| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2010-03-12 13:01:01 |
| Accession Number |
HMDB00172 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
L-Isoleucine |
| 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. BCAA are decreased in patients with liver disease, such as hepatitis, hepatic coma, cirrhosis, extrahepatic biliary atresia or portacaval shunt; aromatic amino acids (AAA)-tyrosine, tryptophan and phenylalanine, as well as methionine-are increased in these conditions. Valine, in particular, has been established as a useful supplemental therapy to the ailing liver. All the BCAA probably compete with AAA for absorption into the brain. Supplemental BCAA with vitamin B6 and zinc help normalize the BCAA:AAA ratio. The BCAA are not without side effects. Leucine alone, for example, exacerbates pellagra and can cause psychosis in pellagra patients by increasing excretion of niacin in the urine. Leucine may lower brain serotonin and dopamine. A dose of 3 g of isoleucine added to the niacin regime has cleared leucine-aggravated psychosis in schizophrenic patients. Isoleucine may have potential as an antipsychotic treatment. Leucine is more highly concentrated in foods than other amino acids. A cup of milk contains 800 mg of leucine and only 500 mg of isoleucine and valine. A cup of wheat germ has about 1.6 g of leucine and 1 g of isoleucine and valine. The ratio evens out in eggs and cheese. One egg and an ounce of most cheeses each contain about 400 mg of leucine and 400 mg of valine and isoleucine. The ratio of leucine to other BCAA is greatest in pork, where leucine is 7 to 8 g and the other BCAA together are only 3 to 4 g. (http://www.dcnutrition.com) |
| Synonyms |
- (2S,3S)-2-Amino-3-methylpentanoate
- (2S,3S)-2-Amino-3-methylpentanoic acid
- (2S,3S)-2-amino-3-methyl-Pentanoate
- (2S,3S)-2-amino-3-methyl-Pentanoic acid
- (2S,3S)-a-Amino-b-methyl-n-valerate
- (2S,3S)-a-Amino-b-methyl-n-valeric acid
- (2S,3S)-a-Amino-b-methylvalerate
- (2S,3S)-a-Amino-b-methylvaleric acid
- (2S,3S)-alph-Amino-beta-methylvalerate
- (2S,3S)-alph-Amino-beta-methylvaleric acid
- (2S,3S)-alpha-Amino-beta-merthyl-n-valerate
- (2S,3S)-alpha-Amino-beta-merthyl-n-valeric acid
- (2S,3S)-alpha-Amino-beta-merthylvalerate
- (2S,3S)-alpha-Amino-beta-merthylvaleric acid
- (2S,3S)-alpha-Amino-beta-methyl-n-valerate
- (2S,3S)-alpha-Amino-beta-methyl-n-valeric acid
- (2S,3S)-alpha-Amino-beta-methylvalerate
- (2S,3S)-alpha-Amino-beta-methylvaleric acid
- (S)-Isoleucine
- (S,S)-Isoleucine
- 2-Amino-3-methylpentanoate
- 2-Amino-3-methylpentanoic acid
- 2-Amino-3-methylvalerate
- 2-Amino-3-methylvaleric acid
- 2S,3S-Isoleucine
- Ile
- Isoleucine
- L-(+)-Isoleucine
- L-Ile
- [S-(R*,R*)]-2-Amino-3-methylpentanoate
- [S-(R*,R*)]-2-Amino-3-methylpentanoic acid
- erythro-L-Isoleucine
- iso-leucine
|
| Chemical IUPAC Name |
2-amino-3-methylpentanoic acid |
| Chemical Formula |
C6H13NO2 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- primary amine
- primary aliphatic amine (alkylamine)
- carboxylic acid
- alpha-aminoacid
|
| Biofunction |
- Essential amino acids
- Component of Aminoacyl-tRNA biosynthesis
- Component of Valine, leucine and isoleucine biosynthesis
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
131.173 |
| Monoisotopic Molecular Weight |
131.094635 |
| Isomeric SMILES |
CC[C@H](C)[C@H](N)C(O)=O |
| Canonical SMILES |
CCC(C)C(N)C(O)=O |
| KEGG Compound ID |
C00407  |
| BioCyc ID |
ILE |
| BiGG ID |
34887 |
| Wikipedia Link |
Ile |
| NuGOwiki Link |
HMDB00172 |
| Metagene Link |
HMDB00172 |
| METLIN ID |
5193 |
| PubChem Compound |
791 |
| PubChem Substance |
10367061 |
| ChEBI ID |
17191 |
| CAS Registry Number |
73-32-5 |
| InChI Identifier |
InChI=1/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1 |
| Synthesis Reference |
Marvel, C. S. L-Isoleucine. Organic Syntheses (1941), 21 60-4. |
| Melting Point (Experimental) |
285.5 oC |
| Experimental Water Solubility |
