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 Phenylpyruvic acid (HMDB00205)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-25 17:02:57
Accession Number HMDB00205
Secondary Accession Numbers HMDB01237
Common Name Phenylpyruvic acid
Description Phenylpyruvic acid is a keto-acid that is an intermediate or catabolic byproduct of phenylalanine metabolism. It has a slight honey-like odor. Levels of phenylpyruvate are normally very low in blood or urine. High levels of phenylpyruvic acid can be found in the urine of individuals with phenylketonuria (PKU). PKU is due to lack of the enzyme phenylalanine hydroxylase (PAH), so that phenylalanine is converted not to tyrosine but to phenylpyruvic acid. In particular, excessive phenylalanine can be metabolized into phenylketones through, a transaminase pathway route involving glutamate. Metabolites of this transamination reaction include phenylacetate, phenylpyruvate and phenethylamine. In persons with PKU, dietary phenylalanine either accumulates in the body or some of it is converted to phenylpyruvic acid. Individuals with PKU tend to excrete large quantities of phenylpyruvate, phenylacetate and phenyllactate, along with phenylalanine, in their urine. If untreated, mental retardation effects and microcephaly are evident by the first year along with other symptoms which include: unusual irritability, epileptic seizures and skin lesions. Hyperactivity, EEG abnormalities and seizures, and severe learning disabilities are major clinical problems later in life. A "musty or mousy" odor of skin, hair, sweat and urine (due to phenylacetate accumulation); and a tendency to hypopigmentation and eczema are also observed. The neural-development effects of PKU are primarily due to the disruption of neurotransmitter synthesis. In particular, phenylalanine is a large, neutral amino acid which moves across the blood-brain barrier (BBB) via the large neutral amino acid transporter (LNAAT). Excessive phenylalanine in the blood saturates the transporter. Thus, excessive levels of phenylalanine significantly decrease the levels of other LNAAs in the brain. But since these amino acids are required for protein and neurotransmitter synthesis, phenylalanine accumulation disrupts brain development, leading to mental retardation.
Synonyms
  1. 2-Oxo-3-phenylpropanoate
  2. 2-Oxo-3-phenylpropanoic acid
  3. 3-Phenyl-2-oxopropanoate
  4. 3-Phenyl-2-oxopropanoic acid
  5. 3-Phenylpyruvate
  6. 3-Phenylpyruvic acid
  7. Phenylpyroracemate
  8. Phenylpyroracemic acid
  9. Phenylpyruvate
  10. alpha-Ketohydrocinnamate
  11. alpha-Ketohydrocinnamic acid
  12. b-Phenylpyruvate
  13. b-Phenylpyruvic acid
  14. keto-Phenylpyruvate
  15. beta-Phenylpyruvate
  16. beta-Phenylpyruvic acid
Chemical IUPAC Name 2-oxo-3-phenyl-propanoic acid
Chemical Formula C9H8O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Aromatic Acids
Sub Class
  • Miscellaneous aromatic acids
Family
  • Mammalian Metabolite
Species
  • ketone
  • carboxylic acid
  • aromatic compound
Biofunction
  • Component of Novobiocin biosynthesis
  • Component of Phenylalanine metabolism
  • Component of Phenylalanine, tyrosine and tryptophan biosynthesis
  • Component of Tyrosine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 164.158
Monoisotopic Molecular Weight 164.047348
Isomeric SMILES OC(=O)C(=O)CC1=CC=CC=C1
Canonical SMILES OC(=O)C(=O)CC1=CC=CC=C1
KEGG Compound ID C00166 Link Image
BioCyc ID PHENYL-PYRUVATE Link Image
BiGG ID 34111 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00205 Link Image
Metagene Link HMDB00205 Link Image
METLIN ID 328 Link Image
PubChem Compound 997 Link Image
PubChem Substance 7885109 Link Image
ChEBI ID 18005 Link Image
CAS Registry Number 156-06-9
InChI Identifier InChI=1/C9H8O3/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5H,6H2,(H,11,12)
Synthesis Reference Li, Hongbin; Luo, Yuzhong. Preparation of phenyl-pyruvic acid by dicarbonylation of benzyl halide. Faming Zhuanli Shenqing Gongkai Shuomingshu (1996), 5 pp.
