Human Metabolome Database Version 2.5

Showing metabocard for 3-Mercaptopyruvic acid (HMDB01368)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2005-11-16 15:48:42

Update Date

2009-11-05 11:30:36

Accession Number

HMDB01368

Secondary Accession Numbers

Not Available

Common Name

3-Mercaptopyruvic acid

Description

3-Mercaptopyruvic acid is an intermediate in the metabolism of Cysteine. It is a substrate for L-lactate dehydrogenase A chain, 3-mercaptopyruvate sulfurtransferase, Aspartate aminotransferase (mitochondrial), L-lactate dehydrogenase C chain, L-lactate dehydrogenase A-like 6A, Aspartate aminotransferase (cytoplasmic), L-lactate dehydrogenase B chain and L-lactate dehydrogenase A-like 6B.

Synonyms

3-Mercaptopyruvate
3-mercapto-pyruvate
3-mercapto-pyruvic acid
3-mercaptopyruvic acid
beta-3-mercapto-2-oxo-propanoate
beta-3-mercapto-2-oxo-propanoic acid
beta-mercaptopyruvate
beta-mercaptopyruvic acid
beta-thiopyruvate
beta-thiopyruvic acid
mercaptopyruvate
mercaptopyruvic acid
thiopyruvate

Chemical IUPAC Name

2-oxo-3-sulfanyl-propanoic acid

Chemical Formula

C₃H₄O₃S

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Organic acids
Class
Keto-Acids
Sub Class
Sulfur-containing keto-acids
Family
Mammalian Metabolite
Species
ketone carboxylic acid thiol (sulfanyl compound) alkylthiol
Biofunction
Component of Cysteine metabolism
Application
—
Source
Endogenous

Average Molecular Weight

120.127

Monoisotopic Molecular Weight

119.988113

Isomeric SMILES

OC(=O)C(=O)CS

Canonical SMILES

OC(=O)C(=O)CS

KEGG Compound ID

C00957

BioCyc ID

3-MERCAPTO-PYRUVATE Link Image

BiGG ID

36476

Wikipedia Link

Not Available

NuGOwiki Link

HMDB01368

Metagene Link

HMDB01368

METLIN ID

6195

PubChem Compound

PubChem Substance

698356

ChEBI ID

16208

CAS Registry Number

2464-23-5

InChI Identifier

InChI=1/C3H4O3S/c4-2(1-7)3(5)6/h7H,1H2,(H,5,6)

Synthesis Reference

Not Available

Melting Point (Experimental)

Not Available

Experimental Water Solubility

Not Available Source: PhysProp

Predicted Water Solubility

9.09 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS

Physiological Charge

-1

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

0.15 [Predicted by ALOGPS]; -0.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

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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
Medium Energy
Download File Show Experimental Conditions
High Energy
Download File Show Experimental Conditions

Simplified TOCSY Spectrum

Not Available

BMRB Spectrum

Not Available

Cellular Location

Cytoplasm (Predicted from LogP)
mitochondria

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	map00270

General References

Not Available

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5515

Enzyme 1 Name

Aspartate aminotransferase, cytoplasmic

Enzyme 1 Synonyms

Transaminase A
Glutamate oxaloacetate transaminase 1

Enzyme 1 Gene Name

GOT1

Enzyme 1 Protein Sequence

>Aspartate aminotransferase, cytoplasmic

MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ

Enzyme 1 Number of Residues

413

Enzyme 1 Molecular Weight

46248

Enzyme 1 Theoretical pI

7.01

Enzyme 1 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 1 General Function

Amino acid transport and metabolism

Enzyme 1 Specific Function

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

Enzyme 1 Pathways

Arginine and Proline Metabolism (map00330 )
Carbon fixation (map00710 )
Cysteine Metabolism (map00272 )
Glutamate Metabolism (map00251 )
Phenylalanine Metabolism (map00360 )
Phenylalanine and Tyrosine Metabolism (map00400 )
Tyrosine Metabolism (map00350 )
Novobiocin biosynthesis (map00401 )

