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Information on EC 2.7.2.1 - acetate kinase
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2.7.2.1 acetate kinaseIUBMB Comments
Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate , others have found that the enzyme can also use propanoate as a substrate, but more slowly . 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 .
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Word Map
- 2.7.2.1
- phosphotransacetylase
- acetyl-coa
- methanosarcina
- thermophila
- acetoin
- acetobutylicum
-
formate-lyase
-
cdc42-associated
- acetylphosphate
-
adp-forming
-
acetate-activating
-
acetogenic
-
substrate-level
-
embden-meyerhof-parnas
- butyryl-coa
- industry
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ack, acetokinase, acka2, acka1, ackase, urkinase, atp-ecoak, stacka, atp-specific ak, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetate kinase (phosphorylating)
-
-
-
-
acetic kinase
-
-
-
-
acetokinase
-
-
-
-
ACK
ackA
AckA1
AckA2
AK
-
-
-
-
MM_0495
Sak
StAckA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + propanoate = ADP + propanoyl phosphate
-
-
-
-
ATP + acetate = ADP + acetyl phosphate
propanoate also acts as acceptor, but more slowly
-
-
-
ATP + acetate = ADP + acetyl phosphate
residue F179 is essential for catalysis
-
ATP + acetate = ADP + acetyl phosphate
roles for the arginine residues Arg241 and Arg91 in transition state stabilization for catalysis but not in nucleotide binding determined, experimental evidence for domain motion
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
(S)-propane-1,2-diol degradation, acetate and ATP formation from acetyl-CoA I, acetylene degradation, Bifidobacterium shunt, ethanolamine utilization, gallate degradation III (anaerobic), glycine degradation (Stickland reaction), L-lysine fermentation to acetate and butanoate, L-threonine degradation I, methanogenesis from acetate, mixed acid fermentation, purine nucleobases degradation I (anaerobic), purine nucleobases degradation II (anaerobic), pyruvate fermentation to acetate II, pyruvate fermentation to acetate IV, superpathway of fermentation (Chlamydomonas reinhardtii)
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9027-42-3
-
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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
ATP + ethanol
ADP + ethyl phosphate
-
1% of reactivity with acetate
-
-
r
ATP + glycerol
ADP + glycerol phosphate
-
1% of reactivity with acetate
-
-
r
ATP + glycine
ADP + glycyl phosphate
-
1% of reactivity with acetate
-
-
r
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
?
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
-
r
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
r
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
-
r
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
?
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
?
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
high-energy acetyl phosphate reacts with hydroxylamine forming acetyl hydroxamate and inorganic phosphate
-
-
?
ADP + acetyl phosphate
ATP + acetate
20fold more active in the reaction of acetate synthesis compared to acetate phosphorylation. The enzyme shows strong specificity to ATP and ADP
-
-
r
ADP + acetyl phosphate
ATP + acetate
20fold more active in the reaction of acetate synthesis compared to acetate phosphorylation. The enzyme shows strong specificity to ATP and ADP
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
acetate kinase/phosphotransacetylase, major role of this two-enzyme sequence is to provide acetyl coenzyme A which may participate in fatty acid synthesis, citrate formation and subsequent oxidation
-
r
ATP + acetate
ADP + acetyl phosphate
-
the equilibrium lies far to the left side
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
function in the metabolism of pyruvate or synthesis of acetyl-CoA coupling with phosphoacetyltransacetylase
-
r
ATP + acetate
ADP + acetyl phosphate
-
function in the metabolism of pyruvate or synthesis of acetyl-CoA coupling with phosphoacetyltransacetylase
-
r
ATP + acetate
ADP + acetyl phosphate
key enzyme and responsible for dephosphorylation of acetyl phosphate with the concomitant production of acetate and ATP
-
r
ATP + acetate
ADP + acetyl phosphate
acetate kinase is a key enzymes of acetate metabolism of anaerobes
-
-
?
ATP + acetate
ADP + acetyl phosphate
acetate kinase is a key enzymes of acetate metabolism of anaerobes
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
function in the initial activation of acetate for conversion to methane and CO2
-
r
ATP + acetate
ADP + acetyl phosphate
-
catalytic mechanism, roles for the arginine residues Arg241 and Arg91 in transition state stabilization for catalysis but not in nucleotide binding determined, experimental evidence for domain motion
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
activity in the reverse direction is 2.6fold greater than in the forward direction (acetate kinase activity)
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
the wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP
-
-
?
