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Human Metabolome Database Version 2.5

 

Showing metabocard for 3-Mercaptolactic acid (HMDB02127)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:37
Update Date 2009-05-05 20:59:12
Accession Number HMDB02127
Secondary Accession Numbers Not Available
Common Name 3-Mercaptolactic acid
Description 3-Mercaptolactic acid is a thiol that has been confirmed to be found in urine (PMID 8852041).
Synonyms
  1. 3-mercaptolactate
  2. b-Mercaptolactate
  3. b-Mercaptolactic acid
  4. beta-Mercaptolactate
  5. beta-Mercaptolactic acid
Chemical IUPAC Name 2-hydroxy-3-sulfanyl-propanoate
Chemical Formula C3H6O3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Hydroxy Acids
Sub Class
  • Short chain hydroxy acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • thiol (sulfanyl compound)
  • alkylthiol
  • alpha-hydroxyacid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 122.143
Monoisotopic Molecular Weight 122.003761
Isomeric SMILES OC(CS)C(O)=O
Canonical SMILES OC(CS)C(O)=O
KEGG Compound ID C05823 Link Image
BioCyc ID Not Available
BiGG ID 46576 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB02127 Link Image
Metagene Link HMDB02127 Link Image
METLIN ID 6499 Link Image
PubChem Compound 440803 Link Image
PubChem Substance 8118 Link Image
ChEBI ID Not Available
CAS Registry Number 2614-83-7
InChI Identifier InChI=1/C3H6O3S/c4-2(1-7)3(5)6/h2,4,7H,1H2,(H,5,6)
Synthesis Reference Costa, Mara; Pensa, Bernardo; Iavarone, Carlo; Cavallini, Doriano. Preparation of 3-mercaptolactic acid and S-aminoethylmercaptolactic acid. Preparative Biochemistry (1982), 12(5), 417-27.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 28.800001 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.33 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Cysteine Metabolism SMP00013 Link Image map00270 Link Image
General References
  1. Hannestad U, Sorbo B: Determination of 3-mercaptolactate, mercaptoacetate and N-acetylcysteine in urine by gas chromatography. Clin Chim Acta. 1979 Jul 16;95(2):189-200. [PubMed Link Image]
  2. Wronski M: Separation of urinary thiols as tributyltinmercaptides and determination using capillary isotachophoresis. J Chromatogr B Biomed Appl. 1996 Feb 9;676(1):29-34. [PubMed Link Image]
Metabolic Enzymes
  1. L-lactate dehydrogenase B chain
  2. L-lactate dehydrogenase C chain
  3. L-lactate dehydrogenase A-like 6B
  4. L-lactate dehydrogenase A-like 6A
  5. cDNA FLJ54086, moderately similar to L-lactate dehydrogenase A chain (EC 1.1.1.27)
Enzyme 1 [top]
Enzyme 1 ID 5791
Enzyme 1 Name L-lactate dehydrogenase B chain
Enzyme 1 Synonyms
  1. LDH-B
  2. LDH heart subunit
  3. LDH-H
  4. Renal carcinoma antigen NY-REN-46
Enzyme 1 Gene Name LDHB
Enzyme 1 Protein Sequence >L-lactate dehydrogenase B chain 
MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLK
GEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKF
IIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLG
IHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAY
EVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARG
LTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
Enzyme 1 Number of Residues 334
Enzyme 1 Molecular Weight 36639
Enzyme 1 Theoretical pI 5.93
Enzyme 1 GO Classification
Function
  • L-lactate dehydrogenase activity
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
