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Information on EC - sn-glycerol-1-phosphate dehydrogenase

for references in articles please use BRENDA:EC1.1.1.261
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IUBMB Comments
This enzyme is found primarily as a Zn2+-dependent form in Archaea but a Ni2+-dependent form has been found in Gram-positive bacteria . The Zn2+-dependent metalloenzyme is responsible for the formation of Archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in Archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC (phosphoglycerol geranylgeranyltransferase) and EC (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine . Activity of the enzyme is stimulated by K+ .
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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, more
sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
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