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Information on EC 2.7.1.36 - mevalonate kinase
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EC Tree
2.7.1.36 mevalonate kinaseIUBMB Comments
CTP, GTP and UTP can also act as donors.
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Word Map
- 2.7.1.36
- fever
- autoinflammatory
- cholesterol
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isoprenoids
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mediterranean
- aciduria
- hereditary
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receptor-associated
- hyperimmunoglobulinemia
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vinyl
- ketone
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cryopyrin-associated
- phosphomevalonate
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febrile
- igd
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isopentenyl
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monogenic
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farnesyl
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tnfrsf1a
- isoprene
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hyper-igd
-
anakinra
- rash
- lymphadenopathy
- hmg-coa
- inflammasome
-
geranylgeranylation
- amyloidosis
-
aphthous
- porokeratosis
- arthralgia
-
non-sterol
-
pyoderma
- nod2
- papa
- autoinflammation
- gangrenosum
-
canakinumab
- adenitis
-
pstpip1
-
hyperimmunoglobulin
- medicine
-
hepatosplenomegaly
-
cholesterogenesis
-
etanercept
-
cryopyrin
- synthesis
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mevalonate kinase, mvk, tcmvk, mva kinase, temvk, mevalonic kinase, atp mevalonate 5-phosphotransferase, mevalonate phosphokinase, mevalonate 5-phosphotransferase, atp:mevalonate 5-phosphotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
mevalonic acid kinase
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mevalonic kinase
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MVA kinase
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MVK
SSO0383
TeMVK
mevalonate phosphokinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
sequential mechanism
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ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
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
ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
role for residue E193 in interacting with the cation of the MgATP substrate, and for D204 as the catalytic base that facilitates deprotonation of the C5 hydroxyl of mevalonic acid
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ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-mevalonate 5-phosphotransferase
CTP, GTP and UTP can also act as donors.
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CAS REGISTRY NUMBER
COMMENTARY
9026-52-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenosine 5'-O-(1-thio-triphosphate) + mevalonate
adenosine 5'-O-(1-thio-diphosphate) + 5-phosphomevalonate
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40% of activity with ATP in the presence of 2 mM Mg2+
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?
adenosine 5'-O-(2-thio-triphosphate) + mevalonate
adenosine 5'-O-(2-thio-diphosphate) + 5-phosphomevalonate
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54% of activity with ATP in the presence of 2 mM Mg2+
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?
adenosine 5'-O-(3-thio-triphosphate) + mevalonate
adenosine 5'-O-(3-thio-diphosphate) + 5-phosphomevalonate
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4% of activity with ATP in the presence of 2 mM Mg2+
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?
dATP + mevalonate
dADP + phosphomevalonate
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67% of the activity with ATP
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?
dCTP + mevalonate
dCDP + phosphomevalonate
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17% of the activity with ATP
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?
dGTP + mevalonate
dGDP + phosphomevalonate
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17% of the activity with ATP
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?
TTP + mevalonate
TDP + phosphomevalonate
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15% of the activity with ATP
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?
XTP + mevalonate
XDP + phosphomevalonate
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27% of the activity with ATP
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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100% activity with ATP
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in isopentenyl diphosphate synthesis
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol synthesis
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol synthesis, decreased enzyme activity involved in mevalonic aciduria and hyperimmunoglobulin D syndrome
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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a step in the production of farnesyldiphosphate and geranylgeranyl diphosphate, overview
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol synthesis
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol, steroid hormones und terpenoids synthesis
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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a step in the mevalonate pathway, overview
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in isopentenyl diphosphate synthesis
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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the enzyme catalyzes a step in the isoprenoid biosynthetic pathway via the essential intermediate 5-diphosphomevalonate
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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substrate binding structure, overview
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?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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?
ATP + mevalonate
ADP + phosphomevalonate
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ATP is the most effective phosphate donor
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?
ATP + mevalonate
ADP + phosphomevalonate
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via mevalonate pathway involved in isoprenoid biosynthesis
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?
ATP + mevalonate
ADP + phosphomevalonate
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no activity with GTP
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?
ATP + mevalonate
ADP + phosphomevalonate
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no activity with CTP
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?