Melting Point (Experimental) 154
Experimental Water Solubility 112 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 0.932 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.30 [Predicted by ALOGPS]; 1.1 [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 1LCO Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
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
  • mitochondria
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.5 +/- 0.1 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Turchany JM, Leung PS, Iwayama T, Jefferson DM, Ishida J, Yamaguchi M, Munoz S, Danner DJ, Dickson ER, Gershwin ME: Comparative metabolism and structure of BCKD-E2 in primary biliary cirrhosis. J Autoimmun. 1993 Aug;6(4):459-66. [PubMed Link Image]
Biofluid Urine
Value 0.17 (0.05-0.67) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 0.24 (0.10-0.76) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 0.25 +/- 0.43 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 2.00 (0.00-4.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 50.0 (40.0-60.0) uM
Age Newborn:0-30 days old
Sex Both
Condition Phenylketonuria
Comments Not Available
References
  • Langenbeck U, Behbehani A, Luthe H: Renal transport of aromatic acids in patients with phenylketonuria. J Inherit Metab Dis. 1981;4(2):69-70. [PubMed Link Image]
Biofluid Blood
Value 1.4 +/- 0.2 uM
Age Adult:>18 yrs old
Sex Both
Condition Primary biliary cirrhosis
Comments Not Available
References
  • Turchany JM, Leung PS, Iwayama T, Jefferson DM, Ishida J, Yamaguchi M, Munoz S, Danner DJ, Dickson ER, Gershwin ME: Comparative metabolism and structure of BCKD-E2 in primary biliary cirrhosis. J Autoimmun. 1993 Aug;6(4):459-66. [PubMed Link Image]
Biofluid Urine
Value 650.00 (300.00-1000.00) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Condition Phenylketonuria
Comments Not Available
References
Biofluid Urine
Value 146.6 +/- 244.6 umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Condition Phenylketonuria
Comments Not Available
References
  • Monch E, Kneer J, Jakobs C, Arnold M, Diehl H, Batzler U: Examination of urine metabolites in the newborn period and during protein loading tests at 6 months of age--Part 1. Eur J Pediatr. 1990;149 Suppl 1:S17-24. [PubMed Link Image]
Associated Disorders
Condition References
Phenylketonuria
Primary biliary cirrhosis
  • Turchany JM, Leung PS, Iwayama T, Jefferson DM, Ishida J, Yamaguchi M, Munoz S, Danner DJ, Dickson ER, Gershwin ME: Comparative metabolism and structure of BCKD-E2 in primary biliary cirrhosis. J Autoimmun. 1993 Aug;6(4):459-66. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Phenylalanine and Tyrosine Metabolism SMP00008 Link Image map00360 Link Image
General References
  1. Lasala JM, Coscia CJ: Accumulation of a tetrahydroisoquinoline in phenylketonuria. Science. 1979 Jan 19;203(4377):283-4. [PubMed Link Image]
  2. Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
  3. Cassidei L, Dell'atti A, Sciacovelli O: Improvement of the FeCl3 test for phenylpyruvic acid. Clin Chim Acta. 1978 Dec 1;90(2):121-7. [PubMed Link Image]
  4. Michals K, Matalon R: Phenylalanine metabolites, attention span and hyperactivity. Am J Clin Nutr. 1985 Aug;42(2):361-5. [PubMed Link Image]
  5. 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]
  6. Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
  7. Nakahara T, Ishida J, Yamaguchi M, Nakamura M: Determination of alpha-keto acids including phenylpyruvic acid in human plasma by high-performance liquid chromatography with chemiluminescence detection. Anal Biochem. 1990 Nov 1;190(2):309-13. [PubMed Link Image]
Metabolic Enzymes
  1. Tyrosine aminotransferase
  2. Aspartate aminotransferase, cytoplasmic
  3. Aspartate aminotransferase, mitochondrial precursor
  4. cDNA FLJ76150, highly similar to Homo sapiens 4-hydroxyphenylpyruvate dioxygenase
  5. cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K (Cysteine conjugate-beta lyase
