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Gene Review

MVD1  -  diphosphomevalonate decarboxylase MVD1

Saccharomyces cerevisiae S288c

Synonyms: Diphosphomevalonate decarboxylase, ERG19, Ergosterol biosynthesis protein 19, MDD, MDDase, ...
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Disease relevance of MVD1

  • Because mevalonate pyrophosphate decarboxylase is a unique enzyme in the cholesterol biosynthetic pathway it is a potential therapeutic target for the treatment of hypercholesterolemia and other diseases [1].

High impact information on MVD1

  • Mevalonate-5-diphosphate decarboxylase (MDD) is a single-domain alpha/beta protein that catalyzes the last of three sequential ATP-dependent reactions which convert mevalonate to isopentenyl diphosphate [2].
  • New sequence relationships were detected, including similarities between diphosphomevalonate decarboxylase and kinases of the galactokinase superfamily, between the metazoan phosphomevalonate kinase and the nucleoside monophosphate kinase superfamily, and between isopentenyl pyrophosphate isomerases and MutT pyrophosphohydrolases [3].
  • Alignment of more than 20 deduced sequences for mevalonate diphosphate decarboxylase (MDD) indicates that serines 34, 36, 120,121, 153, and 155 are invariant residues that map within a proposed interdomain active site cleft [4].
  • A combination of sequence homology analyses of mevalonate diphosphate decarboxylase (MDD) proteins and structural information for MDD leads to the hypothesis that Asp 302 and Lys 18 are active site residues in MDD [5].
  • When expressed in yeast, the A. thaliana cDNA complemented both the thermosensitive MN19-34 strain deficient in MVD, and the lethal phenotype of an ERG19 deleted strain [6].

Biological context of MVD1

  • Complementation experiments were done both in the erg19-mutated background and in a strain in which the ERG19 gene, which was shown to be an essential gene for yeast, was disrupted [7].
  • The Saccharomyces cerevisiae mevalonate diphosphate decarboxylase (erg19p) forms homodimers in vivo, and a single substitution in a structurally conserved region impairs dimerization [8].
  • Availability of C. neoformans MPD1 should permit direct testing of the hypotheses that (i) MPD is required for mannitol biosynthesis and (ii) the ability to synthesize mannitol is essential for wild-type stress tolerance and virulence [9].

Anatomical context of MVD1

  • Mannosylphosphodolichol synthase (MPD-synthase) (EC catalyzing formation of MPD from GDPMan and dolichylphosphate (PD) has been purified from T. reesei cellular membranes almost to homogeneity [10].

Associations of MVD1 with chemical compounds

  • Yeast mutant strains auxotrophic for ergosterol and blocked in mevalonate diphosphate decarboxylase (erg19) and farnesyl diphosphate (FPP) synthetase (erg20) were isolated [11].
  • Furthermore, during the course of this study, we observed that a high level of expression of the wild-type ERG19 gene led to a lower sterol steady-state accumulation compared to that of a wild-type strain, suggesting that this enzyme may be a key enzyme in mevalonate pathway regulation [7].
  • Lastly, Northern analyses demonstrated MPD mRNA in glucose- and mannitol-grown C. neoformans cells [9].
  • Guamerin, a small peptide inhibitor of the serine protease from Hirudo nipponia, was expressed in yeast and crystallized using the vapor diffusion method, with MPD as precipitant [12].

Analytical, diagnostic and therapeutic context of MVD1

  • Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase [1].


  1. Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. Toth, M.J., Huwyler, L. J. Biol. Chem. (1996) [Pubmed]
  2. Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Bonanno, J.B., Edo, C., Eswar, N., Pieper, U., Romanowski, M.J., Ilyin, V., Gerchman, S.E., Kycia, H., Studier, F.W., Sali, A., Burley, S.K. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  3. Biosynthesis of isoprenoids via mevalonate in Archaea: the lost pathway. Smit, A., Mushegian, A. Genome Res. (2000) [Pubmed]
  4. Investigation of the functional contributions of invariant serine residues in yeast mevalonate diphosphate decarboxylase. Krepkiy, D.V., Miziorko, H.M. Biochemistry (2005) [Pubmed]
  5. Identification of active site residues in mevalonate diphosphate decarboxylase: implications for a family of phosphotransferases. Krepkiy, D., Miziorko, H.M. Protein Sci. (2004) [Pubmed]
  6. Heterologous expression in Saccharomyces cerevisiae of an Arabidopsis thaliana cDNA encoding mevalonate diphosphate decarboxylase. Cordier, H., Karst, F., Bergès, T. Plant Mol. Biol. (1999) [Pubmed]
  7. The Saccharomyces cerevisiae mevalonate diphosphate decarboxylase is essential for viability, and a single Leu-to-Pro mutation in a conserved sequence leads to thermosensitivity. Bergès, T., Guyonnet, D., Karst, F. J. Bacteriol. (1997) [Pubmed]
  8. The Saccharomyces cerevisiae mevalonate diphosphate decarboxylase (erg19p) forms homodimers in vivo, and a single substitution in a structurally conserved region impairs dimerization. Cordier, H., Lacombe, C., Karst, F., Bergès, T. Curr. Microbiol. (1999) [Pubmed]
  9. Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase. Suvarna, K., Bartiss, A., Wong, B. Microbiology (Reading, Engl.) (2000) [Pubmed]
  10. Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei. Kruszewska, J.S., Perlińska-Lenart, U., Palamarczyk, G. Acta Biochim. Pol. (1996) [Pubmed]
  11. Sterol pathway in yeast. Identification and properties of mutant strains defective in mevalonate diphosphate decarboxylase and farnesyl diphosphate synthetase. Chambon, C., Ladeveze, V., Servouse, M., Blanchard, L., Javelot, C., Vladescu, B., Karst, F. Lipids (1991) [Pubmed]
  12. Crystallization and preliminary X-ray crystallographic study of the leech protease inhibitor guamerin and its complex with bovine pancreatic chymotrypsin. Kim, D.R., Kim, D.Y., Chu, T.T., Jung, K.H., Kim, K.K. Biochim. Biophys. Acta (2004) [Pubmed]
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