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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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. L-lactate dehydrogenase
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 36638.2
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
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • cellular carbohydrate metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 1 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 1 Specific Function (S)-lactate + NAD(+) = pyruvate + NADH
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 34329 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 >1005 bp
ATGGCAACTCTTAAGGAAAAACTCATTGCACCAGTTGCGGAAGAAGAGGCAACAGTTCCA
AACAATAAGATCACTGTAGTGGGTGTTGGACAAGTTGGTATGGCGTGTGCTATCAGCATT
CTGGGAAAGTCTCTGGCTGATGAACTTGCTCTTGTGGATGTTTTGGAAGATAAGCTTAAA
GGAGAAATGATGGATCTGCAGCATGGGAGCTTATTTCTTCAGACACCTAAAATTGTGGCA
GATAAAGATTATTCTGTGACCGCCAATTCTAAGATTGTAGTGGTAACTGCAGGAGTCCGT
CAGCAAGAAGGGGAGAGTCGGCTCAATCTGGTGCAGAGAAATGTTAATGTCTTCAAATTC
ATTATTCCTCAGATCGTCAAGTACAGTCCTGATTGCATCATAATTGTGGTTTCCAACCCA
GTGGACATTCTTACGTATGTTACCTGGAAACTAAGTGGATTACCCAAACACCGCGTGATT
GGAAGTGGATGTAATCTGGATTCTGCTAGATTTCGCTACCTTATGGCTGAAAAACTTGGC
ATTCATCCCAGCAGCTGCCATGGATGGATTTTGGGGGAACATGGCGACTCAAGTGTGGCT
GTGTGGAGTGGTGTGAATGTGGCAGGTGTTTCTCTCCAGGAATTGAATCCAGAAATGGGA
ACTGACAATGATAGTGAAAATTGGAAGGAAGTGCATAAGATGGTGGTTGAAAGTGCCTAT
GAAGTCATCAAGCTAAAAGGATATACCAACTGGGCTATTGGATTAAGTGTGGCTGATCTT
ATTGAATCCATGTTGAAAAATCTATCCAGGATTCATCCCGTGTCAACAATGGTAAAGGGG
ATGTATGGCATTGAGAATGAAGTCTTCCTGAGCCTTCCATGTATCCTCAATGCCCGGGGA
TTAACCAGCGTTATCAACCAGAAGCTAAAGGATGATGAGGTTGCTCAGCTCAAGAAAAGT
GCAGATACCCTGTGGGACATCCAGAAGGACCTAAAAGACCTGTGA
Enzyme 1 GenBank Gene ID Y00711 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 1
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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL: Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins. 2001 May 1;43(2):175-85. [PubMed Link Image]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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. Cancer/testis antigen 32
  3. CT32
  4. LDH testis subunit
  5. 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 36311.0
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
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • cellular carbohydrate metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 2 Specific Function Possible role in sperm motility
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703]
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 1
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]
  3. Wang H, Zhou Z, Xu M, Li J, Xiao J, Xu ZY, Sha J: A spermatogenesis-related gene expression profile in human spermatozoa and its potential clinical applications. J Mol Med. 2004 May;82(5):317-24. Epub 2004 Feb 24. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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 41942.5
Enzyme 3 Theoretical pI 8.89
Enzyme 3 GO Classification
Function
  • L-lactate dehydrogenase activity
  • binding
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • cellular carbohydrate metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 3 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 3 Specific Function (S)-lactate + NAD(+) = pyruvate + NADH
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
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 1
Enzyme 3 Locus 15q22.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
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 36507.0
Enzyme 4 Theoretical pI 7.00
Enzyme 4 GO Classification
Function
  • L-lactate dehydrogenase activity
  • binding
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • cellular carbohydrate metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 4 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 4 Specific Function Displays an lactate dehydrogenase activity. Significantly increases the transcriptional activity of JUN, when overexpressed
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
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 1
Enzyme 4 Locus 11p15.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Chen X, Gu X, Shan Y, Tang W, Yuan J, Zhong Z, Wang Y, Huang W, Wan B, Yu L: Identification of a novel human lactate dehydrogenase gene LDHAL6A, which activates transcriptional activities of AP1(PMA). Mol Biol Rep. 2009 Apr;36(4):669-76. Epub 2008 Mar 20. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16419
Enzyme 5 Name L-lactate dehydrogenase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >L-lactate dehydrogenase
MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKG
EMMDLQHGSLFLRTPKIVSGKVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERL
GVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESA
YEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQN
GISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
Enzyme 5 Number of Residues 274
Enzyme 5 Molecular Weight 30205.0
Enzyme 5 Theoretical pI 7.18
Enzyme 5 GO Classification
Function
  • L-lactate dehydrogenase activity
  • binding
  • catalytic activity
  • lactate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • cellular carbohydrate metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • primary metabolic process
  • small molecule metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 5 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 5 Specific Function (S)-lactate + NAD(+) = pyruvate + NADH
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 194383812 Link Image
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 >825 bp
ATGGCAACTCTAAAGGATCAGCTGATTTATAACCTTCTAAAGGAAGAACAGACCCCCCAG
AATAAGATTACAGTTGTTGGGGTTGGTGCTGTTGGCATGGCCTGTGCCATCAGTATCTTA
ATGAAGGACTTGGCAGATGAACTTGCTCTTGTTGATGTCATCGAAGACAAATTGAAGGGA
GAGATGATGGATCTCCAACATGGCAGCCTTTTCCTTAGAACACCAAAGATTGTCTCTGGC
AAAGTGGATATCTTGACCTACGTGGCTTGGAAGATAAGTGGTTTTCCCAAAAACCGTGTT
ATTGGAAGCGGTTGCAATCTGGATTCAGCCCGATTCCGTTACCTAATGGGGGAAAGGCTG
GGAGTTCACCCATTAAGCTGTCATGGGTGGGTCCTTGGGGAACATGGAGATTCCAGTGTG
CCTGTATGGAGTGGAATGAATGTTGCTGGTGTCTCTCTGAAGACTCTGCACCCAGATTTA
GGGACTGATAAAGATAAGGAACAGTGGAAAGAGGTTCACAAGCAGGTGGTTGAGAGTGCT
TATGAGGTGATCAAACTCAAAGGCTACACATCCTGGGCTATTGGACTCTCTGTAGCAGAT
TTGGCAGAGAGTATAATGAAGAATCTTAGGCGGGTGCACCCAGTTTCCACCATGATTAAG
GGTCTTTACGGAATAAAGGATGATGTCTTCCTTAGTGTTCCTTGCATTTTGGGACAGAAT
GGAATCTCAGACCTTGTGAAGGTGACTCTGACTTCTGAGGAAGAGGCCCGTTTGAAGAAG
AGTGCAGATACACTTTGGGGGATCCAAAAGGAGCTGCAATTTTAA
Enzyme 5 GenBank Gene ID AK296667 Link Image
Enzyme 5 GeneCard ID Not Available
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID HGNC:6535 Link Image
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