Description
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 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. Activity of the enzyme is stimulated by K+.
Form
Liquid or lyophilized powder
Storage
Store it at +4 ºC for short term. For long term storage, store it at -20 ºC～-80 ºC.
Synonyms
glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH; AraM
Reaction
sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
Notes
This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.
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