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PMVK encodes a peroxisomal enzyme that catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate, the fifth reaction of the cholesterol biosynthetic pathway.
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Data indicate that exome sequencing revealed disseminated superficial porokeratosis (DSP)-associated mutations in phosphomevalonate kinase gene (PMVK).
found an exclusive cytosolic localization of both endogenously expressed PMVK(in human fibroblasts, human liver, and HEK293 cells) and overexpressed PMVK. No indication of a peroxisomal localization was obtained.
Functional evaluation of conserved basic residues in PMVK is reported.
This is the first report of hPMK crystal structure that suggests a potential substrate binding site and a possible enzyme catalytic mechanism.
Binding of mevalonate 5-phosphate causes the phosphomevalonate kinase structure to compress (tau(c) = 13.5 nsec), whereas subsequent binding of Mg-ADP opens the structure up (tau(c) = 15.6 nsec).
This gene encodes a peroxisomal enzyme that catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate, the fifth reaction of the cholesterol biosynthetic pathway. Studies in rat show that the message level and the enzyme activity of this protein is regulated by sterol, and that this regulation is coordinated with 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol biosynthesis.