  6. cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
  7. cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
  8. cDNA, FLJ92196, Homo sapiens macrophage migration inhibitory factor(glycosylation-inhibiting factor) (MIF), mRNA (Macrophage migration inhibitory factor) (Glycosylation-inhibiting factor)
Enzyme 1 [top]
Enzyme 1 ID 5509
Enzyme 1 Name Tyrosine aminotransferase
Enzyme 1 Synonyms
  1. L-tyrosine:2-oxoglutarate aminotransferase
  2. TAT
Enzyme 1 Gene Name TAT
Enzyme 1 Protein Sequence >Tyrosine aminotransferase 
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
Enzyme 1 Number of Residues 454
Enzyme 1 Molecular Weight 50400
Enzyme 1 Theoretical pI 6.24
Enzyme 1 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • binding
  • carbon-sulfur lyase activity
  • catalytic activity
  • lyase activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • tyrosine transaminase activity
  • vitamin binding
Process
  • amino acid and derivative metabolism
  • amino acid catabolism
  • amino acid metabolism
  • aromatic amino acid family catabolism
  • aromatic amino acid family metabolism
  • biosynthesis
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function L-tyrosine + 2-oxoglutarate = 4- hydroxyphenylpyruvate + L-glutamate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + 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 36713 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P17735 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ATTY_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1365 bp 
ATGGACCCATACATGATTCAGATGAGCAGCAAAGGCAACCTCCCCTCAATTCTGGACGTG
CATGTCAACGTTGGTGGGAGAAGCTCTGTGCCGGGAAAAATGAAAGGCAGAAAGGCCAGG
TGGTCTGTGAGGCCCTCAGACATGGCCAAGAAAACTTTCAACCCCATCCGAGCCATTGTG
GACAACATGAAGGTGAAACCAAATCCAAACAAAACCATGATTTCCCTGTCCATTGGGGAC
CCTACTGTGTTTGGAAACCTGCCTACAGACCCTGAAGTTACCCAGGCAATGAAAGATGCC
CTGGACTCGGGCAAATATAATGGCTATGCCCCATCCATCGGCTTCCTATCCAGTCGGGAG
GAGATTGCTTCTTATTACCACTGTCCTGAGGCACCCCTAGAAGCTAAGGACGTCATTCTG
ACAAGTGGCTGCAGCCAAGCTATTGACCTTTGTTTAGCTGTGTTGGCCAACCCAGGGCAG
AACATCCTGGTTCCAAGACCTGGTTTCTCTCTCTACAAGACTCTGGCTGAGTCTATGGGA
ATTGAGGTCAAACTCTACAATTTGTTGCCAGAGAAATCTTGGGAAATTGACCTGAAACAA
CTGGAATATCTAATTGATGAAAAGACAGCTTGTCTCATTGTCAATAATCCATCAAACCCC
TGTGGGTCAGTGTTCAGCAAACGTCATCTTCAGAAGATTCTGGCAGTGGCTGCACGGCAG
TGTGTCCCCATCTTAGCTGATGAGATCTATGGAGACATGGTGTTTTCGGATTGCAAATAT
GAACCACTGGCCACCCTCAGCACCGATGTCCCCATCCTGTCCTGTGGAGGGCTGGCCAAG
CGCTGGCTGGTTCCTGGCTGGAGGTTGGGCTGGATCCTCATTCATGACCGAAGAGACATT
TTTGGCAATGAGATCCGAGATGGGCTGGTGAAGCTGAGTCAGCGCATTTTGGGACCCTGT
ACCATTGTCCAGGGAGCTCTGAAAAGCATCCTATGTCGCACCCCGGGAGAGTTTTACCAC
AACACTCTGAGCTTCCTCAAGTCCAATGCTGATCTCTGTTATGGGGCGTTGGCTGCCATC
CCTGGACTCCGGCCAGTCCGCCCTTCTGGGGCTATGTACCTCATGGTTGGAATTGAGATG
GAACATTTCCCAGAATTTGAGAACGATGTGGAGTTCACGGAGCGGTTAGTTGCTGAGCAG
TCTGTCCACTGCCTCCCAGCAACGTGCTTTGAGTACCCGAATTTCATCCGAGTGGTCATC
ACAGTCCCCGAGGTGATGATGCTGGAGGCGTGCAGCCGGATCCAGGAGTTCTGTGAGCAG
CACTACCATTGTGCTGAAGGCAGCCAGGAGGAGTGTGATAAATAG
Enzyme 1 GenBank Gene ID X52520 Link Image
Enzyme 1 GeneCard ID TAT Link Image
Enzyme 1 GenAtlas ID TAT Link Image
Enzyme 1 HGNC ID HGNC:11573 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16q22.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Rettenmeier R, Natt E, Zentgraf H, Scherer G: Isolation and characterization of the human tyrosine aminotransferase gene. Nucleic Acids Res. 1990 Jul 11;18(13):3853-61. [PubMed Link Image]
  2. Zelenin SM, Mertvetsov NP: [Nucleotide sequence of the human tyrosine aminotransferase gene] Bioorg Khim. 1994 Feb;20(2):196-204. [PubMed Link Image]
  3. Seralini GE, Luu-The V, Labrie F: Cloning and expression of human tyrosine aminotransferase cDNA. Biochim Biophys Acta. 1995 Jan 2;1260(1):97-101. [PubMed Link Image]
  4. Natt E, Kida K, Odievre M, Di Rocco M, Scherer G: Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9297-301. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5515
Enzyme 2 Name Aspartate aminotransferase, cytoplasmic
Enzyme 2 Synonyms
  1. Transaminase A