Enzyme 1 Reactions

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

Enzyme 1 Pfam Domain Function

Aminotran_1_2 (PF00155 )

Enzyme 1 Signals

None

Enzyme 1 Transmembrane Regions

None

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

179067

Enzyme 1 UniProtKB/Swiss-Prot ID

P17174

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

AATC_HUMAN Link Image

Enzyme 1 PDB ID

1AJS

Enzyme 1 PDB File

Show

Enzyme 1 3D Structure

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>1242 bp

ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA

Enzyme 1 GenBank Gene ID

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

10q24.1-q25.1

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed ]
Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5516

Enzyme 2 Name

Aspartate aminotransferase, mitochondrial precursor

Enzyme 2 Synonyms

Transaminase A
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

Arginine and Proline Metabolism (map00330 )
Carbon fixation (map00710 )
Cysteine Metabolism (map00272 )
Glutamate Metabolism (map00251 )
Phenylalanine Metabolism (map00360 )
Phenylalanine and Tyrosine Metabolism (map00400 )
Tyrosine Metabolism (map00350 )
Novobiocin biosynthesis (map00401 )

Enzyme 2 Reactions

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

Enzyme 2 Pfam Domain Function

Aminotran_1_2 (PF00155 )

Enzyme 2 Signals

1-24

Enzyme 2 Transmembrane Regions

Not Available

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

179104

Enzyme 2 UniProtKB/Swiss-Prot ID

P00505

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

Enzyme 2 GeneCard ID

Enzyme 2 GenAtlas ID

Enzyme 2 HGNC ID

Enzyme 2 Chromosome Location

Enzyme 2 Locus

16q21

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

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 ]
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 ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5789

Enzyme 3 Name

Cystathionine gamma-lyase

Enzyme 3 Synonyms

Gamma-cystathionase

Enzyme 3 Gene Name

CTH

Enzyme 3 Protein Sequence

>Cystathionine gamma-lyase

MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS

Enzyme 3 Number of Residues

405

Enzyme 3 Molecular Weight

44508

Enzyme 3 Theoretical pI

6.69

Enzyme 3 GO Classification

Function
—
Process
amino acid and derivative metabolism amino acid metabolism cellular metabolism metabolism physiological process
Component
—

Enzyme 3 General Function

Amino acid transport and metabolism

Enzyme 3 Specific Function

L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate

Enzyme 3 Pathways

Cysteine Metabolism (map00272 )
Glycine, Serine and Threonine Metabolism (map00260 )
Methionine Metabolism (map00271 )
Nitrogen Metabolism (map00910 )
Selenoamino Acid Metabolism (map00450 )

Enzyme 3 Reactions

L-cystathionine + H2O = L-cysteine + ammonia + 2-oxobutanoate

Enzyme 3 Pfam Domain Function

Cys_Met_Meta_PP (PF01053 )

Enzyme 3 Signals

None

Enzyme 3 Transmembrane Regions

None

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

262476

Enzyme 3 UniProtKB/Swiss-Prot ID

P32929

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

CGL_HUMAN

Enzyme 3 PDB ID

Not Available

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>1218 bp

ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCGGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG

Enzyme 3 GenBank Gene ID

Enzyme 3 GeneCard ID

Enzyme 3 GenAtlas ID

Enzyme 3 HGNC ID

Enzyme 3 Chromosome Location

Enzyme 3 Locus

1p31.1

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Lu Y, O'Dowd BF, Orrego H, Israel Y: Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase. Biochem Biophys Res Commun. 1992 Dec 15;189(2):749-58. [PubMed ]
Wang J, Hegele RA: Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH). Hum Genet. 2003 Apr;112(4):404-8. Epub 2003 Feb 6. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5791

Enzyme 4 Name

L-lactate dehydrogenase B chain

Enzyme 4 Synonyms

LDH-B
LDH heart subunit
LDH-H
Renal carcinoma antigen NY-REN-46

Enzyme 4 Gene Name

LDHB

Enzyme 4 Protein Sequence

>L-lactate dehydrogenase B chain

MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLK
GEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKF
IIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLG
IHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAY
EVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARG
LTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL

Enzyme 4 Number of Residues

334

Enzyme 4 Molecular Weight

36639

Enzyme 4 Theoretical pI

5.93

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

Cysteine Metabolism (map00272 )
Gluconeogenesis (map00010 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )

Enzyme 4 Reactions

(S)-lactate + NAD+ = pyruvate + NADH + H+

Enzyme 4 Pfam Domain Function

Ldh_1_C (PF02866 )
Ldh_1_N (PF00056 )

Enzyme 4 Signals

None

Enzyme 4 Transmembrane Regions

None

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

1200083

Enzyme 4 UniProtKB/Swiss-Prot ID

P07195

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

LDHB_HUMAN Link Image

Enzyme 4 PDB ID

1I0Z

Enzyme 4 PDB File

Show

Enzyme 4 3D Structure

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>129 bp

ATGGCAACTCTTAAGGAAAAACTCATTGCACCAGTTGCGGAAGAAGAGGCAACAGTTCCA
AACAATAAGATCACTGTAGTGGGTGTTGGACAAGTTGGTATGGCGTGTGCTATCAGCATT
CTGGGAAAG

Enzyme 4 GenBank Gene ID

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

Enzyme 4 Chromosome Location

Enzyme 4 Locus

12p12.2-p12.1

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Takeno T, Li SS: Structure of the human lactate dehydrogenase B gene. Biochem J. 1989 Feb 1;257(3):921-4. [PubMed ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5792

Enzyme 5 Name

L-lactate dehydrogenase C chain

Enzyme 5 Synonyms

LDH-C
LDH testis subunit
LDH-X

Enzyme 5 Gene Name

LDHC

Enzyme 5 Protein Sequence

>L-lactate dehydrogenase C chain

MSTVKEQLIEKLIEDDENSQCKITIVGTGAVGMACAISILLKDLADELALVDVALDKLKG
EMMDLQHGSLFFSTSKITSGKDYSVSANSRIVIVTAGARQQEGETRLALVQRNVAIMKSI
IPAIVHYSPDCKILVVSNPVDILTYIVWKISGLPVTRVIGSGCNLDSARFRYLIGEKLGV
HPTSCHGWIIGEHGDSSVPLWSGVNVAGVALKTLDPKLGTDSDKEHWKNIHKQVIQSAYE
IIKLKGYTSWAIGLSVMDLVGSILKNLRRVHPVSTMVKGLYGIKEELFLSIPCVLGRNGV
SDVVKINLNSEEEALFKKSAETLWNIQKDLIF

Enzyme 5 Number of Residues

332

Enzyme 5 Molecular Weight

36312

Enzyme 5 Theoretical pI

7.53

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

Possible role in sperm motility

Enzyme 5 Pathways

Cysteine Metabolism (map00272 )
Gluconeogenesis (map00010 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )

Enzyme 5 Reactions

(S)-lactate + NAD+ = pyruvate + NADH + H+

Enzyme 5 Pfam Domain Function

Ldh_1_C (PF02866 )
Ldh_1_N (PF00056 )

