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Human Metabolome Database Version 2.5

 

Showing metabocard for 4-Hydroxyphenylpyruvic acid (HMDB00707)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-05-20 04:00:50
Accession Number HMDB00707
Secondary Accession Numbers Not Available
Common Name 4-Hydroxyphenylpyruvic acid
Description 4-Hydroxyphenylpyruvic acid (4-HPPA) is a keto acid. It is a product of the enzyme (R)-4-hydroxyphenyllactate dehydrogenase [EC 1.1.1.222] and is formed during tyrosine metabolism (KEGG). There are two isomers of HPPA, specifically 4HPPA and 3HPPA, of which 4HPPA is the most common. The enzyme 4-hydroxyphenylpyruvic acid dioxygenase (HPD) catalyzes the reaction of 4-hydroxyphenylpyruvic acid to homogentisic acid in the tyrosine catabolism pathway. A deficiency in the catalytic activity of HPD is known to lead to tyrosinemia type III, an autosomal recessive disorder characterized by elevated levels of blood tyrosine and massive excretion of tyrosine derivatives into urine. It has been shown that hawkinsinuria, an autosomal dominant disorder characterized by the excretion of 'hawkinsin,' may also be a result of HPD deficiency (PMID: 11073718).
Synonyms
  1. (p-Hydroxyphenyl)pyruvate
  2. Hydroxyphenylpyruvic acid
  3. (p-Hydroxyphenyl)pyruvic acid
  4. (p-hydroxyphenyl)-Pyruvate
  5. (p-hydroxyphenyl)-Pyruvic acid
  6. 3-(4-Hydroxyphenyl)-2-oxopropionate
  7. 3-(4-Hydroxyphenyl)-2-oxopropionic acid
  8. 3-(4-Hydroxyphenyl)pyruvate
  9. 3-(4-Hydroxyphenyl)pyruvic acid
  10. 3-(p-Hydroxyphenyl)-2-oxopropionate
  11. 3-(p-Hydroxyphenyl)-2-oxopropionic acid
  12. 3-(p-Hydroxyphenyl)pyruvate
  13. 3-(p-Hydroxyphenyl)pyruvic acid
  14. 4-Hydroxy-a-oxobenzenepropanoate
  15. 4-Hydroxy-a-oxobenzenepropanoic acid
  16. 3-(4-hydroxyphenyl)-2-oxo-propanoic acid
  17. 4-hydroxyphenylpyruvate
  18. HPPA
  19. 4HPPA
  20. Hydroxyphenylpyruvate
  21. Testacid
  22. p-hydroxyphenylpyruvic
  23. 4-Hydroxy-alpha-oxobenzenepropanoate
  24. 4-Hydroxy-alpha-oxobenzenepropanoic acid
  25. 3-(4-hydroxyphenyl)-2-oxo-propanoate
Chemical IUPAC Name 4-hydroxy-a-oxo-benzenepropanoic acid
Chemical Formula C9H8O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Aromatic Acids
Sub Class
  • Miscellaneous aromatic acids
Family
  • Mammalian Metabolite
Species
  • ketone
  • phenol or hydroxyhetarene
  • carboxylic acid
  • aromatic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 180.157
Monoisotopic Molecular Weight 180.042252
Isomeric SMILES OC(=O)C(=O)CC1=CC=C(O)C=C1
Canonical SMILES OC(=O)C(=O)CC1=CC=C(O)C=C1
KEGG Compound ID C01179 Link Image
BioCyc ID P-HYDROXY-PHENYLPYRUVATE Link Image
BiGG ID 37006 Link Image
Wikipedia Link Hydroxyphenylpyruvic acid Link Image
NuGOwiki Link HMDB00707 Link Image
Metagene Link HMDB00707 Link Image
METLIN ID 5675 Link Image
PubChem Compound 979 Link Image
PubChem Substance 3043 Link Image
ChEBI ID Not Available
CAS Registry Number 156-39-8
InChI Identifier InChI=1/C9H8O4/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,10H,5H2,(H,12,13)
Synthesis Reference Billek, Gerhard. p-Hydroxyphenylpyruvic acid. Organic Syntheses (1963), 43 49-54.
