3-hydroxyacyl-CoA dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction

(S)-3-hydroxyacyl-CoA + NAD⁺ $\rightleftharpoons$ 3-oxoacyl-CoA + NADH + H⁺

Thus, the two substrates of this enzyme are (S)-3-hydroxyacyl-CoA and NAD⁺, whereas its 3 products are 3-oxoacyl-CoA, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase. Other names in common use include beta-hydroxyacyl dehydrogenase, beta-keto-reductase, 3-keto reductase, 3-hydroxyacyl coenzyme A dehydrogenase, beta-hydroxyacyl-coenzyme A synthetase, beta-hydroxyacylcoenzyme A dehydrogenase, beta-hydroxybutyrylcoenzyme A dehydrogenase, 3-hydroxyacetyl-coenzyme A dehydrogenase, L-3-hydroxyacyl coenzyme A dehydrogenase, L-3-hydroxyacyl CoA dehydrogenase, beta-hydroxyacyl CoA dehydrogenase, 3beta-hydroxyacyl coenzyme A dehydrogenase, 3-hydroxybutyryl-CoA dehydrogenase, beta-ketoacyl-CoA reductase, beta-hydroxy acid dehydrogenase, 3-L-hydroxyacyl-CoA dehydrogenase, 3-hydroxyisobutyryl-CoA dehydrogenase, and 1-specific DPN-linked beta-hydroxybutyric dehydrogenase. This enzyme participates in 8 metabolic pathways: fatty acid elongation in mitochondria, fatty acid metabolism, valine, leucine and isoleucine degradation, lysine degradation, tryptophan metabolism, benzoate degradation via coa ligation, butanoate metabolism, and caprolactam degradation.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 24 structures have been solved for this class of enzymes, with PDB accession codes 1E3S, 1E3W, 1E6W, 1F0Y, 1F12, 1F14, 1F17, 1IL0, 1LSJ, 1LSO, 1M75, 1M76, 1SO8, 1U7T, 1WDK, 1WDL, 1WDM, 1ZBQ, 1ZCJ, 1ZEJ, 2D3T, 2HDH, 3HAD, and 3HDH.

[edit] References

IUBMB entry for 1.1.1.35
BRENDA references for 1.1.1.35 (Recommended.)
PubMed references for 1.1.1.35
PubMed Central references for 1.1.1.35
Google Scholar references for 1.1.1.35
Hillmer P and Gottschalk G (1974). "Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri". Biochim. Biophys. Acta 334: 12–23.
LEHNINGER AL, GREVILLE GD (1953). "The enzymic oxidation of alpha- and 2-beta-hydroxybutyrate". Biochim. Biophys. Acta. 12: 188–202. PMID 13115428.
Stern JR (1957). "Crystalline beta-hydroxybutyrate dehydrogenase from pig heart". Biochim. Biophys. Acta 26: 448–449. doi:10.1016/0006-3002(57)90040-9.
Wakil SJ, Green DE, Mii S and Mahler HR (1954). "Studies on the fatty acid oxidizing system of animal tissues. VI beta-Hydroxyacyl coenzyme A dehydrogenase". J. Biol. Chem. 207: 631–638.