Glycerol dehydrogenase
| glycerol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glycerol dehydrogenase from B. stearothermophilus with glycerol (spheres) PDB 1jqa | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.1.6 | ||||||||
| CAS number | 9028-14-2 | ||||||||
| 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 glycerol dehydrogenase (EC 1.1.1.6) is an enzyme that catalyzes the chemical reaction
- glycerol + NAD+
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.
Structural studies
Structural studies have shown that the enzyme is zinc-dependent with the active site lying between the two domains of the protein. The NAD binding site resembles the Rossmann fold.[1]
A full list of structures solved and deposited in the PDB for this class of enzyme can be found in the info box.
See also
References
- Notes
- Bibliography
- Asnis RE, Brodie AF (1953). "A glycerol dehydrogenase from Escherichia coli". J. Biol. Chem. 203 (1): 153–9. PMID 13069498.
- Burton RM and Kaplan NO (1953). "A DPN specific glycerol dehydrogenase from Aerobacter aerogenes". J. Am. Chem. Soc. 75 (4): 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. PMID 14417009.