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1.1.1.6: glycerol dehydrogenase

This is an abbreviated version!
For detailed information about glycerol dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.6

Reaction

glycerol
+
NAD+
=
Glycerone
+
NADH
+
H+

Synonyms

B4100_2156, CglD, dehydrogenase, glycerol, GDH, GDH2, GLD, Gld3, GldA, GLDH , GlhA, glycerin dehydrogenase, glycerol dehydrogenase, glycerol NAD 2-oxidoreductase, glycerol:NAD+ 2-oxidoreductase, GlyDH, Gro dehydrogenase, GroDHase, GSH, gycerol dehydrogenase, NAD+-dependent glycerol dehydrogenase, NAD-linked glycerol dehydrogenase, NAD-specific glycerol dehydrogenase, TmGlyDH, TTHADH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.6 glycerol dehydrogenase

Crystallization

Crystallization on EC 1.1.1.6 - glycerol dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method at 22°C, solved at 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 3(10)-helices and several loops organized into two domains, the N- and C-terminal domains. The active site is located in a deep cleft between the two domains
structure containing glycerol in the active site, to 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 310-helices and several loops organized into the N- and C-terminal domains. The active site is located in a deep cleft between the two domains. The N-terminal domain contains a classic Rossmann fold for NAD+ binding. The glycerol molecule is sandwiched by the Zn2+ and NAD+ ions
crystal obtained by hanging-drop vaour-diffusion method, S305C mutant
-
crystallization as a contaminant, crystal was initially assumed to be of a mutant of the SurE protein as it shares some structural features with the presumed target protein
-
hanging drop vapour diffusion, mixing of 0.001 ml 6 mg/ml protein in 150 mM ammonium acetate, 50 mM sodium chloride, 20 mM Tris, pH 7.4, 5% glycerol with 0.001 ml reservoir solution containing 5-10% PEG 3350, 0.2 M calcium acetate, and 4% glycerol, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement using PDB entry 1jpu as a search model
-
in presence of glycerol
-
structure of mutant D121N/F245S