1JQA
Bacillus stearothermophilus glycerol dehydrogenase complex with glycerol
Summary for 1JQA
Entry DOI | 10.2210/pdb1jqa/pdb |
Related | 1JPU 1JQ5 |
Descriptor | Glycerol Dehydrogenase, ZINC ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | oxidoreductase, nad, glycerol metabolism |
Biological source | Geobacillus stearothermophilus |
Total number of polymer chains | 1 |
Total formula weight | 39787.91 |
Authors | Ruzheinikov, S.N.,Burke, J.,Sedelnikova, S.,Baker, P.J.,Taylor, R.,Bullough, P.A.,Muir, N.M.,Gore, M.G.,Rice, D.W. (deposition date: 2001-08-04, release date: 2001-10-03, Last modification date: 2023-08-16) |
Primary citation | Ruzheinikov, S.N.,Burke, J.,Sedelnikova, S.,Baker, P.J.,Taylor, R.,Bullough, P.A.,Muir, N.M.,Gore, M.G.,Rice, D.W. Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase. Structure, 9:789-802, 2001 Cited by PubMed Abstract: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD(+) 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD(+) to NADH. Analysis of the sequence of this enzyme indicates that it is a member of the so-called iron-containing alcohol dehydrogenase family. Despite this sequence similarity, GlyDH shows a strict dependence on zinc for activity. On the basis of this, we propose to rename this group the family III metal-dependent polyol dehydrogenases. To date, no structural data have been reported for any enzyme in this group. PubMed: 11566129DOI: 10.1016/S0969-2126(01)00645-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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