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Gene Review

PMVK  -  phosphomevalonate kinase

Homo sapiens

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Disease relevance of PMVK


High impact information on PMVK

  • Phosphomevalonate kinase catalyzes an essential step in the so-called mevalonate pathway, which appears to be the sole pathway for the biosynthesis of sterols and other isoprenoids in mammals and archea [1].
  • Analysis of transcripts from human lymphoblasts subcultured in lipid-depleted sera (LDS) and LDS supplemented with lovastatin indicated that PMKase gene expression is subject to regulation by sterol at the level of transcription [4].
  • Southern blotting indicated that PMKase is a single copy gene covering less than 15 kb in the human genome [4].
  • The human PMKase amino acid sequence contains a consensus peroxisomal targeting sequence (PTS-1), Ser-Arg-Leu, at the C terminus of the protein [4].
  • PMK catalyzes a reversible reaction; kinetic constants of human PMK have been determined for both forward (formation of mevalonate 5-diphosphate) and reverse (formation of mevalonate 5-phosphate) reactions [5].

Biological context of PMVK


Anatomical context of PMVK


Associations of PMVK with chemical compounds


Analytical, diagnostic and therapeutic context of PMVK


  1. The kinetic mechanism of phosphomevalonate kinase. Pilloff, D., Dabovic, K., Romanowski, M.J., Bonanno, J.B., Doherty, M., Burley, S.K., Leyh, T.S. J. Biol. Chem. (2003) [Pubmed]
  2. Molecular functions of conserved aspects of the GHMP kinase family. Andreassi, J.L., Leyh, T.S. Biochemistry (2004) [Pubmed]
  3. Enterococcus faecalis phosphomevalonate kinase. Doun, S.S., Burgner, J.W., Briggs, S.D., Rodwell, V.W. Protein Sci. (2005) [Pubmed]
  4. Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence. Chambliss, K.L., Slaughter, C.A., Schreiner, R., Hoffmann, G.F., Gibson, K.M. J. Biol. Chem. (1996) [Pubmed]
  5. Phosphomevalonate kinase: functional investigation of the recombinant human enzyme. Herdendorf, T.J., Miziorko, H.M. Biochemistry (2006) [Pubmed]
  6. Pig liver phosphomevalonate kinase: Kinetic mechanism. Eyzaguirre, J., Valdebenito, D., Cardemil, E. Arch. Biochem. Biophys. (2006) [Pubmed]
  7. Differential deficiency of mevalonate kinase and phosphomevalonate kinase in patients with distinct defects in peroxisome biogenesis: evidence for a major role of peroxisomes in cholesterol biosynthesis. Wanders, R.J., Romeijn, G.J. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  8. Time series of long-term annual fluxes in the streamwater of nine forest catchments from the Swedish environmental monitoring program (PMK 5). Fölster, J., Bishop, K., Krám, P., Kvarnäs, H., Wilander, A. Sci. Total Environ. (2003) [Pubmed]
  9. Characterization of phosphomevalonate kinase: chromosomal localization, regulation, and subcellular targeting. Olivier, L.M., Chambliss, K.L., Gibson, K.M., Krisans, S.K. J. Lipid Res. (1999) [Pubmed]
  10. Phosphomevalonate kinase is a cytosolic protein in humans. Hogenboom, S., Tuyp, J.J., Espeel, M., Koster, J., Wanders, R.J., Waterham, H.R. J. Lipid Res. (2004) [Pubmed]
  11. Microplate enzyme-coupled assays of mevalonate and phosphomevalonate kinase from Catharanthus roseus suspension cultured cells. Schulte, A.E., van der Heijden, R., Verpoorte, R. Anal. Biochem. (1999) [Pubmed]
  12. Identification of peroxisomal targeting signals in cholesterol biosynthetic enzymes. AA-CoA thiolase, hmg-coa synthase, MPPD, and FPP synthase. Olivier, L.M., Kovacs, W., Masuda, K., Keller, G.A., Krisans, S.K. J. Lipid Res. (2000) [Pubmed]
  13. Determination of synthesis route of 1-(3,4-methylenedioxyphenyl)-2-propanone (MDP-2-P) based on impurity profiles of MDMA. Swist, M., Wilamowski, J., Zuba, D., Kochana, J., Parczewski, A. Forensic Sci. Int. (2005) [Pubmed]
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