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
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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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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
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acetylene degradation
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Bifidobacterium shunt
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Carbon fixation pathways in prokaryotes
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gallate degradation III (anaerobic)
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L-lysine fermentation to acetate and butanoate
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Metabolic pathways
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Methane metabolism
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methanogenesis from acetate
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Microbial metabolism in diverse environments
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mixed acid fermentation
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Propanoate metabolism
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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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Pyruvate metabolism
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superpathway of fermentation (Chlamydomonas reinhardtii)
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Taurine and hypotaurine metabolism
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acetate fermentation
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purine metabolism
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oral strain
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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
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Manually annotated by BRENDA team
gene ack
UniProt
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
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Manually annotated by BRENDA team
strain 217
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Manually annotated by BRENDA team
ATCC 27405
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-
Manually annotated by BRENDA team
gene ackA
UniProt
Manually annotated by BRENDA team
gene ackA
UniProt
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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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
evolution
malfunction
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ackA mutants are unstable and rapidly accumulate suppressor mutations that inactivate suppressors SpxB or SpxR
metabolism
physiological function
additional information
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
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1% of reactivity with acetate
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r
ATP + formate
ADP + formyl phosphate
show the reaction diagram
ATP + glycerol
ADP + glycerol phosphate
show the reaction diagram
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1% of reactivity with acetate
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r
ATP + glycine
ADP + glycyl phosphate
show the reaction diagram
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1% of reactivity with acetate
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r
ATP + glycolic acid
ADP + ?
show the reaction diagram
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4% of reactivity with acetate
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r
ATP + isobutyrate
ADP + isobutyryl phosphate
show the reaction diagram
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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
?
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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
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-Trinitrobenzene sulfonic acid
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5,5'-dithiobis(2-nitrobenzoic acid)
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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
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AlCl3
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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). 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
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non-hydrolyzable inhibitor
Bromoacetate
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CDP
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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
D-fructose-1,6-bisphosphate
inhibits the activities of isozymes AckA1 and AckA2; inhibits the activities of isozymes AckA1 and AckA2
diethyldicarbonate
glyceraldehyde-3-phosphate
inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2; inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2
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
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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
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Iodosobenzoate
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KCl
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activity linearly decreases from 100% (at 0 mM added KCl) to 71% at 500 mM added KCl
MgCl2
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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). 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
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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). 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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phospho-enol-pyruvate
PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM; PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM
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potassium hydroxylamine
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propionate
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preincubation with MgCl2, ADP, AlCl3, NaF, and propionate results in almost complete inhibition of activity
propionic acid
sodium hydroxylamine
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trifluoroethanol
leads to reduced growth and acetate content, binding mode by molecular docking
trifluoroethyl butyrate
leads to reduced growth and acetate content, binding mode by molecular docking
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UDP
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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
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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
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carried out at various temperatures
0.78 - 10.7
ITP
6.2 - 1000
propionate
0.14
Propionyl phosphate
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pH 7.5, 30°C
2.7 - 12.1
TTP
0.096 - 14.2
UTP
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80 - 1420
acetate
12 - 3869
acetyl phosphate
0.42 - 3515
ADP
0.11 - 1500
ATP
0.18 - 294
Butyrate
2.1 - 460
CTP
880
formate
Salmonella enterica subsp. enterica serovar Typhimurium
P63411
pH 7.5, 37°C
8.6 - 571
GTP
11 - 742
ITP
0.37 - 1029
propionate
2.8 - 540
TTP
2.8 - 415
UTP