34.4 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 35 mg/mL [HMP experimental]
Source: PhysProp
|
| Predicted Water Solubility |
114.0 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
-1.70 [HANSCH,C ET AL. (1995)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-1.73 [Predicted by ALOGPS]; -1.6 [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 |
1H74 |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum
Download FID (Varian)
Show Experimental Conditions |
| Experimental 13C NMR Spectrum |
Download Spectrum
Download FID (Bruker)
Show Experimental Conditions |
| Experimental 13C HSQC Spectrum |
Download Spectrum
Download FID (Bruker)
Show Experimental Conditions |
| Predicted 1H NMR Spectrum |
Show Image
Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image
Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Show Image
Show Peaklist |
| BMRB Spectrum |
Show Image
Show Peaklist |
| Cellular Location |
- Cytoplasm
- Extracellular
- mitochondria
|
| Biofluid Location |
- Blood
- Cerebrospinal Fluid
- Saliva
- Urine
|
| Tissue Location |
| Tissue |
References |
| All Tissues |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
62.0 (48.0-76.0) 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 ]
|
| Biofluid |
Blood |
| Value |
40.0 +/- 20.0 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 |
69.0 +/- 13.0 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 |
64.0 +/- 13.0 uM |
| Age |
Children:1-13 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 |
84.0 +/- 18.0 uM |
| Age |
Adult:>18 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 |
44.0 +/- 6.0 uM |
| Age |
Children:1-13 yrs old |
| Sex |
N/A |
| 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 |
81.0 +/- 18.0 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 |
56.0 +/- 12.0 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Female |
| 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 |
58.5 (26.00-91.00) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
|
| Biofluid |
CSF |
| Value |
3.9 +/- 1.0 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 |
5.77 (3.30-8.24) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed ]
|
| Biofluid |
CSF |
| Value |
13.5 (8.8-18.2) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed ]
|
| Biofluid |
CSF |
| Value |
8.4 +/- 2.6 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 ]
|
| Biofluid |
CSF |
| Value |
8.4 +/- 2.5 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 ]
|
| Biofluid |
CSF |
| Value |
4.3 +/- 3.4 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 ]
|
| Biofluid |
CSF |
| Value |
7.0 +/- 5.0 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 ]
|
| Biofluid |
CSF |
| Value |
5.5 +/- 0.64 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed ]
|
| Biofluid |
Saliva |
| Value |
>10 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed ]
|
| Biofluid |
Urine |
| Value |
3.75 +/- 2.75 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 ]
|
| Biofluid |
Urine |
| Value |
1.579 (0.789-2.368) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
|
| Biofluid |
Urine |
| Value |
0.94 +/- 0.67 umol/mmol creatinine |
| Age |
Children:1-13 yrs 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 |
1.8 +/- 1.0 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 |
3.0 +/- 1.5 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 |
1.64 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 ]
|
| Biofluid |
Urine |
| Value |
20 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Based on one measurement |
| References |
- Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
|
|
| Concentrations (Abnormal) |
| Biofluid |
Blood |
| Value |
40.3 (38.0-42.6) 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 ]
|
| Biofluid |
Blood |
| Value |
42.7 (38.1-47.3) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Epilepsy |
| Comments |
Refractory localization-related epilepsy (RLE)