  2. Glutamate oxaloacetate transaminase 1
Enzyme 2 Gene Name GOT1
Enzyme 2 Protein Sequence >Aspartate aminotransferase, cytoplasmic 
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
Enzyme 2 Number of Residues 413
Enzyme 2 Molecular Weight 46248
Enzyme 2 Theoretical pI 7.01
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 179067 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P17174 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AATC_HUMAN Link Image
Enzyme 2 PDB ID 1AJS Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1242 bp 
ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA
Enzyme 2 GenBank Gene ID M37400 Link Image
Enzyme 2 GeneCard ID GOT1 Link Image
Enzyme 2 GenAtlas ID GOT1 Link Image
Enzyme 2 HGNC ID HGNC:4432 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q24.1-q25.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed Link Image]
  2. Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5516
Enzyme 3 Name Aspartate aminotransferase, mitochondrial precursor
Enzyme 3 Synonyms
  1. Transaminase A
  2. Glutamate oxaloacetate transaminase 2
Enzyme 3 Gene Name GOT2
Enzyme 3 Protein Sequence >Aspartate aminotransferase, mitochondrial precursor 
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKGMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
Enzyme 3 Number of Residues 430
Enzyme 3 Molecular Weight 47476
Enzyme 3 Theoretical pI 9.38
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-24
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 179104 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P00505 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AATM_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1293 bp 
ATGGCCCTGCTGCACTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATGCCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGGCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA
Enzyme 3 GenBank Gene ID M22632 Link Image
Enzyme 3 GeneCard ID GOT2 Link Image
Enzyme 3 GenAtlas ID GOT2 Link Image
Enzyme 3 HGNC ID HGNC:4433 Link Image
Enzyme 3 Chromosome Location 16
Enzyme 3 Locus 16q21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed Link Image]
  2. Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13081
Enzyme 4 Name cDNA FLJ76150, highly similar to Homo sapiens 4-hydroxyphenylpyruvate dioxygenase
Enzyme 4 Synonyms
  1. HPD, mRNA
  2. 4-hydroxyphenylpyruvate dioxygenase, isoform CRA_b
Enzyme 4 Gene Name HPD
Enzyme 4 Protein Sequence >cDNA FLJ76150, highly similar to Homo sapiens 4-hydroxyphenylpyruvate dioxygenase 
MTTYSDKGAKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSH
VIKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMRE
PWVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEM
IDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPI
NEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLR
EKLKTAKIKVKENIDALEELKILVDYDEKGYLLQIFTKPVQDRPTLFLEVIQRHNHQGFG
AGNFNSLFKAFEEEQNLRGNLTNMETNGVVPGM
Enzyme 4 Number of Residues 393
Enzyme 4 Molecular Weight 44935
Enzyme 4 Theoretical pI 7.01
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158255088 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K461 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K461_HUMAN Link Image
Enzyme 4 PDB ID 1SQI Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK290826 Link Image
Enzyme 4 GeneCard ID A8K461 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15228
Enzyme 5 Name cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K (Cysteine conjugate-beta lyase
Enzyme 5 Synonyms
  1. cytoplasmic (Glutamine transaminase K, kyneurenine aminotransferase), isoform CRA_a)
Enzyme 5 Gene Name CCBL1
Enzyme 5 Protein Sequence >cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K (Cysteine conjugate-beta lyase 
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
Enzyme 5 Number of Residues 422
Enzyme 5 Molecular Weight 47876
Enzyme 5 Theoretical pI 6.45
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Amino acid transport and metabolism
