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Human Metabolome Database Version 2.5

 

Showing metabocard for 2-Aminobenzoic acid (HMDB01123)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-04 13:45:15
Accession Number HMDB01123
Secondary Accession Numbers Not Available
Common Name 2-Aminobenzoic acid
Description 2-Aminobenzoic acid is an organic compound. It is a substrate of enzyme anthranilate hydroxylase [EC 1.14.13.35] in benzoate degradation via hydroxylation pathway (KEGG).
Synonyms
  1. 1-Amino-2-carboxybenzene
  2. 2-Aminobenzoate
  3. 2-Aminobenzoic acid
  4. 2-Aminophenylacetate
  5. 2-Aminophenylacetic acid
  6. 2-Carboxyaniline
  7. 2-amino-Benzoate
  8. 2-amino-Benzoic acid
  9. Anthranate
  10. Anthranic acid
  11. Anthranilate
  12. Anthranilic acid
  13. Carboxyaniline
  14. H-2-Abz-OH
  15. Kyselina anthranilova
  16. Kyselina o-aminobenzoova
  17. Ortho-amidobenzoate
  18. Ortho-amidobenzoic acid
  19. Ortho-aminobenzoate
  20. Ortho-aminobenzoic acid
  21. Vitamin L
  22. Vitamin L1
  23. anthranilic acid gr
  24. o-Aminobenzoate
  25. o-Aminobenzoic acid
  26. o-Anthranilate
  27. o-Anthranilic acid
  28. o-Carboxyaniline
  29. o-amino-Benzoate
  30. o-amino-Benzoic acid
Chemical IUPAC Name 2-aminobenzoic acid
Chemical Formula C7H7NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
Biofunction
  • Component of Tryptophan metabolism
Application
—
Source
  • Exogenous
Average Molecular Weight 137.136
Monoisotopic Molecular Weight 137.047684
Isomeric SMILES NC1=CC=CC=C1C(O)=O
Canonical SMILES NC1=CC=CC=C1C(O)=O
KEGG Compound ID C00108 Link Image
BioCyc ID ANTHRANILATE Link Image
BiGG ID 33883 Link Image
Wikipedia Link Anthranilic acid Link Image
NuGOwiki Link HMDB01123 Link Image
Metagene Link HMDB01123 Link Image
METLIN ID 6018 Link Image
PubChem Compound 227 Link Image
PubChem Substance 587969 Link Image
ChEBI ID 30754 Link Image
CAS Registry Number 118-92-3
InChI Identifier InChI=1/C7H7NO2/c8-6-4-2-1-3-5(6)7(9)10/h1-4H,8H2,(H,9,10)
Synthesis Reference Wang, Chengyin; Yang, Jisheng; Wang, Honghai. Production of o-aminobenzoic acid from by-product o-nitrobenzoic acid. Huaxue Shijie (1999), 40(5), 274-277.
Melting Point (Experimental) 146.5 oC
Experimental Water Solubility 3.5 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 6.81 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 1.21 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 0.78 [Predicted by ALOGPS]; 1.5 [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 1AN9 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 Not Available
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Epidermis —
Fibroblasts —
Concentrations (Normal)
Biofluid Blood
Value 0.001 +/- 0.000046 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fujigaki S, Saito K, Takemura M, Fujii H, Wada H, Noma A, Seishima M: Species differences in L-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes. Arch Biochem Biophys. 1998 Oct 15;358(2):329-35. [PubMed Link Image]
Biofluid CSF
Value 0.001 +/- 0.00027 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fujigaki S, Saito K, Takemura M, Fujii H, Wada H, Noma A, Seishima M: Species differences in L-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes. Arch Biochem Biophys. 1998 Oct 15;358(2):329-35. [PubMed Link Image]
Biofluid Urine
Value 0.42 (0.15-1.0) umol/mmol creatinine
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 Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Di Marco GS, Quinto BM, Juliano M, Carmona AK, Stella RC, Plavnik FL, Casarini DE: Purification and characterization of a neutral endopeptidase-like enzyme from human urine. J Hypertens. 1998 Dec;16(12 Pt 2):1971-8. [PubMed Link Image]
  2. Hagag N, Birnbaum ER, Darnall DW: Resonance energy transfer between cysteine-34, tryptophan-214, and tyrosine-411 of human serum albumin. Biochemistry. 1983 May 10;22(10):2420-7. [PubMed Link Image]
  3. Little CH, Georgiou GM, Shelton MJ, Simpson F, Cone RE: Clinical and immunological responses in subjects sensitive to solvents. Arch Environ Health. 1999 Jan-Feb;54(1):6-14. [PubMed Link Image]
  4. Calandra P: Research on tryptophan metabolites "via kynurenine" in epidermis of man and mouse. Acta Vitaminol Enzymol. 1975;29(1-6):158-60. [PubMed Link Image]
  5. Ritchie MR, Morton MS, Thompson AM, Deighton N, Blake A, Cummings JH, Steel CM: Investigation of the reliability of 24 h urine excretion as a biomarker of isoflavone exposure over time and over a wide range of isoflavone intakes. Eur J Clin Nutr. 2004 Sep;58(9):1286-9. [PubMed Link Image]
  6. Ortega RM, Andres P, Martinez RM, Lopez-Sobaler AM: Vitamin A status during the third trimester of pregnancy in Spanish women: influence on concentrations of vitamin A in breast milk. Am J Clin Nutr. 1997 Sep;66(3):564-8. [PubMed Link Image]
  7. Alves MF, Araujo MC, Juliano MA, Oliveira EM, Krieger JE, Casarini DE, Juliano L, Carmona AK: A continuous fluorescent assay for the determination of plasma and tissue angiotensin I-converting enzyme activity. Braz J Med Biol Res. 2005 Jun;38(6):861-8. Epub 2005 Jun 1. [PubMed Link Image]