Acute Tonic-Clonic Seizures: increased |
| 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 ]
|
| Biofluid |
Blood |
| Value |
1495.2 +/- 373.0 uM |
| Age |
Elderly:>65 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 ]
|
| Biofluid |
Blood |
| Value |
166.0 +/- 5.0 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 ]
|
| Biofluid |
Blood |
| Value |
6100.00 (200.00-12000.00) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Maple syrup urine disease |
| Comments |
Not Available |
| References |
|
| Biofluid |
CSF |
| Value |
7.1 +/- 4.2 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 ]
|
| Biofluid |
CSF |
| Value |
5.9 +/- 4.0 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 ]
|
| Biofluid |
CSF |
| Value |
6.0 +/- 0.65 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Schizophrenia |
| Comments |
Not Available |
| References |
- Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed ]
|
| Biofluid |
CSF |
| Value |
2.4 +/- 0.65 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 ]
|
| Biofluid |
Urine |
| Value |
0.13 +/- 0.04 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 ]
|
|
| 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 ]
|
| 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 ]
|
| 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 ]
|
| 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 ]
|
| Maple syrup urine disease |
|
| Schizophrenia |
- Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed ]
|
|
| OMIM ID |
|
| Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Transcription/Translation |
SMP00019 |
|
| Valine, Leucine and Isoleucine Degradation |
SMP00032 |
map00280 |
|
| General 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 ]
- 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 ]
- He XY, Yang SY: Roles of type 10 17beta-hydroxysteroid dehydrogenase in intracrinology and metabolism of isoleucine and fatty acids. Endocr Metab Immune Disord Drug Targets. 2006 Mar;6(1):95-102. [PubMed ]
- 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 ]
- Vaalasti A, Suomalainen H, Kuokkanen K, Rechardt L: Neuropeptides in cutaneous neurofibromas of von Recklinghausen's disease. J Cutan Pathol. 1990 Dec;17(6):371-3. [PubMed ]
- Eriste E, Norberg A, Bonetto V, Nepomuceno D, Lovenberg TW, Sillard R, Jornvall H: A C-terminally elongated form of PHI from porcine intestine. Cell Mol Life Sci. 1999 Nov 15;56(7-8):709-13. [PubMed ]
- Jalan R, Olde Damink SW, Lui HF, Glabus M, Deutz NE, Hayes PC, Ebmeier K: Oral amino acid load mimicking hemoglobin results in reduced regional cerebral perfusion and deterioration in memory tests in patients with cirrhosis of the liver. Metab Brain Dis. 2003 Mar;18(1):37-49. [PubMed ]
- Hervieu G, Segretain D, Nahon JL: Developmental and stage-dependent expression of melanin-concentrating hormone in mammalian germ cells. Biol Reprod. 1996 Jun;54(6):1161-72. [PubMed ]
- Suk FM, Lin MH, Newman M, Pan S, Chen SH, Liu JD, Shih C: Replication advantage and host factor-independent phenotypes attributable to a common naturally occurring capsid mutation (I97L) in human hepatitis B virus. J Virol. 2002 Dec;76(23):12069-77. [PubMed ]
- Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed ]
- De Miranda J, Panizzutti R, Foltyn VN, Wolosker H: Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14542-7. Epub 2002 Oct 22. [PubMed ]
- 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 ]
- Blomstrand E, Eliasson J, Karlsson HK, Kohnke R: Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. J Nutr. 2006 Jan;136(1 Suppl):269S-73S. [PubMed ]
- Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed ]
- Sato T, Shimada Y, Nagasawa N, Nakanishi S, Jingami H: Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the activated state. J Biol Chem. 2003 Feb 7;278(6):4314-21. Epub 2002 Nov 19. [PubMed ]
- Edvinsson L: Innervation and effects of dilatory neuropeptides on cerebral vessels. New aspects. Blood Vessels. 1991;28(1-3):35-45. [PubMed ]
