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Identification
HMDB Protein ID HMDBP03579
Secondary Accession Numbers
  • 9167
Name L-lactate dehydrogenase A chain
Synonyms
  1. Cell proliferation-inducing gene 19 protein
  2. LDH muscle subunit
  3. LDH-A
  4. LDH-M
  5. Renal carcinoma antigen NY-REN-59
Gene Name LDHA
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific Function Not Available
Pathways
  • Cysteine and methionine metabolism
  • Glutaminolysis and Cancer
  • Glycolysis / Gluconeogenesis
  • HIF-1 signaling pathway
  • Propanoate metabolism
  • pyruvate fermentation to lactate
  • Pyruvate metabolism
Reactions
L-Lactic acid + NAD → Pyruvic acid + NADH details
L-Lactic acid + NAD → Pyruvic acid + NADH + Hydrogen Ion details
2-Hydroxybutyric acid + NAD → 2-Ketobutyric acid + NADH + Hydrogen Ion details
3-Mercaptolactic acid + NAD → 3-Mercaptopyruvic acid + NADH + Hydrogen Ion details
GO Classification
Biological Process
cellular response to extracellular stimulus
glycolysis
cellular carbohydrate metabolic process
pyruvate metabolic process
Cellular Component
cytosol
mitochondrion
flagellum
Component
cell part
intracellular part
cytoplasm
Function
catalytic activity
lactate dehydrogenase activity
l-lactate dehydrogenase activity
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
oxidoreductase activity, acting on ch-oh group of donors
oxidoreductase activity
Molecular Function
L-lactate dehydrogenase activity
nucleotide binding
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
cellular carbohydrate metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
oxidation reduction
glucose catabolic process
glycolysis
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 11
Locus 11p15.4
SNPs LDHA
Gene Sequence
>999 bp
ATGGCAACTCTAAAGGATCAGCTGATTTATAATCTTCTAAAGGAAGAACAGACCCCCCAG
AATAAGATTACAGTTGTTGGGGTTGGTGCTGTTGGCATGGCCTGTGCCATCAGTATCTTA
ATGAAGGACTTGGCAGATGAACTTGCTCTTGTTGATGTCATCGAAGACAAATTGAAGGGA
GAGATGATGGATCTCCAACATGGCAGCCTTTTCCTTAGAACACCAAAGATTGTCTCTGGC
AAAGACTATAATGTAACTGCAAACTCCAAGCTGGTCATTATCACGGCTGGGGCACGTCAG
CAAGAGGGAGAAAGCCGTCTTAATTTGGTCCAGCGTAACGTGAACATATTTAAATTCATC
ATTCCTAATGTTGTAAAATACAGCCCGAACTGCAAGTTGCTTATTGTTTCAAATCCAGTG
GATATCTTGACCTACGTGGCTTGGAAGATAAGTGGTTTTCCCAAAAACCGTGTTATTGGA
AGTGGTTGCAATCTGGATTCAGCCCGATTCCGTTACCTGATGGGGGAAAGGCTGGGAGTT
CACCCATTAAGCTGTCATGGGTGGGTCCTTGGGGAACATGGAGATTCCAGTGTGCCTGTA
TGGAGTGGAATGAATGTTGCTGGTGTCTCTCTGAAGACTCTGCACCCAGATTTAGGGACT
GATAAAGATAAGGAACAGTGGAAAGAGGTTCACAAGCAGGTGGTTGAGAGTGCTTATGAG
GTGATCAAACTCAAAGGCTACACATCCTGGGCTATTGGACTCTCTGTAGCAGATTTGGCA
GAGAGTATAATGAAGAATCTTAGGCGGGTGCACCCAGTTTCCACCATGATTAAGGGTCTT
TACGGAATAAAGGATGATGTCTTCCTTAGTGTTCCTTGCATTTTGGGACAGAATGGAATC
TCAGACCTTGTGAAGGTGACTCTGACTTCTGAGGAAGAGGCCCGTTTGAAGAAGAGTGCA
GATACACTTTGGGGGATCCAAAAGGAGCTGCAATTTTAA
Protein Properties
Number of Residues 332
Molecular Weight 30204.975
Theoretical pI 7.151
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>L-lactate dehydrogenase A chain
MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKG
EMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFI
IPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGV
HPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYE
VIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGI
SDLVKVTLTSEEEARLKKSADTLWGIQKELQF
GenBank ID Protein 34313
UniProtKB/Swiss-Prot ID P00338
UniProtKB/Swiss-Prot Entry Name LDHA_HUMAN
PDB IDs
GenBank Gene ID X02152
GeneCard ID LDHA
GenAtlas ID LDHA
HGNC ID HGNC:6535
References
General References
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  3. 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:15592455 ]
  4. 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. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. 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. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. 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:18083107 ]
  8. 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:10508479 ]
  9. 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:11276087 ]
  10. Tsujibo H, Tiano HF, Li SS: Nucleotide sequences of the cDNA and an intronless pseudogene for human lactate dehydrogenase-A isozyme. Eur J Biochem. 1985 Feb 15;147(1):9-15. [PubMed:3838278 ]
  11. Chung FZ, Tsujibo H, Bhattacharyya U, Sharief FS, LI SS: Genomic organization of human lactate dehydrogenase-A gene. Biochem J. 1985 Nov 1;231(3):537-41. [PubMed:3000353 ]
  12. Maekawa M, Sudo K, Li SS, Kanno T: Analysis of genetic mutations in human lactate dehydrogenase-A(M) deficiency using DNA conformation polymorphism in combination with polyacrylamide gradient gel and silver staining. Biochem Biophys Res Commun. 1991 Oct 31;180(2):1083-90. [PubMed:1953713 ]
  13. Maekawa M, Sudo K, Li SS, Kanno T: Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification. Hum Genet. 1991 Nov;88(1):34-8. [PubMed:1959923 ]
  14. Maekawa M, Sudo K, Kanno T, Li SS: Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency. Biochem Biophys Res Commun. 1990 Apr 30;168(2):677-82. [PubMed:2334430 ]
  15. Sudo K, Maekawa M, Shioya M, Ikeda K, Takahashi N, Isogai Y, Li SS, Kanno T, Machida K, Toriumi J: Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit. Biochem Int. 1992 Sep;27(6):1051-7. [PubMed:1445373 ]
  16. Maekawa M, Sudo K, Kobayashi A, Sugiyama E, Li SS, Kanno T: Fast-type electrophoretic variant of lactate dehydrogenase M(A) and comparison with other missense mutations in lactate dehydrogenase M(A) and H(B) genes. Clin Chem. 1994 Apr;40(4):665-8. [PubMed:7908613 ]