Enzyme 5 Signals

None

Enzyme 5 Transmembrane Regions

None

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

307120

Enzyme 5 UniProtKB/Swiss-Prot ID

P07864

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

LDHC_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>999 bp

ATGTCAACTGTCAAGGAGCAGCTAATTGAGAAGCTAATTGAGGATGATGAAAACTCCCAG
TGTAAAATTACTATTGTTGGAACTGGTGCCGTAGGCATGGCTTGTGCTATTAGTATCTTA
CTGAAGGATTTGGCTGATGAACTTGCCCTTGTTGATGTTGCATTGGACAAACTGAAGGGA
GAAATGATGGATCTTCAGCATGGCAGTCTTTTCTTTAGTACTTCAAAGGTTACTTCTGGA
AAAGATTACAGTGTATCTGCAAACTCCAGAATAGTTATTGTCACAGCAGGTGCAAGGCAG
CAGGAGGGAGAAACTCGCCTTGCCCTGGTCCAACGTAATGTGGCTATAATGAAAATAATC
ATTCCTGCCATAGTCCATTATAGTCCTGATTGTAAAATTCTTGTTGTTTCAAATCCAGTG
GATATTTTGACATATATAGTCTGGAAGATAAGTGGCTTACCTGTAACTCGTGTAATTGGA
AGTGGTTGTAATCTAGACTCTGCCCGTTTCCGTTACCTAATTGGAGAAAAGTTGGGTGTC
CACCCCACAAGCTGCCATGGTTGGATTATTGGAGAACATGGTGATTCTAGTGTGCCCTTA
TGGAGTGGGGTGAATGTTGCTGGTGTTGCTCTGAAGACTCTGGACCCTAAATTAGGAACG
GATTCAGATAAGGAACACTGGAAAAATATCCATAAACAAGTTATTCAAAGTGCCTATGAA
ATTATCAAGCTGAAGGGGTATACCTCTTGGGCTATTGGACTGTCTGTGATGGATCTGGTA
GGATCCATTTTGAAAAATCTTAGGAGAGTGCACCCAGTTTCCACCATGGTTAAGGGATTA
TATGGAATAAAAGAAGAACTCTTTCTCAGTATCCCTTGTGTCTTGGGGCGGAATGGTGTC
TCAGATGTTGTGAAAATTAACTTGAATTCTGAGGAGGAGGCCCTTTTCAAGAAGAGTGCA
GAAACACTTTGGAATATTCAAAAGGATCTAATATTTTAA

Enzyme 5 GenBank Gene ID

Enzyme 5 GeneCard ID

Enzyme 5 GenAtlas ID

Enzyme 5 HGNC ID

Enzyme 5 Chromosome Location

Enzyme 5 Locus

11p15.5-p15.3

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

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 ]
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 ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5794

Enzyme 6 Name

L-lactate dehydrogenase A-like 6B

Enzyme 6 Synonyms

Not Available

Enzyme 6 Gene Name

LDHAL6B

Enzyme 6 Protein Sequence

>L-lactate dehydrogenase A-like 6B

MSWTVPVVRASQRVSSVGANFLCLGMALCPRQATRIPLNGTWLFTPVSKMATVKSELIER
FTSEKPVHHSKVSIIGTGSVGMACAISILLKGLSDELALVDLDEDKLKGETMDLQHGSPF
TKMPNIVCSKDYFVTANSNLVIITAGARQEKGETRLNLVQRNVAIFKLMISSIVQYSPHC
KLIIVSNPVDILTYVAWKLSAFPKNRIIGSGCNLDTARFRFLIGQKLGIHSESCHGWILG
EHGDSSVPVWSGVNIAGVPLKDLNSDIGTDKDPEQWKNVHKEVTATAYEIIKMKGYTSWA
IGLSVADLTESILKNLRRIHPVSTIIKGLYGIDEEVFLSIPCILGENGITNLIKIKLTPE
EEAHLKKSAKTLWEIQNKLKL

Enzyme 6 Number of Residues

381

Enzyme 6 Molecular Weight

41943

Enzyme 6 Theoretical pI

8.89

Enzyme 6 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 6 General Function

Energy production and conversion

Enzyme 6 Specific Function

(S)-lactate + NAD(+) = pyruvate + NADH

Enzyme 6 Pathways

Cysteine Metabolism (map00272 )
Gluconeogenesis (map00010 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )

Enzyme 6 Reactions

(S)-lactate + NAD+ = pyruvate + NADH + H+

Enzyme 6 Pfam Domain Function

Ldh_1_C (PF02866 )
Ldh_1_N (PF00056 )