- 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 ]
- Wikipedia
|
| Metabolic Enzymes |
- Branched-chain-amino-acid aminotransferase, cytosolic
- Branched-chain-amino-acid aminotransferase, mitochondrial precursor
- Isoleucyl-tRNA synthetase, cytoplasmic
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial precursor
- cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase
- cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
- Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial)
- Isoleucyl-tRNA synthetase, mitochondrial
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5536 |
| Enzyme 1 Name |
Branched-chain-amino-acid aminotransferase, cytosolic |
| Enzyme 1 Synonyms |
- BCAT(c
- 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 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 1 Reactions |
- L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1036780 |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P54687 |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
BCAT1_HUMAN |
| 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 |
| Enzyme 1 GeneCard ID |
BCAT1 |
| Enzyme 1 GenAtlas ID |
BCAT1 |
| Enzyme 1 HGNC ID |
HGNC:976 |
| Enzyme 1 Chromosome Location |
12 |
| Enzyme 1 Locus |
12pter-q12 |
| Enzyme 1 SNPs |
SNPJam Report |
| Enzyme 1 General References |
- 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 ]
|
| 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 |
- BCAT(m
- Placental protein 18
- 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 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 2 Reactions |
- L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
2342862 |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O15382 |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
BCAT2_HUMAN |
| Enzyme 2 PDB ID |
1KTA |
| 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 |
| Enzyme 2 GeneCard ID |
BCAT2 |
| Enzyme 2 GenAtlas ID |
BCAT2 |
| Enzyme 2 HGNC ID |
HGNC:977 |
| Enzyme 2 Chromosome Location |
19 |
| Enzyme 2 Locus |
19q13 |
| Enzyme 2 SNPs |
SNPJam Report |
| Enzyme 2 General References |
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5886 |
| Enzyme 3 Name |
Isoleucyl-tRNA synthetase, cytoplasmic |
| Enzyme 3 Synonyms |
- Isoleucine--tRNA ligase
- IleRS
- IRS
|
| Enzyme 3 Gene Name |
IARS |
| Enzyme 3 Protein Sequence |
>Isoleucyl-tRNA synthetase, cytoplasmic
MSNKMLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHY
GHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEY
NNQCRAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGV
KVMPFSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAV
CVNPEMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYF
LKCKENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASG
CFTTEVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWF
VRVENMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFE
EVVCIGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYA
QVHYPFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLAS
DGQKMSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPW
YNAYRFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRL
YTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFL
TELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIR
DRKTIPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEP
DHMVLGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATG
GTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAK
SEGTYLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLP
GPACAYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDET
EIQNQTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLL
ENPLGQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVL
PTTADF
|
| Enzyme 3 Number of Residues |
1266 |
| Enzyme 3 Molecular Weight |
144960 |
| Enzyme 3 Theoretical pI |
6.10 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- isoleucine-tRNA ligase activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- tRNA ligase activity
