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Information on EC 2.7.4.2 - phosphomevalonate kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P24521

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Saccharomyces cerevisiae
UNIPROT: P24521 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphomevalonate kinase, ccpmk, 5-phosphomevalonate kinase, mevalonate-5-phosphate kinase, mevalonate phosphate kinase, phosphomevalonic kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-phosphomevalonate kinase
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ATP:5-phosphomevalonate phosphotransferase
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kinase, phosphomevalonate (phosphorylating)
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mevalonate phosphate kinase
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mevalonate-5-phosphate kinase
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mevalonic acid phosphate kinase
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phosphomevalonic kinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-5-phosphomevalonate phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-46-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-5-phosphomevalonate
ADP + (R)-5-diphosphomevalonate
show the reaction diagram
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-
-
?
ATP + (R)-5-phosphomevalonate
ADP + 5-diphosphomevalonate
show the reaction diagram
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-
-
?
ATP + 5-phosphomevalonate
ADP + 5-diphosphomevalonate
show the reaction diagram
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maximal activity at 10 mM ATP
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-5-phosphomevalonate
ADP + (R)-5-diphosphomevalonate
show the reaction diagram
-
-
-
?
ATP + (R)-5-phosphomevalonate
ADP + 5-diphosphomevalonate
show the reaction diagram
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-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
dependent on, maximal activity achieved at concentrations of 10 mM or greater
Co2+
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can partially replace Mg2+ in activation
Fe2+
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can partially replace Mg2+ in activation
Mg2+
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divalent cation required, Mg2+ most efficient
Mn2+
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can partially replace Mg2+ in activation
Zn2+
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can partially replace Mg2+ in activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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above 10 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88 - 0.885
(R)-5-phosphomevalonate
0.0743 - 0.0983
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
the enzyme activity drops off below pH 6.5 and above pH 8.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
almost all eukaryotes, most of the MVA pathway-utilizing bacteria, and the archaea of the order Sulfolobales utilize mevalonate kinase (MVK), phosphomevalonate kinase (PMK), and diphosphomevalonate decarboxylase (DMD) for that purpose. The pathway that includes this set of enzymes is called the classical MVA pathway because it was discovered more than half a century ago
physiological function
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
ammonium sulfate, ethanol, phosphate gel, DEAE-cellulose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene ERG8, the pBAD plasmid containing the genes of MVK, PMK, and DMD from Saccharomyces cerevisiae (pBAD-ScMPD) is used for expression of a part of the classical MVA pathway (Fig. 6B). The codon usage of the MVK and PMK genes has been optimized for Escherichia coli, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bloch, K.; Chaykin, S.; Phillips, A.H.; De Waard, A.
Mevalonic acid pyrophosphate and isopentenylpyrophosphate
J. Biol. Chem.
234
2595-2604
1959
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Garcia, D.E.; Keasling, J.D.
Kinetics of phosphomevalonate kinase from Saccharomyces cerevisiae
PLoS ONE
9
e87112
2014
Saccharomyces cerevisiae (P24521), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Motoyama, K.; Sobue, F.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
Conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase by single amino acid mutations
Appl. Environ. Microbiol.
85
e00256-19
2019
Saccharomyces cerevisiae (P24521), Saccharomyces cerevisiae ATCC 204508 (P24521)
Manually annotated by BRENDA team