  8. Soma J, Sugawara T, Huang YD, Nakajima J, Kawamura M: Tranilast slows the progression of advanced diabetic nephropathy. Nephron. 2002;92(3):693-8. [PubMed Link Image]
  9. Ahmad S: The functional roles of cytochrome P-450 mediated systems: present knowledge and future areas of investigations. Drug Metab Rev. 1979;10(1):1-14. [PubMed Link Image]
  10. Spivak W, Carey MC: Reverse-phase h.p.l.c. separation, quantification and preparation of bilirubin and its conjugates from native bile. Quantitative analysis of the intact tetrapyrroles based on h.p.l.c. of their ethyl anthranilate azo derivatives. Biochem J. 1985 Feb 1;225(3):787-805. [PubMed Link Image]
  11. Igari T, Tsuchizawa M, Shimamura T: Alteration of tryptophan metabolism in the synovial fluid of patients with rheumatoid arthritis and osteoarthritis. Tohoku J Exp Med. 1987 Oct;153(2):79-86. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Probable arylformamidase
  2. Kynureninase
  3. AFMID protein
Enzyme 1 [top]
Enzyme 1 ID 13059
Enzyme 1 Name Probable arylformamidase
Enzyme 1 Synonyms
  1. Kynurenine formamidase
  2. KF
Enzyme 1 Gene Name AFMID
Enzyme 1 Protein Sequence >Probable arylformamidase 
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNNPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQVLPVQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQ
IILKTIFQ
Enzyme 1 Number of Residues 308
Enzyme 1 Molecular Weight 34556
Enzyme 1 Theoretical pI 5.78
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites
Enzyme 1 Pathways
Enzyme 1 Reactions
  • N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959] ALL_REAC R01959
  • (other) R00988 R04911
Enzyme 1 Pfam Domain Function Not Available
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 52545961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q63HM1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AFMID_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence Not Available
Enzyme 1 GenBank Gene ID BX648442 Link Image
Enzyme 1 GeneCard ID Q63HM1 Link Image
Enzyme 1 GenAtlas ID AFMID Link Image
Enzyme 1 HGNC ID HGNC:20910 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References Not Available
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13118
Enzyme 2 Name Kynureninase
Enzyme 2 Synonyms
  1. L-kynurenine hydrolase
  2. Kynureninase
  3. L-kynurenine hydrolase, isoform CRA_a
Enzyme 2 Gene Name KYNU
Enzyme 2 Protein Sequence >Kynureninase 
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
Enzyme 2 Number of Residues 307
Enzyme 2 Molecular Weight 34635
Enzyme 2 Theoretical pI 5.71
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
  • vitamin binding
Process
  • NAD biosynthesis
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
  • tryptophan catabolism
  • tryptophan metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12654129 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BVW3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q9BVW3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID BC000879 Link Image
Enzyme 2 GeneCard ID Q9BVW3 Link Image
Enzyme 2 GenAtlas ID KYNU Link Image
Enzyme 2 HGNC ID HGNC:6469 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15219
Enzyme 3 Name AFMID protein
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name AFMID
Enzyme 3 Protein Sequence >AFMID protein 
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNSPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQIILKT
IFQ
Enzyme 3 Number of Residues 303
Enzyme 3 Molecular Weight 33992
Enzyme 3 Theoretical pI 5.78
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 124375910 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A2RUB3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A2RUB3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >912 bp 
ATGATGGATGTGTCTGGTGTGGGTTTCCCAAGCAAGGTTCCTTGGAAGAAGATGTCTGCA
GAGGAGCTGGAGAATCAGTACTGTCCCAGCCGATGGGTTGTCCGACTGGGAGCAGAGGAA
GCCTTGAGGACCTACTCACAGATAGGAATTGAAGCCACCACAAGGGCCCGGGCCACCAGG
AAGAGCCTGCTGCATGTCCCCTATGGAGACGGCGAAGGGGAGAAAGTGGACATTTACTTC
CCCGACGAGTCGTCTGAAGCCTTGCCTTTCTTCCTGTTCTTTCACGGAGGATACTGGCAG
AGCGGAAGTAAGGATGAGTCTGCCTTCATGGTCCACCCGCTGACGGCACAGGGAGTGGCC
GTGGTAATAGTGGCTTACGGCATCGCCCCCAAAGGCACCCTGGACCACATGGTAGACCAG
GTGACCCGCAGCGTTGCGTTTGTCCAGAAGCGGTATCCAAGCAACAAGGGAATTTACCTG
TGTGGACACTCAGCCGGGGCCCACCTGGCTGCCATGATGCTCCTGGCCGACTGGACCAAG
CATGGGGTCACGCCCAACCTCAGAGGCTTTTTCCTGGTGAGTGGGGTCTTTGACCTGGAG
CCCATCGTGTATACTTCACAGAACGTTGCTCTCCAGCTGACCCTGGAGGACGCTCAGAGG
AATAGCCCCCAGCTGAAGGTGGCCCAGGCACAGCCGGTGGACCCCACCTGCCGTGTGCTG
GTGGTCGTGGGCCAGTTCGACTCCCCCGAATTCCACCGACAGTCCTGGGAGTTTTACCAG
ACCCTGTGTCAAGGAGAGTGGAAAGCCTCATTTGAAGAGCTCCACGATGTGGACCACTTT
GAAATTGTTGAGAATCTGACCCAGAAGGACAACGTGCTCACCCAGATTATCTTGAAAACA
ATCTTCCAGTAG
Enzyme 3 GenBank Gene ID BC132824 Link Image
Enzyme 3 GeneCard ID A2RUB3 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available