|
| Process |
- RNA metabolism
- cellular metabolism
- isoleucyl-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-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
551622 |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P41252 |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SYIC_HUMAN |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>3801 bp
ATGAGCAACAAAATGCTTCAACAAGTTCCAGAAAACATAAATTTTCCTGCTGAAGAAGAG
AAAATCTTGGAGTTTTGGACTGAATTTAATTGTTTTCAGGAATGCTTAAAGCAATCAAAA
CATAAACCAAAATTTACCTTCTATGATGGTCCTCCTTTTGCAACTGGACTGCCTCACTAT
GGACATATACTTGCGGGTACAATTAAAGATATAGTTACAAGATATGCTCACCAGAGTGGG
TTTCATGTTGACAGAAGATTTGGATGGGATTGCCATGGCTTACCTGTGGAATATGAAATT
GATAAGACACTGGGAATCAGAGGACCAGAGGATGTGGCCAAAATGGGGATTACAGAGTAT
AACAATCAGTGCCGAGCAATTGTGATGAGATATTCTGCTGAGTGGAAGTCTACTGTTAGC
AGACTTGGCCGATGGATTGACTTTGACAATGACTATAAAACTCTGTATCCACAATTCATG
GAATCAGTCTGGTGGGTCTTCAAACAACTCTATGATAAAGGCCTTGTTTATAGAGGTGTG
AAAGTCATGCCCTTCTCTACGGCATGTAACACTCCACTTTCCAACTTCGAGTCACACCAG
AATTATAAGGATGTTCAAGATCCTTCAGTATTTGTAACTTTCCCTTTGGAAGAAGATGAA
ACTGTATCTTTAGTTGCTTGGACAACCACTCCCTGGACTCTACCTAGTAACCTTGCTGTG
TGTGTTAATCCAGAAATGCAATATGTGAAAATTAAAGATGTTGCCAGAGGACGATTACTC
ATTTTAATGGAAGCCAGATTGTCAGCCCTCTATAAATTGGAGAGTGACTATGAGATCCTT
GAAAGATTTCCTGGTGCCTATCTTAAAGGCAAGAAGTACAGGCCCCTGTTTGACTATTTC
CTGAAGTGTAAAGAGAATGGCGCTTTCACTGTGCTTGTTGACAACTATGTGAAGGAAGAA
GAAGGCACAGGGGTTGTCCACCAAGCTCCTTACTTCGGTGCTGAGGACTATCGGGTCTGT
ATGGACTTTAACATTATTCGGAAAGACTCACTCCCTGTTTGCCCTGTGGATGCTTCAGGC
TGCTTCACAACGGAGGTGACAGATTTCGCAGGACAGTATGTGAAGGATGCTGACAAAAGT
ATCATCAGGACTTTGAAGGAACAAGGCCGACTTCTGGTTGCCACCACCTTCACTCACAGC
TACCCTTTTTGCTGGAGATCAGACACTCCTCTAATTTACAAAGCAGTGCCCAGCTGGTTT
GTGCGAGTGGAGAACATGGTGGACCAGCTCCTAAGGAACAATGACCTGTGCTACTGGGTC
CCAGAGTTGGTACGAGAAAAACGATTTGGAAATTGGCTGAAAGATGCACGTGACTGGACA
ATTTCCAGAAACAGATACTGGGGCACCCCCATCCCACTGTGGGTCAGCGATGACTTTGAG
GAGGTGGTATGCATTGGGTCAGTGGCGGAACTTGAAGAACTGTCAGGAGCAAAGATCTCA
GATCTCCACAGAGAGAGTGTTGACCACCTGACCATTCCTTCACGCTGTGGGAAGGGATCC
TTGCACCGCATCTCTGAAGTGTTTGACTGTTGGTTTGAGAGTGGCAGCATGCCCTATGCT
CAGGTTCATTACCCGTTTGAAAACAAGAGGGAGTTTGAGGATGCTTTTCCTGCAGATTTC
ATTGCCGAGGGCATCGACCAAACCAGAGGATGGTTTTATACCCTGCTGGTGCTGGCCACG
GCCCTCTTTGGACAACCGCCTTTCAAGAACGTAATTGTGAATGGGCTTGTCCTGGCAAGT
GATGGCCAAAAAATGAGCAAACGGAAAAAGAATTATCCAGATCCAGTTTCCATCATCCAG
AAGTATGGTGCTGATGCCCTCAGATTATATCTGATTAACTCCCCTGTGGTGAGAGCAGAA
AACCTCCGCTTTAAAGAAGAGGGTGTGCGGGACGTCCTTAAGGATGTACTGCTCCCATGG
TACAATGCCTATCGCTTCTTAATCCAGAACGTTCTGAGGCTCCAGAAGGAGGAAGAAATA
GAATTTCTCTACAATGAGAACACGGTTAGAGAAAGCCCCAACATTACAGACCGGTGGATC
CTGTCCTTCATGCAGTCTCTCATTGGCTTCTTTGAGACTGAAATGGCAGCTTATAGGCTT
TATACTGTGGTGCCTCGCCTGGTCAAGTTTGTAGATATTCTGACCAATTGGTATGTTAGA
ATGAACCGCAGAAGATTAAAGGGTGAAAATGGGATGGAGGATTGTGTCATGGCCCTAGAA
ACCTTGTTTAGTGTTCTGCTTTCTCTTTGCAGACTTATGGCTCCCTACACACCTTTTCTC
ACTGAATTGATGTACCAGAATCTAAAGGTGCTGATTGACCCTGTTTCTGTTCAGGACAAG
GACACACTCAGCATTCACTACCTCATGCTGCCCCGTGTTCGAGAAGAATTGATTGACAAG
AAAACAGAGAGTGCAGTATCTCAGATGCAGTCTGTGATTGAACTTGGAAGAGTGATCAGA
GACCGAAAAACTATTCCCATAAAGTATCCTTTGAAAGAAATTGTGGTTATCCATCAAGAT
CCAGAAGCTCTTAAAGATATCAAGTCTTTGGAGAAGTATATCATTGAGGAACTCAATGTT
CGAAAAGTTACACTGTCTACAGATAAAAACAAGTATGGCATTCGGCTAAGGGCAGAACCA
GATCACATGGTCCTGGGGAAGCGTCTGAAGGGAGCCTTTAAGGCAGTGATGACGTCCATC
AAGCAGTTGAGCAGTGAGGAGCTGGAGCAGTTCCAGAAGACTGGGACCATTGTTGTGGAA
GGCCATGAATTGCACGATGAAGACATCCGCCTCATGTACACCTTTGATCAGGCCACAGGT
GGGACTGCGCAATTTGAAGCACACTCAGATGCTCAGGCTTTGGTCCTCTTAGATGTCACT
CCTGACCAGTCAATGGTAGATGAAGGAATGGCTCGGGAAGTCATCAATCGCATACAGAAA
CTTCGCAAAAAGTGCAATCTGGTTCCAACTGATGAAATCACAGTGTACTATAAAGCAAAG
TCTGAAGGAACATATCTGAATAGTGTTATTGAAAGCCACACAGAGTTCATATTTACCACC
ATAAAGGCTCCCTTGAAACCATATCCAGTTTCTCCATCGGATAAAGTCCTTATTCAAGAA
AAAACACAGTTGAAGGGATCTGAACTGGAAATTACACTCACCAGAGGATCTTCCCTTCCT
GGTCCTGCTTGTGCATATGTCAATCTTAACATTTGTGCAAATGGCAGTGAACAAGGTGGA
GTATTGCTCCTGGAAAATCCAAAAGGTGACAATAGGTTGGACCTTTTAAAGCTGAAGAGT
GTTGTCACTAGCATTTTTGGTGTGAAAAATACAGAGCTGGCTGTCTTCCATGATGAAACA
GAAATACAAAACCAAACTGACTTACTGAGTCTTAGTGGAAAAACACTTTGTGTGACTGCA
