1.1.1.261: sn-glycerol-1-phosphate dehydrogenase
This is an abbreviated version!
For detailed information about sn-glycerol-1-phosphate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.261
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1.1.1.261
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phospholipids
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ether
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methanobacterium
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sn-glycerol-3-phosphate
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dihydroxyacetone
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thermoautotrophicum
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dehydrogenases
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hyperthermophilic
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methanogen
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isoprenoid
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dhap
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speciation
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stereochemistry
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archaea-specific
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aeropyrum
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dihydroxyacetonephosphate
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nadp+
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methanothermobacter
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pernix
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analysis
- 1.1.1.261
- phospholipids
- ether
-
methanobacterium
- sn-glycerol-3-phosphate
- dihydroxyacetone
- thermoautotrophicum
- dehydrogenases
-
hyperthermophilic
-
methanogen
-
isoprenoid
- dhap
-
speciation
-
stereochemistry
-
archaea-specific
-
aeropyrum
- dihydroxyacetonephosphate
- nadp+
-
methanothermobacter
- pernix
- analysis
Reaction
Synonyms
EgsA, Enantiomeric glycerophosphate synthase, G-1-P dehydrogenase, G-1-P-dehydrogenase, G1PDH, Gro1PDH, NAD(P)H-dependent G1P dehydrogenase, sn-glycerol-1-phosphate dehydrogenase, ST0344 protein, Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase
ECTree
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Crystallization
Crystallization on EC 1.1.1.261 - sn-glycerol-1-phosphate dehydrogenase
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sitting drop vapor diffusion method, using 30% (w/v) poly(ethylene glycol) methyl ether 550/polyethylene glycol 20000 and 0.1 M HEPES, pH 7.6
structure with bound substrate dihydroxyacetone phosphate, product glycerol 1-phosphate, NADPH, and Zn2+ cofactor. The sole role of His226, His247, and Asp148 is to coordinate the active site Zn2+. A pro-R hydride transfer/relay system is in operation during catalysis, mediated by water and completed by the polarization of the carbonyl of dihydroxyacetone phosphate by Zn2+. Residue Asn104 may influence affinity for the coenzyme and the rate of reaction via its interaction with NADPH
to 2.45 A resolution, one homohexamer per asymmetric unit, with presence of the bound cofactor NADPH in subunits D, E, and F. The phosphate group at C2' of the adenine ribose of NADPH is tightly held through the five biased hydrogen bonds with Ser40 and Thr42. The NADPH molecule is pushed away from the normal coenzyme binding site