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Literature summary extracted from

  • Echigoya, Y.; Sato, T.; Itou, T.; Endo, H.; Sakai, T.
    Molecular characterization and expression pattern of the equine lactate dehydrogenase A and B genes (2009), Gene, 447, 40-50.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.27 LDHA, DNA and amino acid sequence determination and analysis, genetic structure, and sequence comparisons, phylogenetic analysis, overview Equus caballus
1.1.1.27 LDHB, DNA and amino acid sequence determination and analysis, genetic structure, and sequence comparisons, phylogenetic analysis, overview Equus caballus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.27 H88X/H226X substitution of His 88 and 226 of the eLDHA monomer alters the surface charge of equine LDH tetramer, the residues are located in an important region affecting the catalytic kinetics Equus caballus
1.1.1.27 additional information deletion of Glu 14 of the eLDHB monomer alters the surface charge of equine LDH tetramers and the residue is located in an important region affecting the catalytic kinetics Equus caballus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.27 L-lactate + NAD+ Equus caballus
-
 pyruvate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Equus caballus B7XH73 eLDHA; isozymes LDH A, encoded by gene LDHA
-
1.1.1.27 Equus caballus C6L1K8 eLDHB, fragment; isozymes LDH B, encoded by gene LDHB
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.27 brain
-
 Equus caballus
-
1.1.1.27 heart
-
 Equus caballus
-
1.1.1.27 uterine cervix muscle Equus caballus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 L-lactate + NAD+
-
 Equus caballus pyruvate + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.27 More three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview Equus caballus
1.1.1.27 More three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview Equus caballus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.27 eLDHA
-
 Equus caballus
1.1.1.27 eLDHB
-
 Equus caballus
1.1.1.27 lactate dehydrogenase A
-
 Equus caballus
1.1.1.27 lactate dehydrogenase B
-
 Equus caballus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+
-
 Equus caballus
1.1.1.27 NADH
-
 Equus caballus