Process
  • alcohol metabolism
  • anaerobic glycolysis
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • main pathways of carbohydrate metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
  • tricarboxylic acid cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function (S)-lactate + NAD(+) = pyruvate + NADH
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1200083 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P07195 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LDHB_HUMAN Link Image
Enzyme 1 PDB ID 1I0Z Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >129 bp 
ATGGCAACTCTTAAGGAAAAACTCATTGCACCAGTTGCGGAAGAAGAGGCAACAGTTCCA
AACAATAAGATCACTGTAGTGGGTGTTGGACAAGTTGGTATGGCGTGTGCTATCAGCATT
CTGGGAAAG
Enzyme 1 GenBank Gene ID X13794 Link Image
Enzyme 1 GeneCard ID LDHB Link Image
Enzyme 1 GenAtlas ID LDHB Link Image
Enzyme 1 HGNC ID HGNC:6541 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12p12.2-p12.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Takeno T, Li SS: Structure of the human lactate dehydrogenase B gene. Biochem J. 1989 Feb 1;257(3):921-4. [PubMed Link Image]
  2. Sakai I, Sharief FS, Pan YC, Li SS: The cDNA and protein sequences of human lactate dehydrogenase B. Biochem J. 1987 Dec 15;248(3):933-6. [PubMed Link Image]
  3. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  4. Maekawa M, Sudo K, Kitajima M, Matsuura Y, Li SS, Kanno T: Analysis of a genetic mutation in an electrophoretic variant of the human lactate dehydrogenase-B(H) subunit. Hum Genet. 1993 Jun;91(5):423-6. [PubMed Link Image]
  5. Maekawa M, Sudo K, Kitajima M, Matsuura Y, Li SS, Kanno T: Detection and characterization of new genetic mutations in individuals heterozygous for lactate dehydrogenase-B(H) deficiency using DNA conformation polymorphism analysis and silver staining. Hum Genet. 1993 Mar;91(2):163-8. [PubMed Link Image]
  6. Sudo K, Maekawa M, Tomonaga A, Tsukada T, Nakayama T, Kitamura M, Li SS, Kanno T, Toriumi J: Molecular characterization of genetic mutations in human lactate dehydrogenase (LDH) B (H) variant. Hum Genet. 1992 May;89(2):158-62. [PubMed Link Image]
  7. Sudo K, Maekawa M, Ikawa S, Machida K, Kitamura M, Li SS: A missense mutation found in human lactate dehydrogenase-B (H) variant gene. Biochem Biophys Res Commun. 1990 Apr 30;168(2):672-6. [PubMed Link Image]
  8. Shonnard GC, Hud NV, Mohrenweiser HW: Arginine to tryptophan substitution in the active site of a human lactate dehydrogenase variant--LDHB GUA1: postulated effects on subunit structure and catalysis. Biochim Biophys Acta. 1996 Jan 17;1315(1):9-14. [PubMed Link Image]
  9. Sudo K, Maekawa M, Houki N, Okuda T, Akizuki S, Magara T, Kawano K: A novel in-frame deletion mutation in a case of lactate dehydrogenase (LD) H subunit deficiency showing an atypical LD isoenzyme pattern in serum and erythrocytes. Clin Biochem. 1999 Mar;32(2):137-41. [PubMed Link Image]
  10. Hidaka K, Ueda N, Hirata I, Watanabe Y, Minatogawa Y, Iuchi I: First case of missense mutation (LDH-H:R171P) in exon 4 of the lactate dehydrogenase gene detected in a Japanese patient. J Hum Genet. 1999;44(1):69-72. [PubMed Link Image]
  11. Takatani T, Takaoka N, Tatsumi M, Kawamoto H, Okuno Y, Morita K, Masutani T, Murakawa K, Okamoto Y: A novel missense mutation in human lactate dehydrogenase B-subunit gene. Mol Genet Metab. 2001 Aug;73(4):344-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5792
