The interaction of alpha-chlorohydrin with glycerol kinase.
alpha-Chlorohydrin has been examined both for its ability to act as a substrate for glycerol kinase and as an inhibitor of the reaction of glycerol with glycerol kinase. Using a purified enzyme from Candida mycoderma, it was established that alpha-chlorohydrin does not act as a substrate for glycerol kinase, but does act as a competitive inhibitor (Ki of 30 mM) of purified glycerol kinase and the enzyme present in a sonicated preparation of ram spermatozoa. Neither alpha-chlorohydrin nor alpha-chlorohydrin phosphate acted as inhibitors of NAD- or flavin-linked glycerolphosphate dehydrogenase. It is concluded that alpha-chlorohydrin does not cause the impairment of sperm metabolism as a result of phosphorylation catalysed by glycerol kinase.
D000818:Animals; D001667:Binding, Competitive; D002728:Chlorohydrins / Q000494:pharmacology*; D005990:Glycerol / Q000494:pharmacology; D005991:Glycerol Kinase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*; D012756:Sheep; D013094:Spermatozoa / Q000201:enzymology / Q000378:metabolism; D000517:alpha-Chlorohydrin / Q000494:pharmacology*
D002728:Chlorohydrins; D000517:alpha-Chlorohydrin; D010770:Phosphotransferases; D005991:Glycerol Kinase; D005990:Glycerol