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PROSITE documentation PDOC00062

L-lactate dehydrogenase active site

Description:

L-lactate dehydrogenase (EC 1.1.1.27) (LDH) [1] catalyzes the reversible NAD-dependent interconversion of pyruvate to L-lactate. In vertebrate muscles and in lactic acid bacteria it represents the final step in anaerobic glycolysis. This tetrameric enzyme is present in prokaryotic and eukaryotic organisms. In vertebrates there are three isozymes of LDH: the M form (LDH-A), found predominantly in muscle tissues; the H form (LDH-B), found in heart muscle and the X form (LDH-C), found only in the spermatozoa of mammals and birds. In birds and crocodilian eye lenses, LDH-B serves as a structural protein and is known as epsilon-crystallin [2].

L-2-hydroxyisocaproate dehydrogenase (EC 1.1.1.-) (L-hicDH) [3] catalyzes the reversible and stereospecific interconversion between 2-ketocarboxylic acids and L-2-hydroxy-carboxylic acids. L-hicDH is evolutionary related to LDH's.

As a signature for LDH's we have selected a region that includes a conserved histidine which is essential to the catalytic mechanism.

Last update:

November 1995 / Text revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

L_LDH, PS00064; L-lactate dehydrogenase active site  (PATTERN)
Consensus pattern: [LIVMA]-G-[EQ]-H-G-[DN]-[ST]
H is the active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: 1
• Retrieve an alignment of Swiss-Prot true positive hits:
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• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00064
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00064
• Scan Swiss-Prot/TrEMBL entries against PS00064
• view ligand binding statistics
Matching PDB structures: 1A5Z 1EZ4 1HYH 1I0Z ... [ALL]

References:

1 AuthorsAbad-Zapatero C., Griffith J.P., Sussman J.L., Rossmann M.G.
SourceJ. Mol. Biol. 198:445-467(1987).
2 AuthorsHendriks W., Mulders J.W.M., Bibby M.A., Slingsby C., Bloemendal H., de Jong W.W.
TitleDuck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions.
SourceProc. Natl. Acad. Sci. U.S.A. 85:7114-7118(1988).
PubMed ID3174623
3 AuthorsLerch H.-P., Frank R., Collins J.
TitleCloning, sequencing and expression of the L-2-hydroxyisocaproate dehydrogenase-encoding gene of Lactobacillus confusus in Escherichia coli.
SourceGene 83:263-270(1989).
PubMed ID2684788

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