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.