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Information on EC 2.7.1.24 - dephospho-CoA kinase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WPA3

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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WPA3 not found.
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
coenzyme a synthase, dpck, dephospho-coa kinase, dephosphocoenzyme a, dephosphocoenzyme a kinase, dephospho-coenzyme a kinase, tk1697, gtp-dependent dpck, ehdpck1, ehdpck2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dephosphocoenzyme A kinase
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3'-dephospho-CoA kinase
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-
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dephosphocoenzyme A kinase
dephosphocoenzyme A kinase (phosphorylating)
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kinase, dephosphocoenzyme A (phosphorylating)
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:3'-dephospho-CoA 3'-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-83-9
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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 + 3'-dephospho-CoA
ADP + CoA
show the reaction diagram
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-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
show the reaction diagram
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-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CTP
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enzymatic activity is regulated by CTP which strongly binds the enzyme at a site overlapping that of the leading substrate, dephosphocoenzyme A, thereby obscuring the binding site and limiting catalysis. 16% residual activity at 1 mM CTP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0217 - 0.501
3'-dephospho-CoA
0.0345 - 0.0867
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.0569
3'-dephospho-CoA
0.014 - 0.067
ATP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00034 - 0.838
3'-dephospho-CoA
0.243 - 1.93
ATP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
141000
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gel filtration
47000
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3 * 47000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
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3 * 47000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D32A
the mutant shows a catalytic efficiency of only 5% of the native enzyme
D32E
the mutant shows increased catalytic efficiency compared to the wild type enzyme
D32N
the mutant shows an almost 2.54times increased Km value for 3'-dephospho-CoA compared to the wild type enzyme. The absence of magnesium completely ablates activity for the D32N mutant
G8A
this mutation does not change either the Km or the Kcat of the reaction considerably
K14A
the substitution affects the kinetic parameters of the reaction resulting in a mere 19% reduction in the Kcat of the enzyme, the mutant demonstrates a 50% increase in the Km for ATP
L114A
the mutation results in a decrease in the affinity of the enzyme for the acceptor substrate
R140A
this mutation completely abolishes kinetic activity
R140K
the mutation results in a dramatic loss of catalytic activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walia, G.; Gajendar, K.; Surolia, A.
Identification of critical residues of the mycobacterial dephosphocoenzyme A kinase by site-directed mutagenesis
PLoS ONE
6
e15228
2011
Mycobacterium tuberculosis (P9WPA3)
Manually annotated by BRENDA team
Walia, G.; Surolia, A.
Insights into the regulatory characteristics of the mycobacterial dephosphocoenzyme A kinase: implications for the universal CoA biosynthesis pathway
PLoS ONE
6
e21390
2011
Mycobacterium tuberculosis
Manually annotated by BRENDA team