Information on EC 2.7.2.1 - acetate kinase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.7.2.1
-
RECOMMENDED NAME
GeneOntology No.
acetate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate = ADP + acetyl phosphate
show the reaction diagram
ATP + propanoate = ADP + propanoyl phosphate
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA I
-
-
acetylene degradation
-
-
Bifidobacterium shunt
-
-
gallate degradation III (anaerobic)
-
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L-lysine fermentation to acetate and butanoate
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-
methanogenesis from acetate
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mixed acid fermentation
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purine nucleobases degradation I (anaerobic)
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purine nucleobases degradation II (anaerobic)
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pyruvate fermentation to acetate II
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pyruvate fermentation to acetate IV
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superpathway of fermentation (Chlamydomonas reinhardtii)
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acetate fermentation
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purine metabolism
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Taurine and hypotaurine metabolism
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Pyruvate metabolism
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Propanoate metabolism
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Methane metabolism
-
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Carbon fixation pathways in prokaryotes
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
ATP:acetate phosphotransferase
Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].
CAS REGISTRY NUMBER
COMMENTARY hide
9027-42-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oral strain
-
-
Manually annotated by BRENDA team
oral strain
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain hit B49
TrEMBL
Manually annotated by BRENDA team
DSM20451, same nucleotide sequence accession number in EMBL/GenBank
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain ATCC 4875
TrEMBL
Manually annotated by BRENDA team
strain 217
-
-
Manually annotated by BRENDA team
strain 217
-
-
Manually annotated by BRENDA team
ATCC 27405
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 221 (ATCC 17745)
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
ackA mutants are unstable and rapidly accumulate suppressor mutations that inactivate suppressors SpxB or SpxR
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
show the reaction diagram
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
ATP + butyrate
ADP + butyryl phosphate
show the reaction diagram
ATP + ethanol
ADP + ethyl phosphate
show the reaction diagram
-
1% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
show the reaction diagram
ATP + glycerol
ADP + glycerol phosphate
show the reaction diagram
-
1% of reactivity with acetate
-
-
r
ATP + glycine
ADP + glycyl phosphate
show the reaction diagram
-
1% of reactivity with acetate
-
-
r
ATP + glycolic acid
ADP + ?
show the reaction diagram
-
4% of reactivity with acetate
-
-
r
ATP + isobutyrate
ADP + isobutyryl phosphate
show the reaction diagram
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
show the reaction diagram
CTP + acetate
CDP + acetyl phosphate
show the reaction diagram
GTP + acetate
GDP + acetyl phosphate
show the reaction diagram
ITP + acetate
IDP + acetyl phosphate
show the reaction diagram
TTP + acetate
TDP + acetyl phosphate
show the reaction diagram
UTP + acetate
UDP + acetyl phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-Trinitrobenzene sulfonic acid
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
acetate
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inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition)
acetyl phosphate
adenosine 5'-(gamma-thio)triphosphate
-
-
AlCl3
-
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Protection from inhibition by a non-hydrolyzable ATP analog or acetylphosphate. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
ATP-gamma-S
-
non-hydrolyzable inhibitor
Bromoacetate
-
-
CDP
-
preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
diethyldicarbonate
HgCl2
hydroxylamine
inhibits acetate kinase reaction in a nonlinear and noncompetitive fashion, substantial inhibition at concentrations of 704 mM and minimal inhibition at concentrations of 250 microM hydroxylamine
IDP
-
preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
iodoacetamide
-
-
Iodosobenzoate
-
-
KCl
-
activity linearly decreases from 100% (at 0 mM added KCl) to 71% at 500 mM added KCl
MgCl2
-
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
N-ethylmaleimide
NaF
-
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
p-chloromercuribenzoate
p-hydroxymercuribenzoate
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-
p-mercuribenzoate
phosphate
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-
potassium hydroxylamine
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-
Propionate
-
preincubation with MgCl2, ADP, AlCl3, NaF, and propionate results in almost complete inhibition of activity
Propionic acid
sodium hydroxylamine
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-
UDP
-
preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-glycerophosphate
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D-fructose 1,6-bisphosphate
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activates formation of ADP
D-Glucose 1,6-bisphosphate
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succinate
additional information
-
succinate is unnecessary for the activity of this enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 1573
acetate
0.0026 - 7
acetyl phosphate
0.063 - 6
ADP
0.016 - 56
ATP
33.4 - 200
Butyrate
0.088 - 15.7
CTP
0.078 - 7.4
GTP
420
isobuytyrate
-
carried out at various temperatures
0.78 - 10.7
ITP
6.2 - 1000
Propionate
0.14
Propionyl phosphate
-
pH 7.5, 30C
2.7 - 12.1
TTP
0.096 - 14.2
UTP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
190 - 1180
acetate
12 - 3869
acetyl phosphate
0.42 - 2650
ADP
0.11 - 1170
ATP
0.18 - 294
Butyrate
2.1 - 460
CTP
880
formate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
8.6 - 571
GTP
11 - 742
ITP
0.37 - 1029
Propionate
2.8 - 540
TTP
43 - 415
UTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
985
acetate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
47
6300
acetyl phosphate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
358
17650
ADP
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
co-substrate: acetate, pH 7.5, 37C
13
0.9 - 16860
ATP
4
0.2 - 148
CTP
60
68
formate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
120
1.2 - 80
GTP
37
1 - 158
ITP
229
85
Propionate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
312
0.2 - 202
TTP
523
152
UTP
Methanosarcina thermophila
-
37C, pH 7.0-7.5, wild-type enzyme
65
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
acetate
-
pH 5.5, temperature not specified in the publication; pH and temperature not specified in the publication
0.24
adenosine 5'-(gamma-thio)triphosphate
-
pH 7.0
0.0184 - 18.4
ADP
0.95 - 3.4
AlCl3
3.4
MgCl2
-
pH and temperature not specified in the publication
3
NaF
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
2,4-diaminobutyric acid
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
3
2-oxobutyrate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
7
2-oxoglutarate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
63
citrate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
75
succinate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.28
-
mutant D148A
3.4
-
mutant E384A
7
cell lysate, pH 7.0, temperature not specified in the publication
19.6
-
isoenzyme AK-II
28.3
-
isoenzyme AK-I
251
isolated enzyme, pH 7.0, temperature not specified in the publication
375 - 500
-
-
539
-
mutant N211A
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11.5
-
-
5.5 - 9
-
about 35% of maximum activity at pH 5.5 and 9.0
6 - 8.5
-
pH 6.0: about 75% of maximal activity, pH 8.5: about 65% of maximal activity, acetate kinase activity
6 - 8.5
-
about 50% activity in this range
6.5 - 8.5
assay can be performed over pH range of
7 - 8
-
most active between
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 43
20C: 75% of maximal activity, 43C: 45% of maximal activity
40 - 100
-
activity increases rapidly above 55C, enzyme does not lose activity at 80C upon incubation for 180 min