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Information on EC 2.7.1.36 - mevalonate kinase and Organism(s) Leishmania major and UniProt Accession Q4Q6K7

for references in articles please use BRENDA:EC2.7.1.36
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EC Tree
IUBMB Comments
CTP, GTP and UTP can also act as donors.
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This record set is specific for:
Leishmania major
UNIPROT: Q4Q6K7
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The taxonomic range for the selected organisms is: Leishmania major
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mevalonate kinase, mvk, tcmvk, mva kinase, temvk, mevalonic kinase, mevalonate phosphokinase, mevalonate 5-phosphotransferase, atp:mevalonate 5-phosphotransferase, mevalonic acid kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:mevalonate 5-phosphotransferase
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kinase, mevalonate (phosphorylating)
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mevalonate 5-phosphotransferase
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mevalonate phosphokinase
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mevalonic acid kinase
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mevalonic kinase
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MVA kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
show the reaction diagram
catalytic reaction mechanism, substrate binding structure involves key residue His25 in a deep cavity lined by highly conserved residues, Lys18, Asp155, Val202, and Thr283 are involved in catalysis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-mevalonate 5-phosphotransferase
CTP, GTP and UTP can also act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-52-2
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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)-mevalonate
ADP + (R)-5-phosphomevalonate
show the reaction diagram
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r
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)-mevalonate
ADP + (R)-5-phosphomevalonate
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
helix alpha2 and the preceding polypeptide adopt a conformation impeding access to the nucleotide triphosphate binding site suggesting that a conformational rearrangement is required to allow ATP binding, the ATP binding structure is distinct from related enzymes, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q4Q6K7_LEIMA
329
0
35485
TrEMBL
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and selenomethionine-labeled enzyme as apoenzyme and in complex with (R)-mevalonate, hanging drop vapor diffusion method, 0.002 ml of 7.5 mg/ml protein in 10 mM Tris-HCl, pH 8.5, 20 mM NaCl, and 1 mM DTT, in presence of 3-25 mM adenosine 5'-(beta,gamma-imino)triphosphate, 6-50 mM (R)-mevalonate, 10 mM Mg2+, mixing with reservoir solution containing 1.15 M sodium citrate, pH 6.2, 18°C, X-ray diffraction structure determination and analysis at 1.75-1.9 A resolution, single-wavelength anomalous dispersion, molecular replacement fails
free enzyme and in complex with mevalonate, 1.75 A and 1.9 A resolution, respectively. The mevalonate binds in a deep cavity lined by highly conserved residues. His25 is key for binding and for discrimination of (R)- over (S)-mevalonate, with the main chain amide interacting with the C3 hydroxyl group of (R)-mevalonate, and the side chain contributing, together with Val202 and Thr283, to the construction of a hydrophobic binding site for the C3 methyl substituent. The C5 hydroxyl, where phosphorylation occurs, points towards catalytic residues, Lys18 and Asp155
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and anion exchange chromatography to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and anaylsis, overexpression in a procyclic form of Trypanosoma brucei, and expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), and of His-tagged selenomethionine-labeled enzyme in Escherichia coli strain B834
expression in Trypanosoma brucei
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sgraja, T.; Smith, T.K.; Hunter, W.N.
Structure, substrate recognition and reactivity of Leishmania major mevalonate kinase
BMC Struct. Biol.
7
20
2007
Leishmania major, Leishmania major (Q4Q6K7), Trypanosoma brucei
Manually annotated by BRENDA team