Enzyme 2 Name L-lactate dehydrogenase C chain
Enzyme 2 Synonyms
  1. LDH-C
  2. LDH testis subunit
  3. LDH-X
Enzyme 2 Gene Name LDHC
Enzyme 2 Protein Sequence >L-lactate dehydrogenase C chain 
MSTVKEQLIEKLIEDDENSQCKITIVGTGAVGMACAISILLKDLADELALVDVALDKLKG
EMMDLQHGSLFFSTSKITSGKDYSVSANSRIVIVTAGARQQEGETRLALVQRNVAIMKSI
IPAIVHYSPDCKILVVSNPVDILTYIVWKISGLPVTRVIGSGCNLDSARFRYLIGEKLGV
HPTSCHGWIIGEHGDSSVPLWSGVNVAGVALKTLDPKLGTDSDKEHWKNIHKQVIQSAYE
IIKLKGYTSWAIGLSVMDLVGSILKNLRRVHPVSTMVKGLYGIKEELFLSIPCVLGRNGV
SDVVKINLNSEEEALFKKSAETLWNIQKDLIF
Enzyme 2 Number of Residues 332
Enzyme 2 Molecular Weight 36312
Enzyme 2 Theoretical pI 7.53
Enzyme 2 GO Classification
Function
  • L-lactate dehydrogenase activity
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
Process
  • alcohol metabolism
  • anaerobic glycolysis
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • main pathways of carbohydrate metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
  • tricarboxylic acid cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Possible role in sperm motility
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + 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 307120 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P07864 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LDHC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >999 bp 
ATGTCAACTGTCAAGGAGCAGCTAATTGAGAAGCTAATTGAGGATGATGAAAACTCCCAG
TGTAAAATTACTATTGTTGGAACTGGTGCCGTAGGCATGGCTTGTGCTATTAGTATCTTA
CTGAAGGATTTGGCTGATGAACTTGCCCTTGTTGATGTTGCATTGGACAAACTGAAGGGA
GAAATGATGGATCTTCAGCATGGCAGTCTTTTCTTTAGTACTTCAAAGGTTACTTCTGGA
AAAGATTACAGTGTATCTGCAAACTCCAGAATAGTTATTGTCACAGCAGGTGCAAGGCAG
CAGGAGGGAGAAACTCGCCTTGCCCTGGTCCAACGTAATGTGGCTATAATGAAAATAATC
ATTCCTGCCATAGTCCATTATAGTCCTGATTGTAAAATTCTTGTTGTTTCAAATCCAGTG
GATATTTTGACATATATAGTCTGGAAGATAAGTGGCTTACCTGTAACTCGTGTAATTGGA
AGTGGTTGTAATCTAGACTCTGCCCGTTTCCGTTACCTAATTGGAGAAAAGTTGGGTGTC
CACCCCACAAGCTGCCATGGTTGGATTATTGGAGAACATGGTGATTCTAGTGTGCCCTTA
TGGAGTGGGGTGAATGTTGCTGGTGTTGCTCTGAAGACTCTGGACCCTAAATTAGGAACG
GATTCAGATAAGGAACACTGGAAAAATATCCATAAACAAGTTATTCAAAGTGCCTATGAA
ATTATCAAGCTGAAGGGGTATACCTCTTGGGCTATTGGACTGTCTGTGATGGATCTGGTA
GGATCCATTTTGAAAAATCTTAGGAGAGTGCACCCAGTTTCCACCATGGTTAAGGGATTA
TATGGAATAAAAGAAGAACTCTTTCTCAGTATCCCTTGTGTCTTGGGGCGGAATGGTGTC
TCAGATGTTGTGAAAATTAACTTGAATTCTGAGGAGGAGGCCCTTTTCAAGAAGAGTGCA
GAAACACTTTGGAATATTCAAAAGGATCTAATATTTTAA
Enzyme 2 GenBank Gene ID J02938 Link Image
Enzyme 2 GeneCard ID LDHC Link Image
Enzyme 2 GenAtlas ID LDHC Link Image
Enzyme 2 HGNC ID HGNC:6544 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11p15.5-p15.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Millan JL, Driscoll CE, LeVan KM, Goldberg E: Epitopes of human testis-specific lactate dehydrogenase deduced from a cDNA sequence. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5311-5. [PubMed Link Image]
  2. Takano T, Li SS: Human testicular lactate dehydrogenase-C gene is interrupted by six introns at positions homologous to those of LDH-A (muscle) and LDH-B (heart) genes. Biochem Biophys Res Commun. 1989 Mar 15;159(2):579-83. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5794
Enzyme 3 Name L-lactate dehydrogenase A-like 6B
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name LDHAL6B
Enzyme 3 Protein Sequence >L-lactate dehydrogenase A-like 6B 