Melting Point (Experimental) 219-220 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.49 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.12 [Predicted by ALOGPS]; 0.7 [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 Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.37 +/- 0.23 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Deutsch JC: Determination of p-hydroxyphenylpyruvate, p-hydroxyphenyllactate and tyrosine in normal human plasma by gas chromatography-mass spectrometry isotope-dilution assay. J Chromatogr B Biomed Sci Appl. 1997 Mar 7;690(1-2):1-6. [PubMed Link Image]
Biofluid Urine
Value 1.65 (0.15-8.74) 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 0.66 (0.23-2.50) 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 4.6 (0.1-21.3) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.8 (0.1-4.5) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Children aged 2-6 years
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.5 (0.6-3.4) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Children aged 6-10 years
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.8 (1.2-4.3) umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Children >10 years old
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 4.9 (4.9-4.9) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.00 (0.00-2.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Urine
Value 885.00 (170.00-1600.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Hawkinsinuria
Comments Not Available
References
Biofluid Urine
Value 24.00 +/- 30.5 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
Hawkinsinuria
Phenylketonuria
  • 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]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Phenylalanine and Tyrosine Metabolism SMP00008 Link Image map00360 Link Image
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. Shoda J, Tanaka N, Osuga T, Matsuura K, Miyazaki H: Altered bile acid metabolism in liver disease: concurrent occurrence of C-1 and C-6 hydroxylated bile acid metabolites and their preferential excretion into urine. J Lipid Res. 1990 Feb;31(2):249-59. [PubMed Link Image]
  2. Wolff JA, Barshop B, Nyhan WL, Leslie J, Seegmiller JE, Gruber H, Garst M, Winter S, Michals K, Matalon R: Effects of ascorbic acid in alkaptonuria: alterations in benzoquinone acetic acid and an ontogenic effect in infancy. Pediatr Res. 1989 Aug;26(2):140-4. [PubMed Link Image]
  3. Deutsch JC: Determination of p-hydroxyphenylpyruvate, p-hydroxyphenyllactate and tyrosine in normal human plasma by gas chromatography-mass spectrometry isotope-dilution assay. J Chromatogr B Biomed Sci Appl. 1997 Mar 7;690(1-2):1-6. [PubMed Link Image]
  4. Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
  5. Muskiet FA, Fremouw-Ottevangers DC, Nagel GT, Wolthers BG, de Vries JA: Determination of 3-methoxy-4-hydroxyphenylpyruvic acid, 3,4-dihydroxyphenylethylene glycol, and 3,4-dihydroxyphenylmandelic acid in urine by mass fragmentography, with use of deuterium-labeled internal standards. Clin Chem. 1978 Nov;24(11):2001-8. [PubMed Link Image]
  6. Endo F, Katoh H, Yamamoto S, Matsuda I: A murine model for type III tyrosinemia: lack of immunologically detectable 4-hydroxyphenylpyruvic acid dioxygenase enzyme protein in a novel mouse strain with hypertyrosinemia. Am J Hum Genet. 1991 Apr;48(4):704-9. [PubMed Link Image]
  7. Wikipedia Link Image
Metabolic Enzymes
  1. Macrophage migration inhibitory factor
  2. Aspartate aminotransferase, mitochondrial precursor
  3. 4-hydroxyphenylpyruvate dioxygenase
  4. cDNA FLJ76150, highly similar to Homo sapiens 4-hydroxyphenylpyruvate dioxygenase
  5. 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)
  6. cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
  7. 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 5332
