D-lactate dehydrogenase (cytochrome)

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D-lactate dehydrogenase (cytochrome)
Identifiers
EC no. 1.1.2.4
CAS no. 37250-79-6
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MetaCyc metabolic pathway
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In enzymology, D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) is an enzyme that catalyzes the chemical reaction

 
Fe3+
Fe2+
D-lactate dehydrogenase (cytochrome)
Fe3+
Fe2+
 
+ 2 H+
 

The substrate of this enzyme is (R)-lactic acid, which is acted on by two equivalents of the cofactor, ferricytochrome c, which oxidises the hydroxy group to a keto group, giving pyruvic acid, while the cofactor's iron is reduced. [1] [2] [3] [4]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (D)-lactate:ferricytochrome-c 2-oxidoreductase. Other names in common use include lactic acid dehydrogenase, D-lactate (cytochrome) dehydrogenase, cytochrome-dependent D-(−)-lactate dehydrogenase, D-lactate-cytochrome c reductase, and D-(−)-lactic cytochrome c reductase. This enzyme participates in pyruvate metabolism. It is a flavoprotein. [1] This type of enzyme has been characterized in animals, fungi, bacteria and plants. [5] [6] It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway.

See also

References

  1. 1 2 Enzyme 1.1.2.4 at KEGG Pathway Database.
  2. Gregolin C, Singer TP (1963). "The lactic dehydrogenase of yeast. III. D(-)Lactic cytochrome c reductase, a zinc-flavoprotein from aerobic yeast". Biochim. Biophys. Acta. 67: 201–18. doi:10.1016/0006-3002(63)91818-3. PMID   13950255.
  3. Nygaard AP (1961). "D(−)-Lactate cytochrome c reductase, a flavoprotein from yeast". J. Biol. Chem. 236 (3): 920–925. doi: 10.1016/S0021-9258(18)64331-5 . PMID   13729965.
  4. Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.
  5. Atlante, A.; de Bari, L.; Valenti, D.; Pizzuto, R.; Paventi, G. & Passarella, S. (2005). "Transport and metabolism of D-lactate in Jerusalem artichoke mitochondria". Biochim. Biophys. Acta. 1708 (1): 13–22. doi: 10.1016/j.bbabio.2005.03.003 . PMID   15949980.
  6. Martin Engqvist; Maria Fabiana Drincovich; Ulf-Ingo Flügge & Veronica G. Maurino (2009). "Two D-2-hydroxyacid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and {beta}-oxidation pathways". J Biol Chem. 284 (September 11): 25026–25037. doi: 10.1074/jbc.M109.021253 . PMC   2757207 . PMID   19586914.