MSWTVPVVRASQRVSSVGANFLCLGMALCPRQATRIPLNGTWLFTPVSKMATVKSELIER
FTSEKPVHHSKVSIIGTGSVGMACAISILLKGLSDELALVDLDEDKLKGETMDLQHGSPF
TKMPNIVCSKDYFVTANSNLVIITAGARQEKGETRLNLVQRNVAIFKLMISSIVQYSPHC
KLIIVSNPVDILTYVAWKLSAFPKNRIIGSGCNLDTARFRFLIGQKLGIHSESCHGWILG
EHGDSSVPVWSGVNIAGVPLKDLNSDIGTDKDPEQWKNVHKEVTATAYEIIKMKGYTSWA
IGLSVADLTESILKNLRRIHPVSTIIKGLYGIDEEVFLSIPCILGENGITNLIKIKLTPE
EEAHLKKSAKTLWEIQNKLKL
Enzyme 3 Number of Residues 381
Enzyme 3 Molecular Weight 41943
Enzyme 3 Theoretical pI 8.89
Enzyme 3 GO Classification
Function
  • L-lactate dehydrogenase activity
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
Process
  • alcohol metabolism
  • anaerobic glycolysis
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • main pathways of carbohydrate metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
  • tricarboxylic acid cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 3 General Function Energy production and conversion
Enzyme 3 Specific Function (S)-lactate + NAD(+) = pyruvate + NADH
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12331000 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9BYZ2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name LDH6B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1146 bp 
ATGAGTTGGACTGTGCCTGTTGTGCGGGCCAGCCAGAGAGTGAGCTCGGTGGGAGCGAAT
TTCCTATGCCTGGGGATGGCCCTGTGTCCGCGTCAAGCAACGCGCATCCCGCTCAACGGC
ACCTGGCTCTTCACCCCCGTGAGCAAGATGGCGACTGTGAAGAGTGAGCTTATTGAGCGT
TTCACTTCCGAGAAGCCCGTTCATCACAGTAAGGTCTCCATCATAGGAACTGGATCGGTG
GGCATGGCCTGCGCTATCAGCATCTTATTAAAAGGCTTGAGTGATGAACTTGCCCTTGTG
GATCTTGATGAAGACAAACTGAAGGGTGAGACGATGGATCTTCAACATGGCAGCCCTTTC
ACGAAAATGCCAAATATTGTTTGTAGCAAAGATTACTTTGTCACAGCAAACTCCAACCTA
GTGATTATCACAGCAGGTGCACGCCAAGAAAAGGGAGAAACGCGCCTTAATTTAGTCCAG
CGAAATGTGGCCATCTTCAAGTTAATGATTTCCAGTATTGTCCAGTACAGCCCCCACTGC
AAACTGATTATTGTTTCCAATCCAGTGGATATCTTAACTTATGTAGCTTGGAAGTTGAGT
GCATTTCCCAAAAACCGTATTATTGGAAGCGGCTGTAATCTGGATACTGCTCGTTTTCGT
TTCTTGATTGGACAAAAGCTTGGTATCCATTCTGAAAGCTGCCATGGATGGATCCTCGGA
GAGCATGGAGACTCAAGTGTTCCTGTGTGGAGTGGAGTGAACATAGCTGGTGTCCCTTTG
AAGGATCTGAACTCTGATATAGGAACTGATAAAGATCCTGAGCAATGGAAAAATGTCCAC
AAAGAAGTGACTGCAACTGCCTATGAGATTATTAAAATGAAAGGTTATACTTCTTGGGCC
ATTGGCCTATCTGTGGCCGATTTAACAGAAAGTATTTTGAAGAATCTTAGGAGAATACAT
CCAGTTTCCACCATAATTAAGGGCCTCTATGGAATAGATGAAGAAGTATTCCTCAGTATT
CCTTGTATCCTGGGAGAGAACGGTATTACCAACCTTATAAAGATAAAGCTGACCCCTGAA
GAAGAGGCCCATCTGAAAAAAAGTGCAAAAACACTCTGGGAAATTCAGAATAAGCTTAAG
CTTTAA
Enzyme 3 GenBank Gene ID AY009108 Link Image
Enzyme 3 GeneCard ID LDHAL6B Link Image
Enzyme 3 GenAtlas ID LDHAL6B Link Image
Enzyme 3 HGNC ID HGNC:21481 Link Image
Enzyme 3 Chromosome Location 15
Enzyme 3 Locus 15q22.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6175
Enzyme 4 Name L-lactate dehydrogenase A-like 6A
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name LDHAL6A
Enzyme 4 Protein Sequence >L-lactate dehydrogenase A-like 6A 
MATIKSELIKNFAEEEAIHHNKISIVGTGSVGVACAISILLKGLSDELVLVDVDEGKLKG
ETMDLQHGSPFMKMPNIVSSKDYLVTANSNLVIITAGARQKKGETRLDLVQRNVSIFKLM
IPNITQYSPHCKLLIVTNPVDILTYVAWKLSGFPKNRVIGSGCNLDSARFRYFIGQRLGI
HSESCHGLILGEHGDSSVPVWSGVNIAGVPLKDLNPDIGTDKDPEQWENVHKKVISSGYE
MVKMKGYTSWGISLSVADLTESILKNLRRVHPVSTLSKGLYGINEDIFLSVPCILGENGI
TDLIKVKLTLEEEACLQKSAETLWEIQKELKL
Enzyme 4 Number of Residues 332
Enzyme 4 Molecular Weight 36508
Enzyme 4 Theoretical pI 7.00
Enzyme 4 GO Classification
Function
  • L-lactate dehydrogenase activity