ATP + acetate
ADP + acetyl phosphate
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
-
?
ATP + acetate
ADP + acetyl phosphate
activity in the reverse direction is 2.6fold greater than in the forward direction (acetate kinase activity)
-
-
r
ATP + acetate
ADP + acetyl phosphate
the enzyme is 20fold more active in the reaction of acetate synthesis compared to acetate phosphorylation and shows strong specificity to ATP/ADP The enzyme has a remarkably high catalytic efficiency for acetate and ATP formation
-
-
r
ATP + acetate
ADP + acetyl phosphate
20fold more active in the reaction of acetate synthesis compared to acetate phosphorylation. The enzyme shows strong specificity to ATP and ADP
-
-
r
ATP + acetate
ADP + acetyl phosphate
20fold more active in the reaction of acetate synthesis compared to acetate phosphorylation. The enzyme shows strong specificity to ATP and ADP
-
-
r
ATP + acetate
ADP + acetyl phosphate
the enzyme is 20fold more active in the reaction of acetate synthesis compared to acetate phosphorylation and shows strong specificity to ATP/ADP The enzyme has a remarkably high catalytic efficiency for acetate and ATP formation
-
-
r
ATP + acetate
ADP + acetyl phosphate
transcriptional control of the ackA gene
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
enzyme assay developed that can measure the released phosphate at a nanomolar level
-
-
?
ATP + butyrate
ADP + butyryl phosphate
-
2% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
-
2% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
-
-
-
?
ATP + propionate
ADP + propionyl phosphate
-
40% lower kinase activity than acetate
-
r
ATP + propionate
ADP + propionyl phosphate
-
40% lower kinase activity than acetate
-
r
ATP + propionate
ADP + propionyl phosphate
-
one-tenth of the rate shown with acetate
-
r
ATP + propionate
ADP + propionyl phosphate
-
poor acceptor, 5% relative to acetate at 500 mM
-
r
ATP + propionate
ADP + propionyl phosphate
-
poor acceptor, 5% relative to acetate at 500 mM
-
r
ATP + propionate
ADP + propionyl phosphate
-
the enzyme phosphorylates propionate at 60% of the rate with acetate
-
-
?
ATP + propionate
ADP + propionyl phosphate
-
-
-
?
CTP + acetate
CDP + acetyl phosphate
-
activity with TP is 53% of the activity with ATP
-
-
?
CTP + acetate
CDP + acetyl phosphate
-
50% of the activity relative to that observed with ATP
-
-
?
CTP + acetate
CDP + acetyl phosphate
-
-
-
?
GTP + acetate
GDP + acetyl phosphate
-
activity with TP is 79% of the activity with ATP
-
-
?
GTP + acetate
GDP + acetyl phosphate
-
85.2% of the activity relative to that observed with ATP
-
-
?
GTP + acetate
GDP + acetyl phosphate
activity with TP is 79% of the activity with ATP
-
-
?
GTP + acetate
GDP + acetyl phosphate
-
-
-
?
ITP + acetate
IDP + acetyl phosphate
-
activity with TP is 83% of the activity with ATP
-
-
?
ITP + acetate
IDP + acetyl phosphate
-
80% of the activity relative to that observed with ATP
-
-
?
ITP + acetate
IDP + acetyl phosphate
activity with TP is 83% of the activity with ATP
-
-
?
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
TTP + acetate
TDP + acetyl phosphate
-
activity with TP is 106% of the activity with ATP
-
-
?
TTP + acetate
TDP + acetyl phosphate
-
64.5% of the activity relative to that observed with ATP
-
-
?
UTP + acetate
UDP + acetyl phosphate
-
activity with TP is 80% of the activity with ATP
-
-
?
UTP + acetate
UDP + acetyl phosphate
-
54.8% of the activity relative to that observed with ATP
-
-
?
UTP + acetate
UDP + acetyl phosphate
-
-
-
?
additional information
?
-
-
UTP is no phosphate donor, lactate, succinate, maleate formate and bicarbonate are not acceptors
-
-
-
additional information
?