Enzyme 1 Name Macrophage migration inhibitory factor
Enzyme 1 Synonyms
  1. MIF
  2. Phenylpyruvate tautomerase
  3. Glycosylation-inhibiting factor
  4. GIF
Enzyme 1 Gene Name MIF
Enzyme 1 Protein Sequence >Macrophage migration inhibitory factor 
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALC
SLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA
Enzyme 1 Number of Residues 115
Enzyme 1 Molecular Weight 12476
Enzyme 1 Theoretical pI 8.05
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function The expression of MIF at sites of inflammation suggest a role for the mediator in regulating the function of macrophage in host defense. Also acts as a phenylpyruvate tautomerase
Enzyme 1 Pathways
Enzyme 1 Reactions
  • keto-phenylpyruvate = enol-phenylpyruvate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 188556 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P14174 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name MIF_HUMAN Link Image
Enzyme 1 PDB ID 1GIF Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >348 bp 
ATGCCGATGTTCATCGTAAACACCAACGTGCCCCGCGCCTCCGTGCCGGACGGGTTCCTC
TCCGAGCTCACCCAGCAGCTGGCGCAGGCCACCGGCAAGCCCCCCCAGTACATCGCGGTG
CACGTGGTCCCGGACCAGCTCATGGCCTTCGGCGGCTCCAGCGAGCCGTGCGCGCTCTGC
AGCCTGCACAGCATCGGCAAGATCGGCGGCGCGCAGAACCGCTCCTACAGCAAGCTGCTG
TGCGGCCTGCTGGCCGAGCGCCTGCGCATCAGCCCGGACAGGGTCTACATCAACTATTAC
GACATGAACGCGGCCAGTGTGGGCTGGAACAACTCCACCTTCGCCTAA
Enzyme 1 GenBank Gene ID M25639 Link Image
Enzyme 1 GeneCard ID MIF Link Image
Enzyme 1 GenAtlas ID MIF Link Image
Enzyme 1 HGNC ID HGNC:7097 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q11.23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Weiser WY, Temple PA, Witek-Giannotti JS, Remold HG, Clark SC, David JR: Molecular cloning of a cDNA encoding a human macrophage migration inhibitory factor. Proc Natl Acad Sci U S A. 1989 Oct;86(19):7522-6. [PubMed Link Image]
  2. Mikayama T, Nakano T, Gomi H, Nakagawa Y, Liu YC, Sato M, Iwamatsu A, Ishii Y, Weiser WY, Ishizaka K: Molecular cloning and functional expression of a cDNA encoding glycosylation-inhibiting factor. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10056-60. [PubMed Link Image]
  3. Paralkar V, Wistow G: Cloning the human gene for macrophage migration inhibitory factor (MIF). Genomics. 1994 Jan 1;19(1):48-51. [PubMed Link Image]
  4. Bernhagen J, Mitchell RA, Calandra T, Voelter W, Cerami A, Bucala R: Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF). Biochemistry. 1994 Nov 29;33(47):14144-55. [PubMed Link Image]
  5. Wistow GJ, Shaughnessy MP, Lee DC, Hodin J, Zelenka PS: A macrophage migration inhibitory factor is expressed in the differentiating cells of the eye lens. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1272-5. [PubMed Link Image]
  6. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  7. Zeng FY, Weiser WY, Kratzin H, Stahl B, Karas M, Gabius HJ: The major binding protein of the interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor. Arch Biochem Biophys. 1993 May 15;303(1):74-80. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Kleemann R, Hausser A, Geiger G, Mischke R, Burger-Kentischer A, Flieger O, Johannes FJ, Roger T, Calandra T, Kapurniotu A, Grell M, Finkelmeier D, Brunner H, Bernhagen J: Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1. Nature. 2000 Nov 9;408(6809):211-6. [PubMed Link Image]
  10. Shen L, Hu J, Lu H, Wu M, Qin W, Wan D, Li YY, Gu J: The apoptosis-associated protein BNIPL interacts with two cell proliferation-related proteins, MIF and GFER. FEBS Lett. 2003 Apr 10;540(1-3):86-90. [PubMed Link Image]
  11. Sugimoto H, Suzuki M, Nakagawa A, Tanaka I, Nishihira J: Crystal structure of macrophage migration inhibitory factor from human lymphocyte at 2.1 A resolution. FEBS Lett. 1996 Jul 1;389(2):145-8. [PubMed Link Image]
