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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. Additionally we are shipping Phosphomevalonate Kinase Antibodies (59) and Phosphomevalonate Kinase Kits (4) and many more products for this protein.
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Human PMVK Protein expressed in Escherichia coli (E. coli) - ABIN3216417
Danielsen, Sylvestersen, Bekker-Jensen, Szklarczyk, Poulsen, Horn, Jensen, Mailand, Nielsen: Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. in Molecular & cellular proteomics : MCP 2011
Human PMVK Protein expressed in Escherichia coli (E. coli) - ABIN667225
Hogenboom, Tuyp, Espeel, Koster, Wanders, Waterham: Phosphomevalonate kinase is a cytosolic protein in humans. in Journal of lipid research 2004
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.