Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy

sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase

sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+ [RN:R05679 R05680]

R05679 R05680
Reaction

sn-glycerol 1-phosphate [CPD:C00623];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]

This enzyme is found primarily as a Zn2+-dependent form in archaea but a Ni2+-dependent form has been found in Gram-positive bacteria [6]. 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 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (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 [4]. Activity of the enzyme is stimulated by K+ [2].

EC 1.1.1.261 created 2000, modified 2009