  12. Kato Y, Muto T, Tomura T, Tsumura H, Watarai H, Mikayama T, Ishizaka K, Kuroki R: The crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded beta-sheets. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3007-10. [PubMed Link Image]
  13. Sun HW, Bernhagen J, Bucala R, Lolis E: Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5191-6. [PubMed Link Image]
  14. Lubetsky JB, Swope M, Dealwis C, Blake P, Lolis E: Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity. Biochemistry. 1999 Jun 1;38(22):7346-54. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5516
Enzyme 2 Name Aspartate aminotransferase, mitochondrial precursor
Enzyme 2 Synonyms
  1. Transaminase A
  2. Glutamate oxaloacetate transaminase 2
Enzyme 2 Gene Name GOT2
Enzyme 2 Protein Sequence >Aspartate aminotransferase, mitochondrial precursor 
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKGMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
Enzyme 2 Number of Residues 430
Enzyme 2 Molecular Weight 47476
Enzyme 2 Theoretical pI 9.38
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
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 179104 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00505 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AATM_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID M22632 Link Image
Enzyme 2 GeneCard ID GOT2 Link Image
Enzyme 2 GenAtlas ID GOT2 Link Image
Enzyme 2 HGNC ID HGNC:4433 Link Image
Enzyme 2 Chromosome Location 16
Enzyme 2 Locus 16q21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6122
Enzyme 3 Name 4-hydroxyphenylpyruvate dioxygenase
Enzyme 3 Synonyms
  1. 4HPPD
  2. HPD
  3. HPPDase
  4. 4-hydroxyphenylpyruvic acid oxidase
Enzyme 3 Gene Name HPD
Enzyme 3 Protein Sequence >4-hydroxyphenylpyruvate dioxygenase 
MTTYSDKGAKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSH
VIKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMRE
PWVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEM
IDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPI
NEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLR
EKLKTAKIKVKENIDALEELKILVDYDEKGYLLQIFTKPVQDRPTLFLEVIQRHNHQGFG
AGNFNSLFKAFEEEQNLRGNLTNMETNGVVPGM
Enzyme 3 Number of Residues 393
Enzyme 3 Molecular Weight 44935
Enzyme 3 Theoretical pI 7.01
Enzyme 3 GO Classification
Function
  • 4-hydroxyphenylpyruvate dioxygenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function 4-hydroxyphenylpyruvate + O(2) = homogentisate + CO(2)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 3860238 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P32754 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HPPD_HUMAN Link Image
Enzyme 3 PDB ID 1SQI Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1182 bp 
ATGACGACTTACAGTGACAAAGGGGCAAAGCCTGAGAGAGGCCGATTCCTCCACTTCCAC
TCTGTGACCTTCTGGGTTGGCAACGCCAAGCAGGCCGCGTCATTCTACTGCAGCAAGATG
GGCTTTGAACCTCTAGCCTACAGGGGCCTGGAGACCGGTTCCCGGGAGGTGGTCAGCCAT
GTAATCAAACAAGGGAAGATTGTGTTTGTCCTCTCCTCAGCGCTCAACCCCTGGAACAAA
GAGATGGGCGATCACCTGGTGAAACACGGTGACGGAGTGAAGGACATTGCGTTCGAGGTG
GAAGATTGTGACTACATCGTGCAGAAAGCACGGGAACGGGGCGCCAAAATCATGCGGGAG
CCCTGGGTAGAGCAAGACAAGTTTGGGAAGGTGAAGTTTGCTGTGCTGCAGACGTATGGG
GACACCACACACACCCTGGTGGAGAAGATGAACTACATCGGCCAATTCTTGCCTGGATAT
GAGCCCCCAGCGTTCATGGACCCCCTACTTCCTAAACTGCCCAAATGCAGTCTGGAGATG
ATCGACCACATTGTGGGAAACCAGCCTGATCAGGAGATGGTGTCCGCCTCCGAATGGTAC
CTGAAAAACCTGCAGTTCCACCGCTTCTGGTCCGTGGATGACACGCAGGTGCACACGGAA
TATAGCTCTCTGCGATCCATTGTGGTGGCCAACTATGAAGAGTCCATCAAGATGCCCATC
AATGAGCCAGCGCCTGGCAAGAAGAAGTCCCAGATCCAGGAATATGTGGACTATAACGGG
GGCGCTGGGGTCCAGCACATCGCTCTCAAGACCGAAGACATCATCACAGCGATTCGCCAC
TTGAGAGAGAGAGGCCTGGAGTTCTTATCTGTTCCCTCCACGTACTACAAACAACTGCGG
GAGAAGCTGAAGACGGCCAAGATCAAGGTGAAGGAGAACATTGATGCCCTGGAGGAGCTG
AAAATCCTGGTGGACTACGACGAGAAAGGCTACCTCCTGCAGATCTTCACCAAACCGGTG
CAGGACCGGCCCACGCTCTTCCTGGAAGTCATCCAGCGCCACAACCACCAGGGTTTTGGA
