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Human Metabolome Database Version 2.5

 

Showing metabocard for 3,4-Dihydroxymandelic acid (HMDB01866)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-02-23 11:07:11
Update Date 2010-07-13 13:49:29
Accession Number HMDB01866
Secondary Accession Numbers Not Available
Common Name 3,4-Dihydroxymandelic acid
Description 3,4-Dihydroxymandelic acid is is a minor metabolite of norepinephrine in humans (PMID 12649306). Patients with neuroblastoma experience elevated levels of 3,4-Dihydroxymandelic acid and other Catecholamines metabolites, and their presence in urine is a good indicator for diagnosis and follow-up (PMID 8193481)
Synonyms
  1. 3,4 Dihydroxymandelate
  2. 3,4 Dihydroxymandelic acid
  3. 3,4-Dihydroxymandelate
  4. 3,4-Dihydroxyphenylglycolate
  5. 3,4-Dihydroxyphenylglycolic acid
  6. Dihydroxymandelate
  7. Dihydroxymandelic acid
Chemical IUPAC Name 2-(3,4-dihydroxyphenyl)-2-hydroxy-acetic acid
Chemical Formula C8H8O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Hydroxy Acids
Sub Class
  • Miscellaneous catecholamines
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • phenol or hydroxyhetarene
  • 1,2-diphenol
  • carboxylic acid
  • aromatic compound
  • alpha-hydroxyacid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 184.146
Monoisotopic Molecular Weight 184.037170
Isomeric SMILES OC(C(O)=O)C1=CC=C(O)C(O)=C1
Canonical SMILES OC(C(O)=O)C1=CC=C(O)C(O)=C1
KEGG Compound ID C07470 Link Image
BioCyc ID Not Available
BiGG ID 46062 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01866 Link Image
Metagene Link HMDB01866 Link Image
METLIN ID 696 Link Image
PubChem Compound 85782 Link Image
PubChem Substance 10221499 Link Image
ChEBI ID Not Available
CAS Registry Number 775-01-9
InChI Identifier InChI=1/C8H8O5/c9-5-2-1-4(3-6(5)10)7(11)8(12)13/h1-3,7,9-11H,(H,12,13)
Synthesis Reference Joray, Marcel; Breuninger, Manfred. Process for the preparation of phenolic compounds. PCT Int. Appl. (2007), 15pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 10.7 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.72 [Predicted by ALOGPS]; 0.062 [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
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High Energy
Download File
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Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Nerve Cells —
Concentrations (Normal)
Biofluid Blood
Value 0.011 +/- 0.004 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Izzo JL Jr, Greulich D: Radioenzymatic assay for plasma dihydroxyphenylglycol (DHPG), dihydroxymandelic acid (DOMA) and dihydroxyphenylacetic acid (DOPAC). Life Sci. 1983 Aug 1;33(5):483-8. [PubMed Link Image]
Biofluid Urine
Value 0.12 +/- 0.05 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. 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
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. O'Meara A, Tormey W, FitzGerald RJ, Fitzgibbon M, Kenny D: Interpretation of random urinary catecholamines and their metabolites in neuroblastoma. Acta Paediatr. 1994 Jan;83(1):88-92. [PubMed Link Image]
  2. Eisenhofer G, Kopin IJ, Goldstein DS: Catecholamine metabolism: a contemporary view with implications for physiology and medicine. Pharmacol Rev. 2004 Sep;56(3):331-49. [PubMed Link Image]
  3. Zambotti F, Blau K, King GS, Campbell S, Sandler M: Monoamine metabolites and related compounds in human amniotic fluid: assay by gas chromatography and gas chromatography-mass spectrometry. Clin Chim Acta. 1975 Jun 20;61(3):247-56. [PubMed Link Image]
  4. Nohta H, Yamaguchi E, Ohkura Y, Watanabe H: Measurement of catecholamines, their precursor and metabolites in human urine and plasma by solid-phase extraction followed by high-performance liquid chromatography with fluorescence derivatization. J Chromatogr. 1989 Aug 25;493(1):15-26. [PubMed Link Image]
  5. Odink J, Korthals H, Knijff JH: Simultaneous determination of the major acidic metabolites of catecholamines and serotonin in urine by liquid chromatography with electrochemical detection after a one-step sample clean-up on Sephadex G-10; influence of vanilla and banana ingestion. J Chromatogr. 1988 Feb 26;424(2):273-83. [PubMed Link Image]
Metabolic Enzymes
  1. Catechol O-methyltransferase
  2. Aldehyde dehydrogenase, dimeric NADP-preferring
Enzyme 1 [top]
Enzyme 1 ID 5504
Enzyme 1 Name Catechol O-methyltransferase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name COMT
Enzyme 1 Protein Sequence >Catechol O-methyltransferase 
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
Enzyme 1 Number of Residues 271
Enzyme 1 Molecular Weight 30037
Enzyme 1 Theoretical pI 5.15
Enzyme 1 GO Classification
Function
  • O-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-32
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 180920 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P21964 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name COMT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >816 bp 
