Information on EC 2.7.2.12 - acetate kinase (diphosphate)

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The expected taxonomic range for this enzyme is: Entamoeba histolytica

EC NUMBER
COMMENTARY hide
2.7.2.12
-
RECOMMENDED NAME
GeneOntology No.
acetate kinase (diphosphate)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
diphosphate + acetate = phosphate + acetyl phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pyruvate metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
diphosphate:acetate phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
57657-58-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain H200
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + acetate
phosphate + acetyl phosphate
show the reaction diagram
-
-
-
-
r
diphosphate + butyrate
phosphate + butyryl phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + hexanoate
?
show the reaction diagram
-
-
-
-
?
diphosphate + valerate
phosphate + valeryl phosphate
show the reaction diagram
-
-
-
-
?
phosphate + acetyl phosphate
diphosphate + acetate
show the reaction diagram
propionate + acetate
phosphate + propionyl phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
-
employed in assay mixture
Mn2+
-
only weak activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
106 - 169
acetate
0.06 - 8
acetyl phosphate
56.5 - 75.6
Butyrate
1.9 - 16.3
diphosphate
20.4 - 20.5
hexanoate
2.2 - 48.9
phosphate
79.8 - 98.7
Propionate
41.6 - 56.7
valerate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 1.76
acetate
2 - 8333
acetyl phosphate
0.18 - 0.33
Butyrate
0.051 - 0.065
hexanoate
0.61 - 1.16
Propionate
0.19 - 0.21
valerate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0077 - 0.016
acetate
47
3846
acetyl phosphate
Entamoeba histolytica
-
37C, pH 7, wild-type
358
0.0032 - 0.0043
Butyrate
462
0.0025 - 0.0032
hexanoate
1061
0.0062 - 0.015
Propionate
312
0.0034 - 0.0049
valerate
2040
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
acetate-forming direction
45
-
acetyl phosphate-forming direction
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, under N2, stable for a week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H117A
-
mutant is inactive in the direction of acetyl phosphate formation. In the direction of acetate formation, alteration of the His117 results in a 16fold increase in the Km for acetyl phosphate and a 95fold decreased kcat, and for a 1500fold reduction in catalytic efficiency
H172A
-
mutant is inactive in the direction of acetyl phosphate formation. The His172Ala mutant has a similar Km for acetyl phosphate as wild-type, the kcat value is reduced 970fold
I116A
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mutant shows no substantial change in the Km for acetate, mutant has a 26fold decreased kcat. In the direction of acetate formation, the Ile116Ala and Ile116Leu variants both display a mild increase in the Km for acetyl phosphate and decreased kcat, resulting in 22- to 27fold-decreased catalytic efficiencies, respectively
I116L
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mutant shows no substantial change in the Km for acetate. In the direction of acetate formation, the Ile116Ala and Ile116Leu variants both display a mild increase in the Km for acetyl phosphate and decreased kcat, resulting in 22- to 27fold-decreased catalytic efficiencies, respectively
T223G
-
mutant shows significant activity in the acetate-forming direction of the assay but does not display activity in the acyl phosphate-forming direction with any acyl substrate
T223P
-
mutant shows little effect on enzyme activity in the direction of acyl phosphate formation. The enzyme remains capable of utilizing substrates as long as hexanoate, and the Km and kcat values for each substrate are comparable to wild-type. In the direction of acetate formation, the Km for acetyl phosphate increases 4fold, the kcat also shows a 4fold increase, and thus the catalytic efficiency, kcat/Km, is unchanged
V87A
-
mutant displays 16- to 20fold decreased turnover rates in the direction of acetate synthesis but no change in the Km for acetyl phosphate, and they are inactive in the acetyl phosphate-forming direction
V87G
-
mutant displays 16- to 20fold decreased turnover rates in the direction of acetate synthesis but no change in the Km for acetyl phosphate, and they are inactive in the acetyl phosphate-forming direction