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InterPro: IPR001557 L-lactate/malate dehydrogenase
Protein matches
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UniProtKB Matches: 3762 proteins |
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Accession
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IPR001557 L-lactate/malate_DH |
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Type
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Family |
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Signatures
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InterPro Relationships
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Parent
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IPR001236 Lactate/malate dehydrogenase
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Children
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IPR011275 Malate dehydrogenase, NAD-dependent
IPR011304 L-lactate dehydrogenase
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Contains
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IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
IPR016040 NAD(P)-binding domain
IPR018177 L-lactate dehydrogenase, active site
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GO Term annotation
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Process
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GO:0006096 glycolysis
GO:0044262 cellular carbohydrate metabolic process
GO:0055114 oxidation reduction
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Function
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GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This family contains both lactate and malate dehydrogenases. Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle.
L-lactate dehydrogenase (EC:1.1.1.27) (LDH) [1] catalyses 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] catalyses the reversible and stereospecific interconversion between 2-ketocarboxylic acids and L-2-hydroxy-carboxylic acids. L-hicDH is evolutionary related to LDH's.
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Structural links
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Database links
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Publications
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1.
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Abad-Zapatero C, Griffith JP, Sussman JL, Rossmann MG.
Refined crystal structure of dogfish M4 apo-lactate dehydrogenase.
J. Mol. Biol. 198 445-67 1987
[PubMed: 3430615]
http://dx.doi.org/10.1016/0022-2836(87)90293-2
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2.
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Hendriks W, Mulders JW, Bibby MA, Slingsby C, Bloemendal H, de Jong WW.
Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions.
Proc. Natl. Acad. Sci. U.S.A. 85 7114-8 1988
[PubMed: 3174623]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=3174623
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3.
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Lerch HP, Frank R, Collins J.
Cloning, sequencing and expression of the L-2-hydroxyisocaproate dehydrogenase-encoding gene of Lactobacillus confusus in Escherichia coli.
Gene 83 263-70 1989
[PubMed: 2684788]
http://dx.doi.org/10.1016/0378-1119(89)90112-1
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Additional Reading
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Kawakami R, Sakuraba H, Goda S, Tsuge H, Ohshima T.
Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.
Biochim. Biophys. Acta 1794 2009 1496-504
[PubMed: 19555779]
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Fioravanti E, Vellieux FM, Amara P, Madern D, Weik M.
Specific radiation damage to acidic residues and its relation to their chemical and structural environment.
14 2007 84-91
[PubMed: 17211074]
http://dx.doi.org/10.1107/S0909049506038623
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Coquelle N, Fioravanti E, Weik M, Vellieux F, Madern D.
Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments.
J. Mol. Biol. 374 2007 547-62
[PubMed: 17936781]
http://dx.doi.org/10.1016/j.jmb.2007.09.049
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Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R.
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol. Biochem. Parasitol. 151 2007 100-10
[PubMed: 17125854]
http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
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Sass C, Briand M, Benslimane S, Renaud M, Briand Y.
Characterization of rabbit lactate dehydrogenase-M and lactate dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in rabbit muscle.
J. Biol. Chem. 264 1989 4076-81
[PubMed: 2917988]
http://intl.jbc.org/cgi/reprint/264/7/4076.pdf
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Cox B, Chit MM, Weaver T, Gietl C, Bailey J, Bell E, Banaszak L.
Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence.
FEBS J. 272 2005 643-54
[PubMed: 15670147]
http://dx.doi.org/10.1111/j.1742-4658.2004.04475.x
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InterPro 23.1
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