Enzyme 6 Signals

None

Enzyme 6 Transmembrane Regions

None

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

12331000

Enzyme 6 UniProtKB/Swiss-Prot ID

Q9BYZ2

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

LDH6B_HUMAN Link Image

Enzyme 6 PDB ID

Not Available

Enzyme 6 Cellular Location

Not Available

Enzyme 6 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 6 GenBank Gene ID

AY009108

Enzyme 6 GeneCard ID

LDHAL6B

Enzyme 6 GenAtlas ID

LDHAL6B

Enzyme 6 HGNC ID

HGNC:21481 Link Image

Enzyme 6 Chromosome Location

Enzyme 6 Locus

15q22.2

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

6061

Enzyme 7 Name

3-mercaptopyruvate sulfurtransferase

Enzyme 7 Synonyms

Enzyme 7 Gene Name

MPST

Enzyme 7 Protein Sequence

>3-mercaptopyruvate sulfurtransferase

MASPQLCRALVSAQWVAEALRAPRAGQPLQLLDASWYLPKLGRDARREFEERHIPGAAFF
DIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAF
GHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQV
VDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDL
SKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRARPEDVISEGRGKTH

Enzyme 7 Number of Residues

297

Enzyme 7 Molecular Weight

33179

Enzyme 7 Theoretical pI

6.58

Enzyme 7 GO Classification

Function
catalytic activity sulfurtransferase activity thiosulfate sulfurtransferase activity transferase activity transferase activity, transferring sulfur-containing groups
Process
anion transport cellular physiological process inorganic anion transport ion transport physiological process sulfate transport transport
Component
—

Enzyme 7 General Function

Inorganic ion transport and metabolism

Enzyme 7 Specific Function

Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. May have a role in cyanide degradation or in thiosulfate biosynthesis

Enzyme 7 Pathways

Cysteine Metabolism (map00272 )

Enzyme 7 Reactions

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate

Enzyme 7 Pfam Domain Function

Rhodanese (PF00581 )

Enzyme 7 Signals

None

Enzyme 7 Transmembrane Regions

None

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

432376

Enzyme 7 UniProtKB/Swiss-Prot ID

P25325

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

THTM_HUMAN Link Image

Enzyme 7 PDB ID

Not Available

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>891 bp

ATGGCTTCGCCGCAGCTCTGCCGCGCGCTGGTGTCGGCGCAATGGGTGGCGGAGGCGCTG
CGGGCCCCGCGCGCTGGGCAGCCTCTGCAGCTGCTGGACGCCTCCTGGTACCTGCCGAAG
CTGGGGCGCGACGCGACGCAGTTCGAGGAGCGCCACATCCCGGGCGCCGCTTTCTTCGAC
ATCGACCAGTGCAGCGACCGCACCTCGCCCTACGACCACATGCTGCCCGGGGCCGAGCAT
TTCGCGGAGTACGCAGGCCGCCTGGGCGTGGGCGCGGCCACCCACGTCGTGATCTACGAC
GCCAGCGACCAGGGCCTCTACTCCGCCCCGCGCGTCTGGTGGATGTTCCGCGCCTTCGGC
CACCACGCCGTGTCACTGCTTGATGGCGGCCTCCGCCACTGGCTGCGCCAGAACCTCCCG
CTCAGCTCCGGCAAGAGCCAACCTGCTCCCGCCGAGTTCCGCGCTCAGCTCGACCCCGCC
TTCATCAAGACCTACGAGGACATCAAGGAGAACCTGGAATCCCGGCGCTTCCAGGTGGTG
GACTCCCGAGCCACTGGCAGGTTCCGCGGCACCGAGCCCGAGCCCCGAGACGGCATTGAA
CCTGGCCACATCCCAGGTACCGTGAACATCCCCTTCACAGACTTCCTGAGCCAGGAGGGG
CTGGAGAAGAGCCCTGAGGAGATCCGCCATCTGTTCCAGGAGAAGAAAGTGGACCTGTCT
AAGCCACTGGTGGCCACGTGTGGCTCTGGCGTCACAGCCTGCCACGTGGCACTAGGGGCC
TACCTCTGCGGCAAGCCAGACGTGCCCATCTACGATGGCTCCTGGGTGGAGTGGTACATG
CGCGCCCGGCCCGAGGATGTCATCTCAGAGGGCCGGGGGAAGACCCACTGA