GGATCGGCTCCCTCTCTGATCAACAGTTCTAGTACTCTTCTTTGTCAGTATATCAACCTA
CAGCTCCTGAATGCAAAGCCACAAGAGTGTTTAATGGGGACAGTGGGCACTCTCCTGCTT
GAAAACCCACTTGGGCAGAATGGACTCACCCACCAAGGTCTTCTGTATGAAGCAGCCAAG
GTGTTTGGCCTTCGGAGCAGGAAGCTAAAGCTGTTTCTGAATGAGACCCAAACGCAGGAA
ATTACAGAAGACATCCCCGTGAAGACTTTGAATATGAAGACTGTGTATGTTTCTGTGTTA
CCAACAACAGCAGACTTCTAG
|
| Enzyme 3 GenBank Gene ID |
D28473 |
| Enzyme 3 GeneCard ID |
IARS |
| Enzyme 3 GenAtlas ID |
IARS |
| Enzyme 3 HGNC ID |
HGNC:5330 |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report |
| Enzyme 3 General References |
- Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T: Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7435-9. [PubMed ]
- Nichols RC, Raben N, Boerkoel CF, Plotz PH: Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension. Gene. 1995 Apr 3;155(2):299-304. [PubMed ]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6936 |
| Enzyme 4 Name |
Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial precursor |
| Enzyme 4 Synonyms |
- SBCAD
- 2-methyl branched chain acyl-CoA dehydrogenase
- 2-MEBCAD
- 2-methylbutyryl-coenzyme A dehydrogenase
- 2-methylbutyryl-CoA dehydrogenase
|
| Enzyme 4 Gene Name |
ACADSB |
| Enzyme 4 Protein Sequence |
>Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial precursor
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDE
EMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLS
TVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAG
AGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRD
TPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQ
MLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAG
KPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ
LNTIAKHIDAEY
|
| Enzyme 4 Number of Residues |
432 |
| Enzyme 4 Molecular Weight |
47486 |
| Enzyme 4 Theoretical pI |
7.00 |
| Enzyme 4 GO Classification |
| Function |
- acyl-CoA dehydrogenase activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Lipid transport and metabolism |
| Enzyme 4 Specific Function |
Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
531391 |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P45954 |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ACDSB_HUMAN |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1299 bp
ATGGAGGGCCTGGCAGTGCGGTTGCTGCGCGGCAGCAGGCTGCTAAGAAGAAATTTCCTG
ACTTGTTTGTCTTCTTGGAAGATTCCTCCTCATGTCTCAAAATCTTCCCAGTCAGAAGCT
CTACTCAATATAACAAATAATGGAATACACTTTGCTCCCCTGCAAACATTTACAGATGAG
GAAATGATGATAAAGAGTTCAGTTAAAAAATTTGCTCAGGAACAAATTGCACCTTTGGTT
TCAACCATGGATGAAAATTCGAAAATGGAGAAATCAGTAATACAAGGATTATTTCAACAA
GGGTTGATGGGTATTGAAGTTGACCCAGAATATGGAGGCACAGGAGCTTCTTTTTTATCC
ACTGTGCTCGTGATAGAGGAATTAGCCAAAGTTGATGCATCTGTGGCTGTCTTTTGTGAG
ATCCAGAACACATTAATTAACACACTGATTAGAAAACATGGAACAGAAGAACAAAAGGCC
ACCTATTTGCCTCAGCTCACTACAGAAAAAGTAGGAAGTTTCTGCCTTTCAGAGGCTGGA
GCAGGTAGTGACTCATTTGCTTTGAAGACCAGAGCTGATAAAGAGGGAGATTATTATGTC
CTCAATGGATCAAAGATGTGGATCAGCAGTGCTGAGCATGCAGGGCTCTTTCTGGTGATG
GCAAATGTAGACCCTACCATTGGATATAAGGGAATTACCTCCTTCTTAGTAGATCGTGAT
ACTCCGGGCCTTCATATAGGGAAACCTGAAAACAAATTGGGGCTCAGAGCTTCTTCCACC
TGCCCGTTAACATTCGAAAATGTCAAGGTTCCAGAAGCCAATATCTTGGGACAAATTGGA
CATGGCTATAAGTATGCCATAGGGAGTCTCAATGAAGGTAGAATAGGAATTGCTGCACAG
ATGCTGGGACTGGCGCAAGGATGTTTTGACTACACTATTCCATATATTAAAGAAAGGATA
CAATTTGGCAAAAGACTATTTGATTTTCAGGGCCTCCAACACCAAGTGGCTCACGTGGCC
ACCCAGCTGGAAGCTGCAAGATTACTAACATACAATGCTGCTAGGCTTTTAGAAGCTGGA
AAGCCATTCATAAAAGAAGCGTCAATGGCCAAATACTATGCATCAGAGATTGCAGGACAA
ACAACGAGTAAATGTATCGAGTGGATGGGGGGAGTAGGCTACACCAAAGATTACCCTGTG
GAGAAATACTTCCGAGATGCAAAGATTGGTACGATATATGAAGGAGCTTCCAACATCCAG
TTGAACACCATTGCAAAGCATATCGATGCAGAATACTGA
|
| Enzyme 4 GenBank Gene ID |
U12778 |
| Enzyme 4 GeneCard ID |
ACADSB |
| Enzyme 4 GenAtlas ID |
ACADSB |
| Enzyme 4 HGNC ID |
HGNC:91 |
| Enzyme 4 Chromosome Location |
10 |
| Enzyme 4 Locus |
10q26.13 |
| Enzyme 4 SNPs |
SNPJam Report |
| Enzyme 4 General References |
