Glycerol dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a glycerol dehydrogenase (EC 1.1.1.6) is an enzyme that catalyzes the chemical reaction:

glycerol + NAD⁺ $\rightleftharpoons$ glycerone + NADH + H⁺

Thus, the two substrates of this enzyme are glycerol and NAD⁺, whereas its three products are glycerone, 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 glycerol:NAD+ 2-oxidoreductase. Other names in common use include glycerin dehydrogenase, and NAD+-linked glycerol dehydrogenase. This enzyme participates in glycerolipid metabolism.

1 Structural studies
2 See also
3 References
4 External links
- 4.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1JPU, 1JQ5, 1JQA, and 1TA9.

[edit] See also

[edit] References

IUBMB entry for 1.1.1.6
BRENDA references for 1.1.1.6 (Recommended.)
PubMed references for 1.1.1.6
PubMed Central references for 1.1.1.6
Google Scholar references for 1.1.1.6
ASNIS RE, BRODIE AF (1953). "A glycerol dehydrogenase from Escherichia coli". J. Biol. Chem. 203: 153–9. PMID 13069498.
Burton RM and Kaplan NO (1953). "A DPN specific glycerol dehydrogenase from Aerobacter aerogenes". J. Am. Chem. Soc. 75: 1005–1007. doi:10.1021/ja01100a520.
Lin ECC and Magasanik B (1960). "The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations". J. Biol. Chem. 235: 1820–1823.