D-lactate dehydrogenase (cytochrome)
| D-lactate dehydrogenase (cytochrome) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 1.1.2.4 | ||||||
| CAS number | 37250-79-6 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
|
|||||||
In enzymology, a D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) is an enzyme that catalyzes the chemical reaction
- (D)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c
Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c.
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 employs one cofactor, FAD. This type of enzyme has been characterized in animals, fungi, bacteria and recently in plants[1] [2]. It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway
References
- ^ Atlante, A., de Bari, L., Valenti, D., Pizzuto, R., Paventi, G., and 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. http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T1S-4FV40TJ-1&_user=10&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=5ba860db6f0499628ce76246a7d07d28.
- ^ Martin Engqvist, Maria Fabiana Drincovich, Ulf-Ingo Flügge, and 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. http://www.jbc.org/cgi/reprint/M109.021253v1?view=long&pmid=19586914.
- 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.
- GREGOLIN C, SINGER TP, KEARNEY EB, BOERI E (1961). "The formation and enzymatic properties of the various lactic dehydrogenases of yeast". Ann. N. Y. Acad. Sci. 94 (3): 780–97. doi:10.1111/j.1749-6632.1961.tb35573.x. PMID 13901630.
- Nygaard AP (1961). "D(-)-Lactate cytochrome c reductase, a flavoprotein from yeast". J. Biol. Chem. 236: 920–925.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.