- Rozen R, Vockley J, Zhou L, Milos R, Willard J, Fu K, Vicanek C, Low-Nang L, Torban E, Fournier B: Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics. 1994 Nov 15;24(2):280-7. [PubMed ]
- Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [PubMed ]
- Gibson KM, Burlingame TG, Hogema B, Jakobs C, Schutgens RB, Millington D, Roe CR, Roe DS, Sweetman L, Steiner RD, Linck L, Pohowalla P, Sacks M, Kiss D, Rinaldo P, Vockley J: 2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism. Pediatr Res. 2000 Jun;47(6):830-3. [PubMed ]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
13126 |
| Enzyme 5 Name |
cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase |
| Enzyme 5 Synonyms |
- IARS, transcript variant short, mRNA
- Isoleucine-tRNA synthetase, isoform CRA_e
|
| Enzyme 5 Gene Name |
IARS |
| Enzyme 5 Protein Sequence |
>cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase
MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHIL
AGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQC
RAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMP
FSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNP
EMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCK
ENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTT
EVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVE
NMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVC
IGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHY
PFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQK
MSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAY
RFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVV
PRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELM
YQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKT
IPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMV
LGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQ
FEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGT
YLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPAC
AYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQN
QTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPL
GQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTA
DF
|
| Enzyme 5 Number of Residues |
1262 |
| Enzyme 5 Molecular Weight |
144500 |
| Enzyme 5 Theoretical pI |
6.03 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
Not Available |
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
158259489 |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
A8KAE9 |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
A8KAE9_HUMAN |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AK293014 |
| Enzyme 5 GeneCard ID |
A8KAE9 |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
Not Available |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
16424 |
| Enzyme 6 Name |
cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial) |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
BCAT2 |
| Enzyme 6 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 6 Number of Residues |
392 |
| Enzyme 6 Molecular Weight |
44288 |
| Enzyme 6 Theoretical pI |
8.82 |
| Enzyme 6 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 6 General Function |
Amino acid transport and metabolism |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
B2RB87 |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
B2RB87_HUMAN |
| Enzyme 6 PDB ID |
1KTA |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
AK314548 |
| Enzyme 6 GeneCard ID |
B2RB87 |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
Not Available |
| Enzyme 6 Chromosome Location |
19 |
| Enzyme 6 Locus |
19q13 |
| Enzyme 6 SNPs |
SNPJam Report |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
16441 |
| Enzyme 7 Name |
Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial) |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
IARS2 |
| Enzyme 7 Protein Sequence |
>Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial)
MRWGLRPRGPGAAALATARSLWGTPRLPCSPGWQGATKRLLVRSVSGASNHQPNSNSGRY
RDTVLLPQTSFPMKLLGRQQPDTELEIQQKCGFSELYSWQRERKVKTEFCLHDGPPYANG
