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Phosphomevalonate kinase

phosphomevalonate kinase, PMKase
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. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: ACID, CAN, galactokinase, V1a, STEP
Papers on phosphomevalonate kinase
Metabolic pathway optimization using ribosome binding site variants and combinatorial gene assembly.
Keasling et al., Berkeley, United States. In Appl Microbiol Biotechnol, 2014
RBSs of various strengths, selected based on their theoretical strengths, were cloned 5' of the genes encoding mevalonate kinase, phosphomevalonate kinase, mevalonate diphosphate decarboxylase, and amorphadiene synthase.
Kinetics of phosphomevalonate kinase from Saccharomyces cerevisiae.
Keasling et al., Berkeley, United States. In Plos One, 2013
We have characterized the kinetic parameters of phosphomevalonate kinase (PMK, EC from Saccharomyces cerevisiae, a previously unstudied enzyme.
Biochemical evidence supporting the presence of the classical mevalonate pathway in the thermoacidophilic archaeon Sulfolobus solfataricus.
Hemmi et al., Nagoya, Japan. In J Biochem, 2013
The pathway is considered uncommon among archaea because the genes of the orthologues of phosphomevalonate kinase (PMK) and/or diphosphomevalonate decarboxylase (DMD) are absent in the genomes of most archaea.
Molecular docking and NMR binding studies to identify novel inhibitors of human phosphomevalonate kinase.
Sem et al., Milwaukee, United States. In Biochem Biophys Res Commun, 2013
Phosphomevalonate kinase (PMK) phosphorylates mevalonate-5-phosphate (M5P) in the mevalonate pathway, which is the sole source of isoprenoids and steroids in humans.
Functional diversity of genes for the biosynthesis of paeoniflorin and its derivatives in Paeonia.
Huang et al., Beijing, China. In Int J Mol Sci, 2012
The correlation analysis of gene expression and active compound contents support the idea that hydroxymethylglutaryl-CoA synthase and phosphomevalonate kinase in the mevalonate pathway and 3-dehydroquinate dehydratase/shikimate dehydrogenase in shikimate biosynthesis are potentially closely related to the accumulation of paeoniflorin and benzoylpaeoniflorin.
Transcriptome exploration of the sex pheromone gland of Lutzomyia longipalpis (Diptera: Psychodidae: Phlebotominae).
Brazil et al., Rio de Janeiro, Brazil. In Parasit Vectors, 2012
Among them, protein-coding transcripts for four enzymes of the mevalonate pathway such as 3-hydroxyl-3-methyl glutaryl CoA reductase, phosphomevalonate kinase, diphosphomevalonate descarboxylase, and isopentenyl pyrophosphate isomerase were identified.
Protein refolding in peroxisomes is dependent upon an HSF1-regulated function.
Lubsen et al., Nijmegen, Netherlands. In Cell Stress Chaperones, 2012
HSP90, HSPA5, HSPA6, and phosphomevalonate kinase (of which the synthesis is also downregulated by dnHSF1) had no effect on peroxisomal refolding in either control or chaperone-depleted cells.
Cycloheximide as a tool to investigate protein import in peroxisomes: a case study of the subcellular localization of isoprenoid biosynthetic enzymes.
Courdavault et al., Tours, France. In J Plant Physiol, 2012
This approach was used here successfully for the study of the subcellular localization of distinct plant isoprenoid biosynthetic enzymes, allowing us to clearly demonstrate that 5-phosphomevalonate kinase, mevalonate 5-diphosphate decarboxylase and a short isoform of farnesyl diphosphate synthase from Catharanthus roseus are exclusively localized to peroxisomes.
Subcellular evidence for the involvement of peroxisomes in plant isoprenoid biosynthesis.
Simkin et al., Tours, France. In Plant Signal Behav, 2011
In this addendum, we provide additional data describing the peroxisomal localization of 5-phosphomevalonate kinase and mevalonate 5-diphosphate decarboxylase, the last two enzymes of the mevalonic acid pathway leading to IPP.
Peroxisomal localisation of the final steps of the mevalonic acid pathway in planta.
Clastre et al., Tours, France. In Planta, 2011
Here, we have cloned the cDNA encoding enzymes catalysing the final three steps of the MVA pathway from Madagascar periwinkle (Catharanthus roseus), mevalonate kinase (MVK), 5-phosphomevalonate kinase (PMK) and mevalonate 5-diphosphate decarboxylase (MVD).
Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko, Kansas City, United States. In Arch Biochem Biophys, 2011
While bacterial enzymes responsible for these three reactions share a common protein fold, animal enzymes differ in this respect as the recently reported structure of human phosphomevalonate kinase demonstrates.
Substrate induced structural and dynamics changes in human phosphomevalonate kinase and implications for mechanism.
Sem et al., Milwaukee, United States. In Proteins, 2009
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).
Crystal structure of human phosphomevalonate kinase at 1.8 A resolution.
Liang et al., Beijing, China. In Proteins, 2008
This is the first report of hPMK crystal structure that suggests a potential substrate binding site and a possible enzyme catalytic mechanism.
Functional evaluation of conserved basic residues in human phosphomevalonate kinase.
Miziorko et al., Kansas City, United States. In Biochemistry, 2007
Functional evaluation of conserved basic residues in PMVK is reported.
Studies on biosynthetic genes and enzymes of isoprenoids produced by actinomycetes.
Dairi, Kosugi, Japan. In J Antibiot (tokyo), 2005
All these clusters contained genes coding for mevalonate kinase, mevalonate diphosphate decarboxylase, phosphomevalonate kinase, type 2 IPP isomerase, HMG-CoA reductase, and HMG-CoA synthase.
Phosphomevalonate kinase is a cytosolic protein in humans.
Waterham et al., Amsterdam, Netherlands. In J Lipid Res, 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.
Peroxisomal protein targeting and identification of peroxisomal targeting signals in cholesterol biosynthetic enzymes.
Krisans et al., San Diego, United States. In Biochim Biophys Acta, 2001
Peroxisomes have been shown to contain acetoacetyl-CoA thiolase, HMG-CoA synthase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, phosphomevalonate decarboxylase, isopentenyl diphosphate isomerase and FPP synthase.
Formation of isopentenyl diphosphate via mevalonate does not occur within etioplasts and etiochloroplasts of mustard (Sinapis alba L.) seedlings.
Kleinig et al., Freiburg, Germany. In Planta, 1987
They lack, however, any enzymatic activities for the formation of isopentenyl diphosphate via the mevalonate pathway, i.e. hydroxymethylglutaryl-CoA reductase, mevalonate kinase, phosphomevalonate kinase and diphosphomevalonate decarboxylase, which are present and easily detectable within the endoplasmic reticulum and cytoplasm.
On the compartmentation of isopentenyl diphosphate synthesis and utilization in plant cells.
Kleinig et al., Freiburg, Germany. In Planta, 1981
phosphomevalonate kinase (EC, and diphosphomevalonate decarboxylase (EC
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