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
Process
  • alcohol metabolism
  • anaerobic glycolysis
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • main pathways of carbohydrate metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
  • tricarboxylic acid cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function (S)-lactate + NAD(+) = pyruvate + NADH
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 46405145 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q6ZMR3 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name LDH6A_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >999 bp 
ATGGCAACTATCAAGAGTGAACTTATTAAGAATTTCGCGGAAGAGGAGGCCATTCATCAC
AATAAGATCTCCATTGTAGGAACTGGATCGGTTGGTGTGGCTTGTGCTATCAGCATCTTA
TTAAAAGGTTTGAGTGATGAACTTGTCCTTGTGGATGTTGATGAAGGCAAACTGAAGGGT
GAGACAATGGATCTTCAACATGGCAGCCCTTTTATGAAAATGCCAAATATTGTCTCCAGC
AAAGATTACCTGGTCACTGCAAACTCCAATCTAGTGATTATCACAGCAGGTGCACGCCAG
AAAAAAGGAGAAACACGCCTTGATTTAGTCCAGCGAAATGTATCCATCTTTAAATTAATG
ATTCCCAATATTACCCAGTACAGTCCTCACTGCAAACTGCTTATTGTTACTAATCCAGTG
GATATCTTAACTTATGTAGCCTGGAAGTTGAGTGGATTTCCCAAAAACCGTGTTATTGGA
AGTGGTTGTAATCTGGACTCTGCTCGTTTTCGTTACTTTATTGGGCAAAGGCTTGGCATC
CACTCTGAAAGCTGTCATGGGCTGATCCTTGGAGAGCATGGCGACTCAAGTGTTCCTGTG
TGGAGTGGTGTGAACATTGCTGGCGTCCCTCTGAAGGATCTGAACCCAGATATAGGAACT
GATAAAGATCCTGAGCAGTGGGAAAATGTCCACAAAAAAGTGATTTCCAGTGGCTATGAG
ATGGTCAAAATGAAAGGTTATACTTCTTGGGGCATTAGCCTATCTGTAGCTGATTTAACA
GAAAGTATTTTGAAGAATCTTAGGAGAGTGCATCCAGTTTCTACCCTAAGTAAGGGCCTC
TATGGAATAAATGAAGACATATTCCTTAGTGTCCCATGTATCCTGGGAGAGAATGGTATC
ACAGACCTCATAAAAGTAAAACTGACTCTTGAAGAGGAGGCCTGCTTGCAAAAGAGTGCA
GAAACACTTTGGGAAATTCAGAAGGAGCTCAAGCTTTAA
Enzyme 4 GenBank Gene ID AY581313 Link Image
Enzyme 4 GeneCard ID LDHAL6A Link Image
Enzyme 4 GenAtlas ID LDHAL6A Link Image
Enzyme 4 HGNC ID HGNC:28335 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11p15.1
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 16419
Enzyme 5 Name cDNA FLJ54086, moderately similar to L-lactate dehydrogenase A chain (EC 1.1.1.27)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >cDNA FLJ54086, moderately similar to L-lactate dehydrogenase A chain (EC 1.1.1.27) 
MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKG
EMMDLQHGSLFLRTPKIVSGKVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERL
GVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESA
YEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQN
GISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
Enzyme 5 Number of Residues 274
Enzyme 5 Molecular Weight 30206
Enzyme 5 Theoretical pI 7.18
Enzyme 5 GO Classification
Function
  • L-lactate dehydrogenase activity
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
Process
  • alcohol metabolism
  • anaerobic glycolysis
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • main pathways of carbohydrate metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
  • tricarboxylic acid cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703] ALL_REAC R00703
  • (other) R01000 R03104
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 B4DKQ2 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B4DKQ2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK296667 Link Image
Enzyme 5 GeneCard ID B4DKQ2 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 Not Available
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available