DPHVGHALNKILKDIANRFHMMNGSKIHFVPGWDCHGLPIEIKVLSELGREAQNLSAMEI
RKKARSFAKAAIEKQKSAFIRWGIMADWNNCYYTFDGKYEAKQLRTFYQMYDKGLVYRSY
KPVFWSPSSRTALAEAELEYNPEHVSRSIYVKFPLLKPSPKLASLIDGSSPVSILVWTTQ
PWTIPANEAVCYMPESKYAVVKCSKSGDLYVLAADKVASVASTLETTFETISTLSGVDLE
NGTCSHPLIPDKASPLLPANHVTMAKGTGLVHTAPAHGMEDYGVASQHNLPMDCLVDEDG
VFTDVAGPELQNKAVLEEGTDVVIKMLQTAKNLLKEEKLVHSYPYDWRTKKPVVIRASKQ
WFINITDIKTAAKELLKKVKFIPGSALNGMVEMMDRRPYWCISRQRVWGVPIPVFHHKTK
DEYLINSQTTEHIVKLVEQHGSDIWWTLPPEQLLPKEVLSEVGGPDALEYVPGQDILDIW
FDSGTSWSYVLPGPDQRADLYLEGKDQLGGWFQSSLLTSVAARKRAPYKTVIVHGFTLGE
KGEKMSKSLGNVIHPDVVVNGGQDQSKEPPYGADVLRWWVADSNVFTEVAIGPSVLNAAR
DDISKLRNTLRFLLGNVADFNPETDSIPVNDMYVIDQYMLHLLQDLANKITELYKQYDFG
KVVRLLRTFYTRELSNFYFSIIKDRLYCEKENDPKRRSCQTALVEILDVIVRSFAPILPH
LAEEVFQHIPYIKEPKSVFRTGWISTSSIWKKPGLEEAVESACAMRDSFLGSIPGKNAAE
YKVITVIEPGLLFEIIEMLQSEETSSTSQLNELMMASESTLLAQEPREMTADVIELKGKF
LINLEGGDIREESSYKVIVMPTTKEKCPRCWKYTAESSDTLCPRCAEVVSGK
|
| Enzyme 7 Number of Residues |
1012 |
| Enzyme 7 Molecular Weight |
113793 |
| Enzyme 7 Theoretical pI |
7.20 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- isoleucine-tRNA ligase activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- tRNA ligase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- RNA metabolism
- cellular metabolism
- isoleucyl-tRNA aminoacylation
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolism
|
| Component |
| — |
|
| Enzyme 7 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
B2RPG8 |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
B2RPG8_HUMAN |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
BC137438 |
| Enzyme 7 GeneCard ID |
B2RPG8 |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
Not Available |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
16933 |
| Enzyme 8 Name |
Isoleucyl-tRNA synthetase, mitochondrial |
| Enzyme 8 Synonyms |
- Isoleucine--tRNA ligase
- IleRS
|
| Enzyme 8 Gene Name |
IARS2 |
| Enzyme 8 Protein Sequence |
>Isoleucyl-tRNA synthetase, mitochondrial
MRWGLRPRGPGAAALATARSLWGTPRLPCSPGWQGATKRLLVRSVSGASNHQPNSNSGRY
RDTVLLPQTSFPMKLLGRQQPDTELEIQQKCGFSELYSWQRERKVKTEFCLHDGPPYANG
DPHVGHALNKILKDIANRFHMMNGSKIHFVPGWDCHGLPIEIKVLSELGREAQNLSAMEI
RKKARSFAKAAIEKQKSAFIRWGIMADWNNCYYTFDGKYEAKQLRTFYQMYDKGLVYRSY
KPVFWSPSSRTALAEAELEYNPEHVSRSIYVKFPLLKPSPKLASLIDGSSPVSILVWTTQ
PWTIPANEAVCYMPESKYAVVKCSKSGDLYVLAADKVASVASTLETTFETISTLSGVDLE
NGTCSHPLIPDKASPLLPANHVTMAKGTGLVHTAPAHGMEDYGVASQHNLPMDCLVDEDG
VFTDVAGPELQNKAVLEEGTDVVIKMLQTAKNLLKEEKLVHSYPYDWRTKKPVVIRASKQ
WFINITDIKTAAKELLKKVKFIPGSALNGMVEMMDRRPYWCISRQRVWGVPIPVFHHKTK
DEYLINSQTTEHIVKLVEQHGSDIWWTLPPEQLLPKEVLSEVGGPDALEYVPGQDILDIW
FDSGTSWSYVLPGPDQRADLYLEGKDQLGGWFQSSLLTSVAARKRAPYKTVIVHGFTLGE
KGEKMSKSLGNVIHPDVVVNGGQDQSKEPPYGADVLRWWVADSNVFTEVAIGPSVLNAAR
DDISKLRNTLRFLLGNVADFNPETDSIPVNDMYVIDQYMLHLLQDLANKITELYKQYDFG
KVVRLLRTFYTRELSNFYFSIIKDRLYCEKENDPKRRSCQTALVEILDVIVRSFAPILPH
LAEEVFQHIPYIKEPKSVFRTGWISTSSIWKKPGLEEAVESACAMRDSFLGSIPGKNAAE
YKVITVIEPGLLFEIIEMLQSEETSSTSQLNELMMASESTLLAQEPREMTADVIELKGKF
LINLEGGDIREESSYKVIVMPTTKEKCPRCWKYTAESSDTLCPRCAEVVSGK
|
| Enzyme 8 Number of Residues |
1012 |
| Enzyme 8 Molecular Weight |
113793 |
| Enzyme 8 Theoretical pI |
7.20 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- isoleucine-tRNA ligase activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- tRNA ligase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- RNA metabolism
- cellular metabolism
- isoleucyl-tRNA aminoacylation
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolism
|
| Component |
| — |
|
| Enzyme 8 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 8 Specific Function |
ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile) |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9NSE4 |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
SYIM_HUMAN |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
AY267462 |
| Enzyme 8 GeneCard ID |
Q9NSE4 |
| Enzyme 8 GenAtlas ID |
IARS2 |
| Enzyme 8 HGNC ID |
HGNC:29685 |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |