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
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158255792 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8K563 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K563_HUMAN Link Image
Enzyme 5 PDB ID 1W7N Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1269 bp 
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTTATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Enzyme 5 GenBank Gene ID AK291178 Link Image
Enzyme 5 GeneCard ID A8K563 Link Image
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 Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16502
Enzyme 6 Name cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name GOT1
Enzyme 6 Protein Sequence >cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b) 
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
Enzyme 6 Number of Residues 413
Enzyme 6 Molecular Weight 46248
Enzyme 6 Theoretical pI 7.01
Enzyme 6 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • 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
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2R6R7 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2R6R7_HUMAN Link Image
Enzyme 6 PDB ID 1AJS Link Image
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 AK312684 Link Image
Enzyme 6 GeneCard ID B2R6R7 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q24.1-q25.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16503
Enzyme 7 Name cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name TAT
Enzyme 7 Protein Sequence >cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a) 
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
Enzyme 7 Number of Residues 454
Enzyme 7 Molecular Weight 50400
Enzyme 7 Theoretical pI 6.24
Enzyme 7 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • binding
  • carbon-sulfur lyase activity
  • catalytic activity
  • lyase activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • tyrosine transaminase activity
  • vitamin binding
Process
  • amino acid and derivative metabolism
  • amino acid catabolism
  • amino acid metabolism
  • aromatic amino acid family catabolism
  • aromatic amino acid family metabolism
  • biosynthesis
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Amino acid transport and metabolism
Enzyme 7 Specific Function Not Available
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 Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B2R8I1 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2R8I1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK313380 Link Image
Enzyme 7 GeneCard ID B2R8I1 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 16
Enzyme 7 Locus 16q22.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16510
Enzyme 8 Name cDNA, FLJ92196, Homo sapiens macrophage migration inhibitory factor(glycosylation-inhibiting factor) (MIF), mRNA (Macrophage migration inhibitory factor) (Glycosylation-inhibiting factor)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name MIF
Enzyme 8 Protein Sequence >cDNA, FLJ92196, Homo sapiens macrophage migration inhibitory factor(glycosylation-inhibiting factor) (MIF), mRNA (Macrophage migration inhibitory factor) (Glycosylation-inhibiting factor) 
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALC
SLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA
Enzyme 8 Number of Residues 115
Enzyme 8 Molecular Weight 12476
Enzyme 8 Theoretical pI 8.05
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
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 Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B2R4S3 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B2R4S3_HUMAN Link Image
Enzyme 8 PDB ID 1GIF Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK311929 Link Image
Enzyme 8 GeneCard ID B2R4S3 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location 22
Enzyme 8 Locus 22q11.23
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available