GCCGGCAACTTCAACTCACTGTTCAAGGCTTTCGAGGAGGAGCAGAACCTGCGGGGTAAC
CTCACCAACATGGAGACCAATGGGGTGGTGCCCGGCATGTAA
Enzyme 3 GenBank Gene ID U29895 Link Image
Enzyme 3 GeneCard ID HPD Link Image
Enzyme 3 GenAtlas ID HPD Link Image
Enzyme 3 HGNC ID HGNC:5147 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12q24-qter
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ruetschi U, Dellsen A, Sahlin P, Stenman G, Rymo L, Lindstedt S: Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene. Eur J Biochem. 1993 May 1;213(3):1081-9. [PubMed Link Image]
  2. Awata H, Endo F, Matsuda I: Structure of the human 4-hydroxyphenylpyruvic acid dioxygenase gene (HPD). Genomics. 1994 Oct;23(3):534-9. [PubMed Link Image]
  3. Stenman G, Roijer E, Ruetschi U, Dellsen A, Rymo L, Lindstedt S: Regional assignment of the human 4-hydroxyphenylpyruvate dioxygenase gene (HPD) to 12q24-->qter by fluorescence in situ hybridization. Cytogenet Cell Genet. 1995;71(4):374-6. [PubMed Link Image]
  4. Ruetschi U, Cerone R, Perez-Cerda C, Schiaffino MC, Standing S, Ugarte M, Holme E: Mutations in the 4-hydroxyphenylpyruvate dioxygenase gene (HPD) in patients with tyrosinemia type III. Hum Genet. 2000 Jun;106(6):654-62. [PubMed Link Image]
  5. Tomoeda K, Awata H, Matsuura T, Matsuda I, Ploechl E, Milovac T, Boneh A, Scott CR, Danks DM, Endo F: Mutations in the 4-hydroxyphenylpyruvic acid dioxygenase gene are responsible for tyrosinemia type III and hawkinsinuria. Mol Genet Metab. 2000 Nov;71(3):506-10. [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 16502
Enzyme 5 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 5 Synonyms Not Available
Enzyme 5 Gene Name GOT1
Enzyme 5 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 5 Number of Residues 413
Enzyme 5 Molecular Weight 46248
Enzyme 5 Theoretical pI 7.01
Enzyme 5 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 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
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B2R6R7 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B2R6R7_HUMAN Link Image
Enzyme 5 PDB ID 1AJS Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK312684 Link Image
Enzyme 5 GeneCard ID B2R6R7 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q24.1-q25.1
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 16503
Enzyme 6 Name cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name TAT
Enzyme 6 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 6 Number of Residues 454
Enzyme 6 Molecular Weight 50400
Enzyme 6 Theoretical pI 6.24
Enzyme 6 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 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 B2R8I1 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2R8I1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK313380 Link Image
Enzyme 6 GeneCard ID B2R8I1 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 16
Enzyme 6 Locus 16q22.1
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 16510
Enzyme 7 Name cDNA, FLJ92196, Homo sapiens macrophage migration inhibitory factor(glycosylation-inhibiting factor) (MIF), mRNA (Macrophage migration inhibitory factor) (Glycosylation-inhibiting factor)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name MIF
Enzyme 7 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 7 Number of Residues 115
Enzyme 7 Molecular Weight 12476
Enzyme 7 Theoretical pI 8.05
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
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 B2R4S3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2R4S3_HUMAN Link Image
Enzyme 7 PDB ID 1GIF Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK311929 Link Image
Enzyme 7 GeneCard ID B2R4S3 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 22
Enzyme 7 Locus 22q11.23
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available