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1JQA

Bacillus stearothermophilus glycerol dehydrogenase complex with glycerol

Summary for 1JQA
Entry DOI10.2210/pdb1jqa/pdb
Related1JPU 1JQ5
DescriptorGlycerol Dehydrogenase, ZINC ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsoxidoreductase, nad, glycerol metabolism
Biological sourceGeobacillus stearothermophilus
Total number of polymer chains1
Total formula weight39787.91
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 citationRuzheinikov, 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: 11566129
DOI: 10.1016/S0969-2126(01)00645-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

226707

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