Characterization of phosphomevalonate kinase: Chromosomal localization, regulation, and subcellular targeting

Lisa M. Olivier, Ken L. Chambliss, K. Michael Gibson, Skaidrite K. Krisans

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Phosphomevalonate kinase catalyzes the conversion of mevalonate-5- phosphate to mevalonate-5-diphosphate and was originally believed to be a cytosolic enzyme. In this study we have localized the phosphomevalonate kinase gene to chromosome 1p13-1q22-23 and present a genomic map indicating that the gene spans more than 8.4 kb in the human genome. Furthermore, we show that message levels and enzyme activity of rat liver phosphomevalonate kinase are regulated in response to dietary sterol levels and that this regulation is coordinate with 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol biosynthesis. In addition, we demonstrate that phosphomevalonate kinase is a peroxisomal protein which requires the C-terminal peroxisomal targeting signal, Ser-Arg-Leu, for localization to the organelle.

Original languageEnglish (US)
Pages (from-to)672-679
Number of pages8
JournalJournal of lipid research
Issue number4
StatePublished - Apr 1999
Externally publishedYes


  • 3-hydroxy-3-methylglutaryl CoA
  • Dietary sterols
  • Peroxisomes

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology


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