-
-
UTP is no phosphate donor, lactate, succinate, maleate formate and bicarbonate are not acceptors
-
-
-
additional information
?
-
-
formate and butyrate are no substrates
-
-
-
additional information
?
-
-
neither propionic acid nor butyric acid are active as substrates
-
-
-
additional information
?
-
-
formate, butyrate and various holo and hydroxy derivatives of acetate and propionate are not phosphorylated
-
-
-
additional information
?
-
-
UTP and CTP are active only partially
-
-
-
additional information
?
-
-
formate is no substrate
-
-
-
additional information
?
-
-
UTP and CTP are active only partially
-
-
-
additional information
?
-
-
the enzyme is unable to use formate
-
-
-
additional information
?
-
the enzyme is unable to use formate
-
-
-
additional information
?
-
-
not active toward formate, butyrate, valerate and succinate
-
-
-
additional information
?
-
-
neither propionic acid nor butyric acid are active as substrates
-
-
-
additional information
?
-
-
neither propionic acid nor butyric acid are active as substrates
-
-
-
additional information
?
-
-
isobutyrate, isovalerate, 2-methylbutyrate, butyrate and valerate are no substrates
-
-
-
additional information
?
-
-
isobutyrate, isovalerate, 2-methylbutyrate, butyrate and valerate are no substrates
-
-
-
additional information
?
-
-
butyrate, isobutyrate, valerate and isovalerate are no substrates
-
-
-
additional information
?
-
-
enzyme does not react with malate, maleate, bicarbonate, butyrate, tartrate, citrate, formate or succinate
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
ATP + acetate
ADP + acetyl phosphate
-
acetate kinase/phosphotransacetylase, major role of this two-enzyme sequence is to provide acetyl coenzyme A which may participate in fatty acid synthesis, citrate formation and subsequent oxidation
-
r
ATP + acetate
ADP + acetyl phosphate
-
function in the metabolism of pyruvate or synthesis of acetyl-CoA coupling with phosphoacetyltransacetylase
-
r
ATP + acetate
ADP + acetyl phosphate
-
function in the metabolism of pyruvate or synthesis of acetyl-CoA coupling with phosphoacetyltransacetylase
-
r
ATP + acetate
ADP + acetyl phosphate
Q9F1X7
key enzyme and responsible for dephosphorylation of acetyl phosphate with the concomitant production of acetate and ATP
-
r
ATP + acetate
ADP + acetyl phosphate
P0CW04
acetate kinase is a key enzymes of acetate metabolism of anaerobes
-
-
?
ATP + acetate
ADP + acetyl phosphate
P0CW04
acetate kinase is a key enzymes of acetate metabolism of anaerobes
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
function in the initial activation of acetate for conversion to methane and CO2
-
r
ATP + acetate
ADP + acetyl phosphate
-
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
-
?
ATP + acetate
ADP + acetyl phosphate
P38502
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no activity with CTP, GTP, or UTP
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
-
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Co2+
-
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Co2+
the activity is strongly dependent on Mg2+ (100%), Mn2+ (100%) or Co2+ (68 %) ions
Co2+
Vmax: 15%, compared to Mg2+ or Mn2+
Mg2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Mg2+
-
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Mg2+
dependence on Mg2+ or Mn2+ ions, Km values is 0.28 mM
Mg2+
the activity is strongly dependent on Mg2+ (100%), Mn2+ (100%) or Co2+ (68 %) ions
Mn2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Mn2+
-
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). The maximum rate is obtained with Mn2+
Mn2+
dependence on Mg2+ or Mn2+ ions, Km values is 0.47 mM
Mn2+
the activity is strongly dependent on Mg2+ (100%), Mn2+ (100%) or Co2+ (68 %) ions
Ni2+
Vmax: 5%, compared to Mg2+ or Mn2+
additional information
-
Co2+, Ca2+, Cd2+ and Zn2+ can replace Mg2+ or Mn2+ only partially
additional information
no activity with Ba2+, Ca2+, Zn2+, or Cu2+
additional information
-
no activity with Cu2+, Ni2+, Hg2+, Ba2+ or Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetate
-
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)
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
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
D-fructose-1,6-bisphosphate
inhibits the activities of isozymes AckA1 and AckA2; inhibits the activities of isozymes AckA1 and AckA2
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
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
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
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
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
propionate
-
preincubation with MgCl2, ADP, AlCl3, NaF, and propionate results in almost complete inhibition of activity