ATP + mevalonate
ADP + phosphomevalonate
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no activity with ADP
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?
ATP + mevalonate
ADP + phosphomevalonate
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mevalonate kinase is probably involved in regulation of cholesterol biosynthesis
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?
ATP + mevalonate
ADP + phosphomevalonate
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part of the cholesterol and nonsterol isoprene biosynthetic pathway
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?
ATP + mevalonate
ADP + phosphomevalonate
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involved in mevalonate pathway of terpenoid biosynthesis
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?
ATP + mevalonate
ADP + phosphomevalonate
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ATP is the most effective phosphate donor
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?
ATP + mevalonate
ADP + phosphomevalonate
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no activity with ADP, GTP and UTP
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?
ATP + mevalonate
ADP + phosphomevalonate
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no activity with ITP, UTP and ADP
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?
ATP + mevalonate
ADP + phosphomevalonate
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ATP is the most effective phosphate donor
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?
ATP + mevalonate
ADP + phosphomevalonate
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enzyme may play a key role in regulating cholesterol biosynthesis
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?
ATP + mevalonate
ADP + phosphomevalonate
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no activity with ADP
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?
ATP + mevalonate
ADP + phosphomevalonate
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stereospecific reaction with R-mevalonate
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?
ATP + mevalonate
ADP + phosphomevalonate
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ATP is the most effective phosphate donor
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ir
ATP + mevalonate
ADP + phosphomevalonate
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ATPgammaS, ATPalphaS and ATPbetaS can act as substrates in presence of different activating divalent metal cations, in the presence of Mg2+ the R diastereomers of both ATPalphaS and ATPbetaS are the preferred substrates, in presence of Cd2+ the S diastereomers are more active
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?
CTP + (R)-mevalonate
CDP + (R)-5-phosphomevalonate
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5% activity with GTP compared to ATP
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?
GTP + (R)-mevalonate
GDP + (R)-5-phosphomevalonate
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15% activity with GTP compared to ATP
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?
GTP + mevalonate
GDP + phosphomevalonate
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18% of the activity with ATP
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?
ITP + mevalonate
IDP + phosphomevalonate
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36% of activity with ATP
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?
TTP + (R)-mevalonate
TDP + (R)-5-phosphomevalonate
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11% activity with GTP compared to ATP
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?
UTP + mevalonate
UDP + phosphomevalonate
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61% of the activity with ATP
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?
additional information
?
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mevalonate kinase is directly involved in regulation of luteinizing hormone receptor expression
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?
additional information
?
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analysis of substrate and product binding by archaeal mevalonate kinase compared to eukaryotic enzymes, a striking lack of direct interactions between this archaeal MK and its substrate is detected, substrate-binding site structure, overview
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additional information
?
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the enzyme catalyzes a step in the isoprenoid biosynthetic pathway, which leads to a huge number of compounds that play important roles in plant growth and development
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?
additional information
?
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the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
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-
?
additional information
?
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the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
-
-
?
additional information
?
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the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
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?
additional information
?
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the recombinant enzyme phosphorylates racemic vinyl, ethyl, n-propyl, n-butyl, i-butyl, 2-propenyl, allyl, ethynyl, and 1-propynyl mevalonate lactone analogues, that are diphosphorylated by phosphomevalonate kinase, EC 2.7.4.2, in a second step, overview
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?
additional information
?
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the recombinant enzyme phosphorylates racemic vinyl, ethyl, n-propyl, n-butyl, i-butyl, 2-propenyl, allyl, ethynyl, and 1-propynyl mevalonate lactone analogues, that are diphosphorylated by phosphomevalonate kinase, EC 2.7.4.2, in a second step, overview
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?
additional information
?
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a coupled assay method is performed using lactic dehydrogenase and pyruvate kinase. Specific activity of the three different oligomeric states of purified TeMVK is evaluated using a fluorescence-based assay. TeMVK is highly active only in its tetrameric form
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additional information
?
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Trypanosoma evansi 29-19
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a coupled assay method is performed using lactic dehydrogenase and pyruvate kinase. Specific activity of the three different oligomeric states of purified TeMVK is evaluated using a fluorescence-based assay. TeMVK is highly active only in its tetrameric form
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