Enzyme 7 GenBank Gene ID

Enzyme 7 GeneCard ID

Enzyme 7 GenAtlas ID

Enzyme 7 HGNC ID

Enzyme 7 Chromosome Location

Enzyme 7 Locus

22q13.1

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

Pallini R, Guazzi GC, Cannella C, Cacace MG: Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. Biochem Biophys Res Commun. 1991 Oct 31;180(2):887-93. [PubMed ]
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

6175

Enzyme 8 Name

L-lactate dehydrogenase A-like 6A

Enzyme 8 Synonyms

Not Available

Enzyme 8 Gene Name

LDHAL6A

Enzyme 8 Protein Sequence

>L-lactate dehydrogenase A-like 6A

MATIKSELIKNFAEEEAIHHNKISIVGTGSVGVACAISILLKGLSDELVLVDVDEGKLKG
ETMDLQHGSPFMKMPNIVSSKDYLVTANSNLVIITAGARQKKGETRLDLVQRNVSIFKLM
IPNITQYSPHCKLLIVTNPVDILTYVAWKLSGFPKNRVIGSGCNLDSARFRYFIGQRLGI
HSESCHGLILGEHGDSSVPVWSGVNIAGVPLKDLNPDIGTDKDPEQWENVHKKVISSGYE
MVKMKGYTSWGISLSVADLTESILKNLRRVHPVSTLSKGLYGINEDIFLSVPCILGENGI
TDLIKVKLTLEEEACLQKSAETLWEIQKELKL

Enzyme 8 Number of Residues

332

Enzyme 8 Molecular Weight

36508

Enzyme 8 Theoretical pI

7.00

Enzyme 8 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 8 General Function

Energy production and conversion

Enzyme 8 Specific Function

(S)-lactate + NAD(+) = pyruvate + NADH

Enzyme 8 Pathways

Cysteine Metabolism (map00272 )
Gluconeogenesis (map00010 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )

Enzyme 8 Reactions

(S)-lactate + NAD+ = pyruvate + NADH + H+

Enzyme 8 Pfam Domain Function

Ldh_1_C (PF02866 )
Ldh_1_N (PF00056 )

Enzyme 8 Signals

None

Enzyme 8 Transmembrane Regions

None

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

46405145

Enzyme 8 UniProtKB/Swiss-Prot ID

Q6ZMR3

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

LDH6A_HUMAN Link Image

Enzyme 8 PDB ID

Not Available

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>999 bp

ATGGCAACTATCAAGAGTGAACTTATTAAGAATTTCGCGGAAGAGGAGGCCATTCATCAC
AATAAGATCTCCATTGTAGGAACTGGATCGGTTGGTGTGGCTTGTGCTATCAGCATCTTA
TTAAAAGGTTTGAGTGATGAACTTGTCCTTGTGGATGTTGATGAAGGCAAACTGAAGGGT
GAGACAATGGATCTTCAACATGGCAGCCCTTTTATGAAAATGCCAAATATTGTCTCCAGC
AAAGATTACCTGGTCACTGCAAACTCCAATCTAGTGATTATCACAGCAGGTGCACGCCAG
AAAAAAGGAGAAACACGCCTTGATTTAGTCCAGCGAAATGTATCCATCTTTAAATTAATG
ATTCCCAATATTACCCAGTACAGTCCTCACTGCAAACTGCTTATTGTTACTAATCCAGTG
GATATCTTAACTTATGTAGCCTGGAAGTTGAGTGGATTTCCCAAAAACCGTGTTATTGGA
AGTGGTTGTAATCTGGACTCTGCTCGTTTTCGTTACTTTATTGGGCAAAGGCTTGGCATC
CACTCTGAAAGCTGTCATGGGCTGATCCTTGGAGAGCATGGCGACTCAAGTGTTCCTGTG
TGGAGTGGTGTGAACATTGCTGGCGTCCCTCTGAAGGATCTGAACCCAGATATAGGAACT
GATAAAGATCCTGAGCAGTGGGAAAATGTCCACAAAAAAGTGATTTCCAGTGGCTATGAG
ATGGTCAAAATGAAAGGTTATACTTCTTGGGGCATTAGCCTATCTGTAGCTGATTTAACA
GAAAGTATTTTGAAGAATCTTAGGAGAGTGCATCCAGTTTCTACCCTAAGTAAGGGCCTC
TATGGAATAAATGAAGACATATTCCTTAGTGTCCCATGTATCCTGGGAGAGAATGGTATC
ACAGACCTCATAAAAGTAAAACTGACTCTTGAAGAGGAGGCCTGCTTGCAAAAGAGTGCA
GAAACACTTTGGGAAATTCAGAAGGAGCTCAAGCTTTAA