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
Enzyme 1 GenBank Gene ID M65212 Link Image
Enzyme 1 GeneCard ID COMT Link Image
Enzyme 1 GenAtlas ID COMT Link Image
Enzyme 1 HGNC ID HGNC:2228 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q11.21-q11.23|22q11.21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Lundstrom K, Salminen M, Jalanko A, Savolainen R, Ulmanen I: Cloning and characterization of human placental catechol-O-methyltransferase cDNA. DNA Cell Biol. 1991 Apr;10(3):181-9. [PubMed Link Image]
  2. Bertocci B, Miggiano V, Da Prada M, Dembic Z, Lahm HW, Malherbe P: Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1416-20. [PubMed Link Image]
  3. Tenhunen J, Salminen M, Lundstrom K, Kiviluoto T, Savolainen R, Ulmanen I: Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters. Eur J Biochem. 1994 Aug 1;223(3):1049-59. [PubMed Link Image]
  4. Tilgmann C, Kalkkinen N: Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme. Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002. [PubMed Link Image]
  5. Ulmanen I, Lundstrom K: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur J Biochem. 1991 Dec 18;202(3):1013-20. [PubMed Link Image]
  6. Lachman HM, Papolos DF, Saito T, Yu YM, Szumlanski CL, Weinshilboum RM: Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics. 1996 Jun;6(3):243-50. [PubMed Link Image]
  7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5527
Enzyme 2 Name Aldehyde dehydrogenase, dimeric NADP-preferring
Enzyme 2 Synonyms
  1. ALDH class 3
  2. ALDHIII
Enzyme 2 Gene Name ALDH3A1
Enzyme 2 Protein Sequence >Aldehyde dehydrogenase, dimeric NADP-preferring 
MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAY
YEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNL
TIQPMVGAIAAGNAVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKER
FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNS
GQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEG
QKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREK
PLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFE
TFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH
Enzyme 2 Number of Residues 453
Enzyme 2 Molecular Weight 50380
Enzyme 2 Theoretical pI 6.52
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes
Enzyme 2 Pathways
Enzyme 2 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 178402 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P30838 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AL3A1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1362 bp 
ATGAGCAAGATCAGCGAGGCCGTGAAGCGCGCCCGCGCCGCCTTCAGCTCGGGCAGGACC
CGTCCGCTGCAGTTCCGATTCCAGCAGCTGGAGGCGCTGCAGCGCCTGATCCAGGAGCAG
GAGCAGGAGCTGGTGGGCGCGCTGGCCGCAGACCTGCACAAGAATGAATGGAACGCCTAC
TATGAGGAGGTGGTGTACGTCCTAGAGGAGATCGAGTACATGATCCAGAAGCTCCCTGAG
TGGGCCGCGGATGAGCCCGTGGAGAAGACGCCCCAGACTCAGCAGGACGAGCTCTACATC
CACTCGGAGCCACTGGGCGTGGTCCTCGTCATTGGCACCTGGAACTACCCCTTCAACCTC
ACCATCCAGCCCATGGTGGGCGCCATCGCTGCAGGGAACGCAGTGGTCCTCAAGCCCTCG
GAGCTGAGTGAGAACATGGCGAGCCTGCTGGCTACCATCATCCCCCAGTACCTGGACAAG
GATCTGTACCCAGTAATCAATGGGGGTGTCCCTGAGACCACGGAGCTGCTCAAGGAGAGG
TTCGACCATATCCTGTACACGGGCAGCACGGGGGTGGGGAAGATCATCATGACGGCTGCT
GCCAAGCACCTGACCCCTGTCACGCTGGAGCTGGGAGGGAAGAGTCCCTGCTACGTGGAC
AAGAACTGTGACCTGGACGTGGCCTGCCGACGCATCGCCTGGGGGAAATTCATGAACAGT
GGCCAGACCTGCGTGGCCCCAGACTACATCCTCTGTGACCCCTCGATCCAGAACCAAATT
GTGGAGAAGCTCAAGAAGTCACTGAAAGAGTTCTACGGGGAAGATGCTAAGAAATCCCGG
GACTATGGAAGAATCATTAGTGCCCGGCACTTCCAGAGGGTGATGGGCCTGATTGAGGGC
CAGAAGGTGGCTTATGGGGGCACCGGGGATGCCGCCACTCGCTACATAGCCCCCACCATC
CTCACGGACGTGGACCCCCAGTCCCCGGTGATGCAAGAGGAGATCTTCGGGCCTGTGCTG
CCCATCGTGTGCGTGCGCAGCCTGGAGGAGGCCATCCAGTTCATCAACCAGCGTGAGAAG
CCCCTGGCCCTCTACATGTTCTCCAGCAACGACAAGGTGATTAAGAAGATGATTGCAGAG
ACATCCAGTGGTGGGGTGGCGGCCAACGATGTCATCGTCCACATCACCTTGCACTCTCTG
CCCTTCGGGGGCGTGGGGAACAGCGGCATGGGATCCTACCATGGCAAGAAGAGCTTCGAG
ACTTTCTCTCACCGCCGCTCTTGCCTGGTGAGGCCTCTGATGAATGATGAAGGCCTGAAG
GTCAGATACCCCCCGAGCCCGGCCAAGATGACCCAGCACTGA
Enzyme 2 GenBank Gene ID M74542 Link Image
Enzyme 2 GeneCard ID ALDH3A1 Link Image
Enzyme 2 GenAtlas ID ALDH3A1 Link Image
Enzyme 2 HGNC ID HGNC:405 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17p11.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hsu LC, Chang WC, Shibuya A, Yoshida A: Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli. J Biol Chem. 1992 Feb 15;267(5):3030-7. [PubMed Link Image]
  2. Hsu LC, Yoshida A: Human stomach aldehyde dehydrogenase, ALDH3. Adv Exp Med Biol. 1993;328:141-52. [PubMed Link Image]
  3. Yin SJ, Vagelopoulos N, Wang SL, Jornvall H: Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families. FEBS Lett. 1991 May 20;283(1):85-8. [PubMed Link Image]
  4. Tsukamoto N, Chang C, Yoshida A: Mutations associated with Sjogren-Larsson syndrome. Ann Hum Genet. 1997 May;61(Pt 3):235-42. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available