GAAGGGATGCACAGAGAACTTGTGTTCCGGTTTATTGAAGTTCAGACACTTCTCCTCGCT
CCATTCTGTCCACATTTGTGTGAGCACATCTGGACACTCCTGGGAAAGCCTGACTCAATT
ATGAATGCTTCATGGCCTGTGGCAGGTCCTGTTAATGAAGTTTTAATACACTCCTCACAG
TATCTTATGGAAGTAACACATGACCTTAGACTACGACTCAAGAACTATATGATGCCAGCT
AAAGGGAAGAAGACTGACAAACAACCCCTGCAGAAGCCCTCACATTGCACCATCTATGTG
GCAAAGAACTATCCACCTTGGCAACATACCACCCTGTCTGTTCTACGTAAACACTTTGAG
GCCAATAACGGAAAACTGCCTGACAACAAAGTCATTGCTAGTGAACTAGGCAGTATGCCA
GAACTGAAGAAATACATGAAGAAAGTCATGCCATTTGTTGCCATGATTAAGGAAAATCTG
GAGAAGATGGGGCCTCGTATTCTGGATTTGCAATTAGAATTTGATGAAAAGGCTGTGCTT
ATGGAGAATATAGTCTATCTGACTAATTCGCTTGAGCTAGAACACATAGAAGTCAAGTTT
GCCTCCGAAGCAGAAGATAAAATCAGGGAAGACTGCTGTCCTGGGAAACCACTTAATGTT
TTTAGAATAGAACCTGGTGTGTCCGTTTCTCTGGTGAATCCCCAGCCATCCAATGGCCAC
TTCTCAACCAAAATTGAAATCAGGCAAGGAGATAACTGTGATTCCATAATCAGGCGTTTA
ATGAAAATGAATCGAGGAATTAAAGACCTTTCCAAAGTGAAACTGATGAGATTTGATGAT
CCACTGTTGGGGCCTCGACGAGTTCCTGTCCTGGGAAAGGAGTACACCGAGAAGACCCCC
ATTTCTGAGCATGCTGTTTTCAATGTGGACCTCATGAGCAAGAAAATTCATCTGACTGAG
AATGGGATAAGGGTGGATATTGGCGATACAATAATCTATCTGGTTCATTAA
Enzyme 8 GenBank Gene ID BC150213 Link Image
Enzyme 8 GeneCard ID A7E266 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16424
Enzyme 9 Name cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name BCAT2
Enzyme 9 Protein Sequence >cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial) 
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
Enzyme 9 Number of Residues 392
Enzyme 9 Molecular Weight 44288
Enzyme 9 Theoretical pI 8.82
Enzyme 9 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • branched chain family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 9 General Function Amino acid transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B2RB87 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B2RB87_HUMAN Link Image
Enzyme 9 PDB ID 1KTA Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK314548 Link Image
Enzyme 9 GeneCard ID B2RB87 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location 19
Enzyme 9 Locus 19q13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16930
Enzyme 10 Name Leucine carboxyl methyltransferase 1
Enzyme 10 Synonyms
  1. Protein-leucine O-methyltransferase
Enzyme 10 Gene Name LCMT1
Enzyme 10 Protein Sequence >Leucine carboxyl methyltransferase 1 
MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKE
RKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLPSKYFE
VDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEE
KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQI
MIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLE
FLDEMELLEQLMRHYCLCWATKGGNELGLKEITY
Enzyme 10 Number of Residues 334
Enzyme 10 Molecular Weight 38380
Enzyme 10 Theoretical pI 5.91
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits (PPP2CA) to form alpha-leucine ester residues
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID Q9UIC8 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name LCMT1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AF037601 Link Image
Enzyme 10 GeneCard ID Q9UIC8 Link Image
Enzyme 10 GenAtlas ID LCMT1 Link Image
Enzyme 10 HGNC ID HGNC:17557 Link Image
Enzyme 10 Chromosome Location 16
Enzyme 10 Locus 16p12.3-p12.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J: Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. [PubMed Link Image]
  2. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available