Enzyme 8 GenBank Gene ID

AY581313

Enzyme 8 GeneCard ID

LDHAL6A

Enzyme 8 GenAtlas ID

LDHAL6A

Enzyme 8 HGNC ID

HGNC:28335 Link Image

Enzyme 8 Chromosome Location

Enzyme 8 Locus

11p15.1

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

Not Available

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

16419

Enzyme 9 Name

cDNA FLJ54086, moderately similar to L-lactate dehydrogenase A chain (EC 1.1.1.27)

Enzyme 9 Synonyms

Not Available

Enzyme 9 Gene Name

Not Available

Enzyme 9 Protein Sequence

>cDNA FLJ54086, moderately similar to L-lactate dehydrogenase A chain (EC 1.1.1.27)

MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKG
EMMDLQHGSLFLRTPKIVSGKVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERL
GVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESA
YEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQN
GISDLVKVTLTSEEEARLKKSADTLWGIQKELQF

Enzyme 9 Number of Residues

274

Enzyme 9 Molecular Weight

30206

Enzyme 9 Theoretical pI

7.18

Enzyme 9 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 9 General Function

Energy production and conversion

Enzyme 9 Specific Function

Not Available

Enzyme 9 Pathways

Not Available

Enzyme 9 Reactions

(S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703] ALL_REAC R00703
(other) R01000 R03104

Enzyme 9 Pfam Domain Function

Ldh_1_C (PF02866 )
Ldh_1_N (PF00056 )

Enzyme 9 Signals

None

Enzyme 9 Transmembrane Regions

None

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

Not Available

Enzyme 9 UniProtKB/Swiss-Prot ID

B4DKQ2

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

B4DKQ2_HUMAN Link Image

Enzyme 9 PDB ID

Not Available

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

Not Available

Enzyme 9 GenBank Gene ID

AK296667

Enzyme 9 GeneCard ID

B4DKQ2

Enzyme 9 GenAtlas ID

Not Available

Enzyme 9 HGNC ID

Not Available

Enzyme 9 Chromosome Location

Not Available

Enzyme 9 Locus

Not Available

Enzyme 9 SNPs

Not Available

Enzyme 9 General References

Not Available

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

16502

Enzyme 10 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 10 Synonyms

Not Available

Enzyme 10 Gene Name

GOT1

Enzyme 10 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 10 Number of Residues

413

Enzyme 10 Molecular Weight

46248

Enzyme 10 Theoretical pI

7.01

Enzyme 10 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 10 General Function

Amino acid transport and metabolism

Enzyme 10 Specific Function

Not Available

Enzyme 10 Pathways

Not Available

Enzyme 10 Reactions

Not Available

Enzyme 10 Pfam Domain Function

Aminotran_1_2 (PF00155 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

None

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

Not Available

Enzyme 10 UniProtKB/Swiss-Prot ID

B2R6R7

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

B2R6R7_HUMAN Link Image

Enzyme 10 PDB ID

1AJS

Enzyme 10 PDB File

Show

Enzyme 10 3D Structure

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

Not Available

Enzyme 10 GenBank Gene ID

AK312684

Enzyme 10 GeneCard ID

B2R6R7

Enzyme 10 GenAtlas ID

Not Available

Enzyme 10 HGNC ID

Not Available

Enzyme 10 Chromosome Location

Enzyme 10 Locus

10q24.1-q25.1

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Not Available

Enzyme 10 Metabolite References

Not Available

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Human Metabolome Database Version 2.5

Showing metabocard for 3-Mercaptopyruvic acid (HMDB01368)