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
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
acetyl phosphate
-
product inhibition is noncompetitive versus both acetate and ATP
ADP
-
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
additional information
-
5,5'-dithiobis(2-nitrobenzoic acid), p-chloromercuriphenylsulfonate, N-ethylmaleimide and phenylglyoxal does not affect the enzyme activity
-
additional information
-
iodoacetate and iodoacetamide does not inhibit
-
additional information
inhibitor design using the the structure of the catalytic intermediate
-
additional information
-
not inactivated by 5,5'-dithiobis(2-nitrobenzoic acid), tetranitromethane or 2-hydroxy-3-nitro-benzyl bromide
-
additional information
-
preincubation with butyrate does not significantly inhibit the enzyme
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
succinate is unnecessary for the activity of this enzyme
-
succinate
-
heterotropic allosteric effector, necessary for enzymatic activity in both directions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1 - 2
acetate
pH 7.0, temperature not specified in the publication
4.9
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
17
acetate
-
pH 7.0, 37°C, mutant H180E, H180N, produced in E. coli
18
acetate
-
pH 7.0, 37°C, unaltered wild-type enzyme, produced in E. coli
20.54
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
30
acetate
-
mutant R241A, pH 7.0, presence of 200 mM guanidine/HCl
83
acetate
-
mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl
0.28
acetyl phosphate
pH 7.5, 37°C
0.53
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme; pH 7.5, 15°C, recombinant enzyme; pH 7.5, 20°C, recombinant enzyme
0.54
acetyl phosphate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
0.55
acetyl phosphate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
0.1
ADP
co-substrate: acetate, pH 7.5, 37°C
0.5
ADP
pH 7.5, 10°C, recombinant enzyme; pH 7.5, 15°C, recombinant enzyme
0.068
ATP
-
mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl; wild-type, pH 7.0, presence of 200 mM guanidine/HCl
0.07
ATP
co-substrate: acetate, pH 7.5, 37°C
0.07
ATP
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1; pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
0.075
ATP
co-substrate: propionate, pH 7.5, 37°C
0.264
ATP
-
mutant R241A, pH 7.0, presence of 200 mM guanidine/HCl
0.48
ATP
pH 7.5, 15°C, recombinant enzyme; pH 7.5, 20°C, recombinant enzyme
1.4
ATP
-
pH 7.0, 20°C, mutants E97A, E97D, E97Q, produced in E. coli
2
ATP
-
pH 7.0, 37°C, unaltered wild-type enzyme, produced in E. coli
13.5
ATP
co-substrate: formate, pH 7.5, 37°C
0.088
CTP
co-substrate: acetate, pH 7.5, 37°C
0.078
GTP
co-substrate: acetate, pH 7.5, 37°C
0.096
UTP
co-substrate: acetate, pH 7.5, 37°C
additional information
additional information
-
assay methods for both directions of reaction
-
additional information
additional information
lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods
-
additional information
additional information
the dependence of the activity on acetate and acetyl phosphate concentrations obeys the Michaelis-Menten kinetics, whereas the dependence on ATP and ADP concentrations is sigmoidal
-
additional information
additional information
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics; the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics
-
additional information
additional information
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics; the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics
-
additional information
additional information
-
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics; the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetic analysis and mechanism, detailed overview
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additional information
additional information
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Michaelis-Menten kinetics, kinetic analysis and mechanism, detailed overview
-
additional information
additional information
-
Michaelis-Menten kinetics, thermodynamics
-
additional information
additional information
Michaelis-Menten kinetics, thermodynamics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
80
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
761
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
93
acetyl phosphate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
1105
acetyl phosphate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
1764
acetyl phosphate
pH 7.5, 37°C
1750
ADP
co-substrate: acetate, pH 7.5, 37°C
870
ATP
co-substrate: formate, pH 7.5, 37°C
900
ATP
co-substrate: propionate, pH 7.5, 37°C
1170
ATP
co-substrate: acetate, pH 7.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE