Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
ADP + acetyl phosphate
ATP + acetate
ATP + acetate
ADP + acetyl phosphate
ATP + butyrate
ADP + butyryl phosphate
ATP + ethanol
ADP + ethyl phosphate
-
1% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
ATP + glycerol
ADP + glycerol phosphate
-
1% of reactivity with acetate
-
-
r
ATP + glycine
ADP + glycyl phosphate
-
1% of reactivity with acetate
-
-
r
ATP + glycolic acid
ADP + ?
-
4% of reactivity with acetate
-
-
r
ATP + heptanoate
ADP + heptyl phosphate
-
22% activity compared to acetate
-
-
r
ATP + hexanoate
ADP + hexyl phosphate
-
38% activity compared to acetate
-
-
r
ATP + isobutyrate
ADP + isobutyryl phosphate
ATP + octanoate
ADP + octyl phosphate
-
8.4% activity compared to acetate
-
-
r
ATP + propionate
ADP + propionyl phosphate
ATP + valerate
ADP + valeryl phosphate
-
43.3% activity compared to acetate
-
-
r
CTP + acetate
CDP + acetyl phosphate
GTP + acetate
GDP + acetyl phosphate
ITP + acetate
IDP + acetyl phosphate
TTP + acetate
TDP + acetyl phosphate
UTP + acetate
UDP + acetyl phosphate
additional information
?
-
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
?
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
-
-
-
?
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
-
-
-
r
ADP + acetyl phosphate
ATP + acetate
-
-
-
-
?
ADP + acetyl phosphate
ATP + acetate
-
-
-
-
r
ADP + acetyl phosphate
ATP + acetate
-
-
-
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
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
-
-
-
r
ADP + acetyl phosphate
ATP + acetate
-
-
-
r
ADP + acetyl phosphate
ATP + acetate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
100% activity
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
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
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
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
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
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
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
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
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
acetate kinase is a key enzymes of acetate metabolism of anaerobes
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
acetate kinase is a key enzymes of acetate metabolism of anaerobes
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
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
-
-
-
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
-
-
-
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
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
transcriptional control of the ackA gene
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
highest activity
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
enzyme assay developed that can measure the released phosphate at a nanomolar level
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
ADP + acetyl phosphate
-
-
-
r
ATP + butyrate
ADP + butyryl phosphate
-
59.5% activity compared to acetate
-
-
r
ATP + butyrate
ADP + butyryl phosphate
-
-
-
-
r
ATP + butyrate
ADP + butyryl phosphate
-
2% of reactivity with acetate
-
-
r
ATP + butyrate
ADP + butyryl phosphate
-
-
-
r
ATP + formate
ADP + formyl phosphate
-
2% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
-
-
-
?
ATP + isobutyrate
ADP + isobutyryl phosphate
-
26.7% activity compared to acetate
-
-
r
ATP + isobutyrate
ADP + isobutyryl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
93.3% activity compared to acetate
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
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
-
-
-
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
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
the enzyme phosphorylates propionate at 60% of the rate with acetate
-
-
?
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
?
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
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
-
-
-
-
?
CTP + acetate
CDP + acetyl phosphate
-
-
-
?
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
CTP + acetate
CDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
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
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
-
?
GTP + acetate
GDP + acetyl phosphate
-
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
?
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
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
-
-
-
-
?
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
-
-
-
r
TTP + acetate
TDP + 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
-
-
?
TTP + acetate
TDP + acetyl phosphate
-
-
-
r
TTP + acetate
TDP + acetyl phosphate
-
-
-
r
UTP + acetate
UDP + acetyl phosphate
-
-
-
r
UTP + acetate
UDP + acetyl phosphate
-
-
-
r
UTP + acetate
UDP + acetyl phosphate
-
-
-
r
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
-
-
-
r
UTP + acetate
UDP + acetyl phosphate
-
-
-
-
?
UTP + acetate
UDP + acetyl phosphate
-
-
-
?
UTP + acetate
UDP + acetyl phosphate
-
-
-
r
UTP + acetate
UDP + acetyl phosphate
-
-
-
r
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
?
-
-
butyrate is no substrate
-
-
?
additional information
?
-
-
butyrate is no substrate
-
-
?
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
?
-
no activity with diphosphate
-
-
?
additional information
?
-
-
no activity with diphosphate
-
-
?
additional information
?
-
-
UTP and CTP are active only partially
-
-
?
additional information
?
-
-
formate is no substrate
-
-
?
additional information
?
-
-
formate is no substrate
-
-
?
additional information
?
-
-
UTP and CTP are active only partially
-
-
?
additional information
?
-
-
formate is no substrate
-
-
?
additional information
?
-
the enzyme is unable to use formate
-
-
?
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
?
-
-
no activity with AMP-PCP, CTP or TTP
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4,6-Trinitrobenzene sulfonic acid
-
-
2,4-diaminobutyric acid
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
6-oxopiperidine-3-carboxylic acid
-
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)
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
Ca2+
less than 1% residual activity at 1.3 mM
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
diphosphate
about 70% inhibition in the acetate-forming direction and about 90% inhibition in the acetyl phosphate-forming direction
EDTA
complete inhibition at 1.3 mM
eugenyl acetate
66.52% inhibition at 70 mM
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
p-hydroxymercuribenzoate
-
-
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
pinoresinol
82.6% inhibition at 70 mM
potassium hydroxylamine
-
-
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
Zn2+
less than 5% residual activity at 1.3 mM
6-oxopiperidine-3-carboxylic acid
82.6% inhibition at 70 mM
-
6-oxopiperidine-3-carboxylic acid
-
-
acetyl phosphate
-
-
acetyl phosphate
-
product inhibition
acetyl phosphate
-
product inhibition is noncompetitive versus both acetate and ATP
ADP
-
-
ADP
competitive inhibition; competitive inhibition
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
chlorogenic acid
58.74% inhibition at 70 mM
diethyldicarbonate
-
-
HgCl2
-
-
Li+
-
-
N-ethylmaleimide
-
-
Na+
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-mercuribenzoate
-
-
propionic acid
-
competitive inhibitor with respect to acetate
additional information
-
not inactivated by N-ethylmaleimide
-
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
-
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
-
not inactivated by N-ethylmaleimide
-
additional information
preincubation with butyrate does not significantly inhibit the enzyme
-
additional information
-
preincubation with butyrate does not significantly inhibit the enzyme
-
additional information
not inhibited by phosphate
-
additional information
-
not inhibited by phosphate
-
additional information
not inhibited by eugenyl acetate and pinoresinol
-
additional information
-
not inhibited by eugenyl acetate and pinoresinol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0026 - 7
acetyl phosphate
13.5
formate
pH 7.5, 37°C
109
Isobutyrate
-
at pH 5.7 and 37°C
420
isobuytyrate
-
carried out at various temperatures
0.14
Propionyl phosphate
-
pH 7.5, 30°C
14.2
valerate
-
at pH 5.7 and 37°C
additional information
additional information
-
0.7
acetate
-
acetate kinase EutP, at 40°C, pH not specified in the publication
0.7
acetate
-
acetate kinase EutQ, at 40°C, pH not specified in the publication
1 - 2
acetate
pH 7.0, temperature not specified in the publication
1.5
acetate
-
wild-type, pH 7.0
1.61
acetate
pH 7.5, 10°C, recombinant enzyme
1.63
acetate
pH 7.5, 15°C, recombinant enzyme
1.71
acetate
pH 7.5, 20°C, recombinant enzyme
1.77
acetate
pH 7.5, 25°C, recombinant enzyme
2.3
acetate
-
pH 7.0, 20°C, mutant E97A, produced in E. coli
2.7
acetate
wild-type, pH 7.0
2.8
acetate
-
mutant E97D, pH 7.5, 37°C
4
acetate
-
pH 7.6, 37°C, mutant R175K
4
acetate
-
pH 7.0, 20°C, mutant E97Q, produced in E. coli
4.9
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
5.6
acetate
-
pH 8.0, 30°C
5.8
acetate
R241A/Q43W, double mutant
7.2
acetate
-
pH 7.0, 20°C, mutant E97D, produced in E. coli
10
acetate
-
pH 7.0, 37°C, mutant H180R, produced in E. coli
10.4
acetate
-
mutant F179A, pH 7.0
11.7
acetate
-
pH 7.5, 30°C, isoenzyme I
12.4
acetate
Q43W, mutant
13
acetate
-
pH 7.0, 37°C, mutant H180D, produced in E. coli
14
acetate
-
pH 7.0, 37°C, mutant H180Q, produced in E. coli
14.3
acetate
37°C, pH 7.0-7.5, wild-type enzyme
15
acetate
-
pH 7.0, 20°C, mutant E334A, produced in E. coli
15
acetate
-
pH 7.0, 37°C, mutant H184A, produced in E. coli
16
acetate
-
pH 7.0, 37°C, mutant H123A, produced in E. coli
17
acetate
-
pH 7.0, 20°C, mutant E385C, produced in E. coli
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
19
acetate
-
pH 7.6, 37°C
19
acetate
-
pH 7.0, 20°C, unaltered enzyme, produced in E. coli
19
acetate
-
pH 7.0, 37°C, mutant H180K, produced in E. coli
19.5
acetate
-
mutant L122A, pH 7.0
20
acetate
-
pH 7.6, 37°C, mutant R340L
20
acetate
-
pH 7.0, 37°C, mutant H60A, produced in E. coli
20
acetate
wild type enzyme, at pH 5.5 and 45°C
20.54
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
21.4
acetate
-
mutant V93A, pH 7.0
22
acetate
-
pH 7.3, 37°C
22
acetate
-
wild-type, pH 7.5, 37°C
22
acetate
-
pH 7.0, 37°C, authentic wild-type enzyme
22
acetate
37°C, pH is not specified in the publication
24
acetate
wild-type, pH 7.0, presence of 200 mM guanidine/HCl
26
acetate
-
pH 7.0, 20°C, mutant E32A, produced in E. coli
29.3
acetate
pH 7.5, 25°C, recombinant enzyme
30
acetate
-
pH 7.4, 37°C
30
acetate
mutant R241A, pH 7.0, presence of 200 mM guanidine/HCl
31.32
acetate
pH 7.5, 20°C, recombinant enzyme
32
acetate
-
mutant P232A, pH 7.0
32.26
acetate
pH 7.5, 15°C, recombinant enzyme
33
acetate
-
pH 7.0, 37°C, mutant H208A, produced in E. coli
36.02
acetate
pH 7.5, 10°C, recombinant enzyme
38.5
acetate
-
pH 7.4, 25°C
38.5
acetate
-
pH 7.5, 30°C, isoenzyme II
39.5
acetate
-
mutant V93G, pH 7.0
40
acetate
-
pH 7.0, 50°C
40
acetate
-
carried out at various temperatures
42
acetate
-
pH 7.6, 37°C, mutant R340K
44
acetate
-
pH 7.0, 20°C, mutant E385Q, produced in E. coli
48
acetate
-
pH 7.4, 37°C, wild-type
48
acetate
R91K/Q43W, double mutant
53.9
acetate
-
at pH 5.7 and 37°C
66
acetate
-
pH 7.0, 37°C, mutant H94A, produced in E. coli
70
acetate
mutant R91K, pH 7.0
73
acetate
-
pH 7.3, 30°C
77
acetate
mutant R241K, pH 7.0
80.9
acetate
-
pH 7.5, 30°C
83
acetate
mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl
86
acetate
-
pH 7.0, 20°C, mutant E385A, produced in E. coli
94
acetate
37°C, pH 7.0-7.5, mutant enzyme G239S
100
acetate
-
pH 7.3, 37°C, 50 M succinate
111
acetate
-
pH 7.4, 37°C, mutant N211A
113
acetate
37°C, pH 7.0-7.5, mutant enzyme G239A
129
acetate
-
pH 7.6, 37°C, mutant R285L
135
acetate
-
pH 7.2-8.0, 50°C
140
acetate
37°C, pH 7.0-7.5, mutant enzyme N211S
160
acetate
-
pH 7.0, 36°C
165
acetate
37°C, pH 7.0-7.5, mutant enzyme N211A
170
acetate
-
pH 7.4, 37°C, mutant D148A
170
acetate
-
pH 7.3, 37°C, 5.0 M succinate
179
acetate
R241K/Q43W, double mutant
200
acetate
-
pH 7.4, 37°C, mutant S11A
206
acetate
-
pH 7.6, 37°C, mutant R285A
219
acetate
-
pH 7.6, 37°C, mutant R285K
239
acetate
-
pH 7.4, 37°C, mutant K14R
250
acetate
mutant R91A, pH 7.0
260
acetate
-
pH 7.6, 37°C, mutant R91K
266
acetate
-
pH 7.4, 37°C, mutant S10T
270
acetate
mutant R241L, pH 7.0
302
acetate
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
330
acetate
-
pH 7.0, 37°C, mutant H90A, produced in E. coli
333
acetate
-
pH 7.4, 37°C, mutant S12T
337
acetate
-
pH 7.0, 20°C, mutant E385D, produced in E. coli
390
acetate
-
pH 7.4, 37°C, mutant D148N
420
acetate
mutant R91L, pH 7.0
470
acetate
37°C, pH 7.0-7.5, mutant enzyme N211T
601
acetate
37°C, pH 7.0-7.5, mutant enzyme G331A
693
acetate
-
pH 7.4, 37°C, mutant N7D
710
acetate
mutant R241A, pH 7.0
800
acetate
-
pH 7.3, 37°C
814
acetate
-
pH 7.4, 37°C, mutant S10A
1573
acetate
-
pH 7.4, 37°C, mutant S11T
0.0026
acetyl phosphate
-
carried out at various temperatures
0.0222
acetyl phosphate
at pH 8.0 and 37°C
0.1
acetyl phosphate
-
pH 7.4, 25°C
0.11
acetyl phosphate
pH 8.0, 30°C
0.11
acetyl phosphate
-
pH 8.0, 30°C
0.15
acetyl phosphate
-
mutant F179A, pH 7.4
0.16
acetyl phosphate
-
-
0.16
acetyl phosphate
-
pH 7.9, 37°C
0.2
acetyl phosphate
-
pH 7.4, 25°C, 0.5 M NaCl
0.26
acetyl phosphate
Q43W
0.28
acetyl phosphate
pH 7.5, 37°C
0.33
acetyl phosphate
R241/Q43W
0.34
acetyl phosphate
-
wild-type, pH 7.4
0.44
acetyl phosphate
-
pH 7.5, 30°C
0.44
acetyl phosphate
-
pH 7.0, 50°C
0.47
acetyl phosphate
wild-type
0.47
acetyl phosphate
wild-type, pH 7.4
0.5
acetyl phosphate
pH 7.5, 25°C, recombinant enzyme
0.5
acetyl phosphate
-
mutant L122A, pH 7.4
0.53
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme
0.53
acetyl phosphate
pH 7.5, 15°C, recombinant enzyme
0.53
acetyl phosphate
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
0.58
acetyl phosphate
-
pH 7.3, 30°C
0.59
acetyl phosphate
pH 7.5, 25°C, recombinant enzyme
0.61
acetyl phosphate
mutant R91K, pH 7.4
0.67
acetyl phosphate
pH 7.5, 20°C, recombinant enzyme
0.69
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme
0.71
acetyl phosphate
-
mutant V93G, pH 7.4
0.71
acetyl phosphate
pH 7.5, 15°C, recombinant enzyme
0.74
acetyl phosphate
-
mutant V93A, pH 7.4
0.84
acetyl phosphate
mutant R241A, pH 7.4
0.92
acetyl phosphate
mutant R241K, pH 7.4
1
acetyl phosphate
pH 7.5, 30°C
1.02
acetyl phosphate
R241K/Q43W
1.08
acetyl phosphate
R91K/Q43W
1.19
acetyl phosphate
-
mutant P232A, pH 7.4
1.2
acetyl phosphate
-
pH 7.4, 37°C
1.2
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
1.36
acetyl phosphate
mutant R91A, pH 7.4
1.64
acetyl phosphate
mutant R241L, pH 7.4
1.7
acetyl phosphate
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
2.3
acetyl phosphate
mutant R91L, pH 7.4
2.58
acetyl phosphate
R91A/Q43W
3.3
acetyl phosphate
-
pH 7.3, 37°C, 2.0 M succinate
5
acetyl phosphate
-
pH 7.4
5
acetyl phosphate
-
pH 7.3, 37°C, 0.2 M succinate
7
acetyl phosphate
-
pH 7.3, 37°C
0.063
ADP
mutant R91A, pH 7.4
0.063
ADP
mutant R91L, pH 7.4
0.087
ADP
-
carried out at various temperatures
0.098
ADP
wild-type, pH 7.4
0.1
ADP
co-substrate: acetate, pH 7.5, 37°C
0.147
ADP
R91A/Q43W, double mutant
0.164
ADP
R91K/Q43W, double mutant
0.168
ADP
mutant R91K, pH 7.4
0.188
ADP
at pH 8.0 and 37°C
0.21
ADP
mutant R241A, pH 7.4
0.239
ADP
R241A/Q43W, double mutant
0.47
ADP
pH 7.5, 25°C, recombinant enzyme
0.47
ADP
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
0.49
ADP
pH 7.5, 20°C, recombinant enzyme
0.5
ADP
pH 7.5, 10°C, recombinant enzyme
0.5
ADP
pH 7.5, 15°C, recombinant enzyme
0.578
ADP
mutant R241K, pH 7.4
0.61
ADP
pH 7.5, 25°C, recombinant enzyme
0.62
ADP
pH 7.5, 20°C, recombinant enzyme
0.64
ADP
pH 7.5, 15°C, recombinant enzyme
0.66
ADP
pH 7.5, 10°C, recombinant enzyme
0.74
ADP
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
1.1
ADP
-
pH 7.3, 37°C, 1.0 M succinate
1.26
ADP
mutant R241L, pH 7.4
1.3
ADP
-
pH 7.3, 37°C, 0.2 M succinate
1.53
ADP
-
pH 7.4, 25°C, 0.5 M NaCl
1.8
ADP
wild type enzyme, at pH 7.0 and 37°C
5.7
ADP
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
0.016
ATP
mutant R91A, pH 7.0
0.0499
ATP
-
mutant V93A, pH 7.0
0.0506
ATP
-
mutant F179A, pH 7.0
0.0542
ATP
-
mutant P232A, pH 7.0
0.0576
ATP
-
mutant L122A, pH 7.0
0.068
ATP
mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl
0.068
ATP
wild-type, pH 7.0, presence of 200 mM guanidine/HCl
0.0687
ATP
-
mutant V93G, pH 7.0
0.07
ATP
co-substrate: acetate, pH 7.5, 37°C
0.07
ATP
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
0.07
ATP
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
0.0713
ATP
-
wild-type, pH 7.0
0.075
ATP
co-substrate: propionate, pH 7.5, 37°C
0.076
ATP
mutant R91K, pH 7.0
0.08
ATP
wild-type, pH 7.0
0.08
ATP
R241A/Q43W, double mutant
0.145
ATP
mutant R91L, pH 7.0
0.234
ATP
R91K/Q43W, double mutant
0.264
ATP
mutant R241A, pH 7.0, presence of 200 mM guanidine/HCl
0.297
ATP
mutant R241A, pH 7.0
0.48
ATP
pH 7.5, 15°C, recombinant enzyme
0.48
ATP
pH 7.5, 20°C, recombinant enzyme
0.49
ATP
pH 7.5, 25°C, recombinant enzyme
0.5
ATP
pH 7.5, 10°C, recombinant enzyme
0.5
ATP
-
acetate kinase EutP, at 40°C, pH not specified in the publication
0.5
ATP
-
acetate kinase EutQ, at 40°C, pH not specified in the publication
0.539
ATP
R91A/Q43W, double mutant
0.57
ATP
pH 7.5, 20°C, recombinant enzyme
0.59
ATP
pH 7.5, 25°C, recombinant enzyme
0.64
ATP
pH 7.5, 15°C, recombinant enzyme
0.65
ATP
pH 7.5, 10°C, recombinant enzyme
0.66
ATP
pH 6.5, 30°C, recombinant mutant N213T/G332D/E336L/T385N
0.67
ATP
pH 6.5, 30°C, recombinant wild-type enzyme
0.7
ATP
-
pH 7.0, 20°C, mutant E334A, produced in E. coli
0.7
ATP
-
pH 7.0, 37°C, mutant H180A, produced in E. coli
0.9
ATP
-
pH 7.6, 37°C, mutant R340L
1
ATP
-
pH 7.6, 37°C, wild-type and mutant R175K
1
ATP
-
pH 7.0, 20°C, unaltered enzyme, produced in E. coli
1.1
ATP
-
carried out at various temperatures
1.1
ATP
-
pH 7.0, 20°C, mutant E32A, produced in E. coli
1.3
ATP
-
pH 7.6, 37°C, mutant R340K
1.3
ATP
R241K/Q43W, double mutant
1.4
ATP
-
pH 7.0, 20°C, mutants E97A, E97D, E97Q, produced in E. coli
1.4
ATP
-
pH 7.0, 37°C, mutant H180R, produced in E. coli
1.5
ATP
-
pH 7.0, 37°C, mutant H123A, produced in E. coli
1.6
ATP
-
pH 7.0, 20°C, mutant E385C, produced in E. coli
1.7
ATP
-
pH 7.0, 37°C, mutant H90A, produced in E. coli
1.7
ATP
37°C, pH 7.0-7.5, mutant enzyme G239A
1.7
ATP
pH 6.5, 30°C, recombinant mutant N213T
1.7
ATP
wild type enzyme, at pH 5.5 and 45°C
1.8
ATP
37°C, pH 7.0-7.5, mutant enzyme G239S
1.9
ATP
-
pH 7.0, 37°C, mutant H208A, produced in E. coli
2
ATP
-
pH 7.0, 20°C, mutant E385Q, produced in E. coli
2
ATP
-
pH 7.0, 37°C, unaltered wild-type enzyme, produced in E. coli
2.13
ATP
-
pH 7.4, 37°C, wild-type
2.7
ATP
-
pH 7.0, 37°C, mutant H184A, produced in E. coli
2.8
ATP
-
pH 7.0, 37°C, authentic wild-type enzyme
2.8
ATP
-
pH 7.6, 37°C, recombinant wild-type
2.8
ATP
37°C, pH is not specified in the publication
3
ATP
-
pH 7.0, 37°C, mutant H60A, produced in E. coli
3
ATP
-
pH 7.6, 37°C, mutant R285K, R285L
3
ATP
-
pH 7.4, 37°C, mutant N211A
3.1
ATP
-
pH 7.4, 37°C, mutant D148A
3.1
ATP
-
with acetate as cosubstrate, at pH 5.7 and 37°C
3.2
ATP
-
pH 7.4, 37°C, mutant S10A
3.4
ATP
-
pH 7.6, 37°C, mutant R241K
3.5
ATP
pH 6.5, 30°C, recombinant mutant G332D
3.62
ATP
-
pH 7.4, 37°C, mutant K14R
3.7
ATP
-
pH 7.0, 37°C, mutant H180Q, produced in E. coli
3.7
ATP
-
pH 7.4, 37°C, mutant S12T
3.7
ATP
-
pH 7.5, 30°C, isoenzyme II
3.8
ATP
-
pH 7.5, 30°C, isoenzyme I
3.9
ATP
-
pH 7.6, 37°C, mutant R91K
4
ATP
37°C, pH 7.0-7.5, wild-type enzyme
4.3
ATP
-
pH 7.0, 20°C, mutant E385D, produced in E. coli
4.3
ATP
-
pH 7.4, 37°C, mutant S10T
4.5
ATP
-
pH 7.4, 37°C, mutant S11A
4.6
ATP
-
pH 7.0, 37°C, mutant H180N, produced in E. coli
4.7
ATP
-
pH 7.0, 37°C, mutant H180D, produced in E. coli
5
ATP
-
pH 7.4, 37°C, mutant N7D, D148E
5.2
ATP
-
pH 7.4, 37°C, mutant K14A
5.2
ATP
pH 6.5, 30°C, recombinant mutant G333Q
5.8
ATP
-
pH 7.4, 37°C, mutant S10T
5.8
ATP
-
pH 7.0, 37°C, mutant H94A, produced in E. coli
5.9
ATP
37°C, pH 7.0-7.5, mutant enzyme N211A
6
ATP
-
pH 7.6, 37°C, mutant R285A, R91A
6.2
ATP
-
pH 7.0, 37°C, mutant H180E, produced in E. coli
6.3
ATP
-
pH 7.0, 37°C, mutant H180K, produced in E. coli
6.6
ATP
pH 6.5, 30°C, recombinant mutant I334M
6.8
ATP
-
pH 7.4, 37°C, mutant S11T
6.8
ATP
37°C, pH 7.0-7.5, mutant enzyme N211S
6.9
ATP
-
pH 7.0, 20°C, mutant E385A, produced in E. coli
7
ATP
-
pH 7.4, 37°C, mutant N7A
7.1
ATP
37°C, pH 7.0-7.5, mutant enzyme N211T
7.3
ATP
-
pH 7.4, 37°C, mutant S12A
7.7
ATP
-
pH 7.4, 37°C, mutant E384A
9
ATP
-
pH 7.3, 37°C, 50 M succinate
9.4
ATP
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
10
ATP
-
pH 7.3, 37°C, 5.0 M succinate
10.2
ATP
37°C, pH 7.0-7.5, mutant enzyme G331A
11.4
ATP
mutant R241K, pH 7.0
13.5
ATP
co-substrate: formate, pH 7.5, 37°C
17
ATP
mutant R241L, pH 7.0
18.4
ATP
37°C, pH 7.0-7.5, mutant enzyme G331Q
30.7
ATP
pH 6.5, 30°C, recombinant mutant N337E
56
ATP
-
pH 7.0, 37°C, mutant H180A, produced in E. coli
24.5
Butyrate
-
at pH 5.7 and 37°C
33.4
Butyrate
-
mutant V93A, pH 7.0
39
Butyrate
-
wild-type, pH 7.0
63
Butyrate
-
mutant V93G, pH 7.0
200
Butyrate
-
carried out at various temperatures
0.088
CTP
co-substrate: acetate, pH 7.5, 37°C
1.9
CTP
-
carried out at various temperatures
3.2
CTP
37°C, pH 7.0-7.5, wild-type enzyme
11.1
CTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
15.7
CTP
37°C, pH 7.0-7.5, mutant enzyme G331A
0.078
GTP
co-substrate: acetate, pH 7.5, 37°C
5.3
GTP
37°C, pH 7.0-7.5, mutant enzyme G331A
5.7
GTP
-
carried out at various temperatures
7.2
GTP
37°C, pH 7.0-7.5, wild-type enzyme
7.4
GTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
0.78
ITP
-
pH 7.9, 37°C
3.7
ITP
-
carried out at various temperatures
4.7
ITP
37°C, pH 7.0-7.5, wild-type enzyme
10.1
ITP
37°C, pH 7.0-7.5, mutant enzyme G331Q
10.7
ITP
37°C, pH 7.0-7.5, mutant enzyme G331A
6.2
propionate
-
mutant V93A, pH 7.0
10.7
propionate
-
mutant L122A, pH 7.0
11
propionate
-
mutant F179A, pH 7.0
11.2
propionate
pH 7.5, 37°C
14.4
propionate
-
wild-type, pH 7.0
24
propionate
-
wild-type, pH 7.5, 37°C
25
propionate
-
mutant V93G, pH 7.0
25.8
propionate
-
at pH 5.7 and 37°C
40
propionate
-
pH 7.5, 30°C, isoenzyme I
46
propionate
-
mutant P232A, pH 7.0
63.3
propionate
-
pH 7.5, 30°C
133
propionate
-
pH 7.5, 30°C, isoenzyme II
150
propionate
-
carried out at various temperatures
300
propionate
-
pH 7.3, 37°C, 50 M succinate
1000
propionate
-
pH 7.3, 37°C, 5.0 M succinate
2.7
TTP
37°C, pH 7.0-7.5, wild-type enzyme
11.2
TTP
37°C, pH 7.0-7.5, mutant enzyme G331A
12.1
TTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
0.096
UTP
co-substrate: acetate, pH 7.5, 37°C
1.3
UTP
-
carried out at various temperatures
2.7
UTP
37°C, pH 7.0-7.5, wild-type enzyme
14.2
UTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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
-
lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetic analysis and mechanism, detailed overview
-
additional information
additional information
-
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
-
additional information
additional information
Michaelis-Menten kinetics, thermodynamics
-
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 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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
12 - 3869
acetyl phosphate
65.4
Isobutyrate
-
at pH 5.7 and 37°C
80.2
valerate
-
at pH 5.7 and 37°C
17
acetate
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
80
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
177
acetate
-
at pH 5.7 and 37°C
190
acetate
-
mutant E97D, pH 7.5, 37°C
195
acetate
pH 7.5, 10°C, recombinant enzyme
233.3
acetate
pH 8.0, 30°C
245
acetate
pH 7.5, 15°C, recombinant enzyme
280
acetate
-
pH 7.0, 36°C
300
acetate
pH 7.5, 20°C, recombinant enzyme
318
acetate
-
acetate kinase EutQ, at 40°C, pH not specified in the publication
385
acetate
pH 7.5, 25°C, recombinant enzyme
545
acetate
-
acetate kinase EutP, at 40°C, pH not specified in the publication
560
acetate
pH 7.5, 10°C, recombinant enzyme
760
acetate
pH 7.5, 15°C, recombinant enzyme
761
acetate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
789
acetate
wild type enzyme, at pH 5.5 and 45°C
1042
acetate
-
wild-type, pH 7.5, 37°C
1165
acetate
pH 7.5, 20°C, recombinant enzyme
1180
acetate
pH 7.5, 37°C
1420
acetate
pH 7.5, 25°C, recombinant enzyme
12
acetyl phosphate
-
mutant F179A, pH 7.4
12
acetyl phosphate
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
93
acetyl phosphate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA2
105
acetyl phosphate
at pH 8.0 and 37°C
316.7
acetyl phosphate
pH 8.0, 30°C
700
acetyl phosphate
-
pH 7.0, 36°C
875
acetyl phosphate
-
pH 7.4, 25°C
875
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme
890
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme
1039
acetyl phosphate
-
mutant L122A, pH 7.4
1105
acetyl phosphate
pH 7.5, 30°C, recombinant His-tagged isozyme AckA1
1340
acetyl phosphate
pH 7.5, 15°C, recombinant enzyme
1550
acetyl phosphate
pH 7.5, 15°C, recombinant enzyme
1550
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
1700
acetyl phosphate
pH 7.5, 20°C, recombinant enzyme
1764
acetyl phosphate
pH 7.5, 37°C
2100
acetyl phosphate
pH 7.5, 25°C, recombinant enzyme
2150
acetyl phosphate
pH 7.5, 20°C, recombinant enzyme
2396
acetyl phosphate
-
mutant P232A, pH 7.4
2572
acetyl phosphate
-
mutant V93G, pH 7.4
2680
acetyl phosphate
-
wild-type, pH 7.4
3167
acetyl phosphate
pH 8.0, 30°C
3600
acetyl phosphate
pH 7.5, 25°C, recombinant enzyme
3869
acetyl phosphate
-
mutant V93A, pH 7.4
0.42
ADP
mutant R241L, pH 7.4
2.63
ADP
R91A/Q43W, double mutant
3.5
ADP
mutant R91A, pH 7.4
4.5
ADP
mutant R241A, pH 7.4
4.5
ADP
mutant R241K, pH 7.4
7.7
ADP
mutant R91L, pH 7.4
10.5
ADP
R241K/Q43W, double mutant
12
ADP
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
14.6
ADP
R241A/Q43W, double mutant
23
ADP
mutant R91K, pH 7.4
25.7
ADP
R91K/Q43W, double mutant
177
ADP
-
pH 7.4, 25°C, 0.5 M NaCl
318
ADP
-
pH 7.4, 25°C, 0.5 M NaCl
884
ADP
pH 7.5, 10°C, recombinant enzyme
892
ADP
pH 7.5, 10°C, recombinant enzyme
1260
ADP
wild-type, pH 7.4
1350
ADP
pH 7.5, 15°C, recombinant enzyme
1487
ADP
at pH 8.0 and 37°C
1565
ADP
pH 7.5, 15°C, recombinant enzyme
1700
ADP
pH 7.5, 20°C, recombinant enzyme
1750
ADP
co-substrate: acetate, pH 7.5, 37°C
1915
ADP
wild type enzyme, at pH 7.0 and 37°C
2135
ADP
pH 7.5, 25°C, recombinant enzyme
2178
ADP
pH 7.5, 20°C, recombinant enzyme
3515
ADP
pH 7.5, 25°C, recombinant enzyme
0.11
ATP
mutant R91A, pH 7.0
0.22
ATP
mutant R91L, pH 7.0
0.34
ATP
pH 6.5, 30°C, recombinant mutant N213T/G332D/E336L/T385N
0.4
ATP
R241K/Q43W, double mutant
0.68
ATP
mutant R241A, pH 7.0
1.3
ATP
mutant R241K, pH 7.0
1.38
ATP
mutant R241L, pH 7.0
1.83
ATP
R241A/Q43W, double mutant
2.07
ATP
R91A/Q43W, double mutant
2.2
ATP
-
mutant F179A, pH 7.0
3.7
ATP
mutant R91K, pH 7.0
6.8
ATP
37°C, pH 7.0-7.5, mutant enzyme G239S
9.9
ATP
pH 6.5, 30°C, recombinant mutant G332D
10.5
ATP
pH 6.5, 30°C, recombinant mutant I334M
11.8
ATP
R91K/Q43W, double mutant
13
ATP
37°C, pH 7.0-7.5, mutant enzyme N211S
14
ATP
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
16
ATP
37°C, pH 7.0-7.5, mutant enzyme G331Q
16.3
ATP
pH 6.5, 30°C, recombinant mutant N213T
32
ATP
37°C, pH 7.0-7.5, mutant enzyme N211T
41
ATP
pH 6.5, 30°C, recombinant mutant G333Q
77
ATP
37°C, pH 7.0-7.5, mutant enzyme G239A
88
ATP
37°C, pH 7.0-7.5, mutant enzyme G331A
132
ATP
-
mutant P232A, pH 7.0
150
ATP
-
mutant L122A, pH 7.0
205
ATP
pH 7.5, 10°C, recombinant enzyme
235
ATP
pH 7.5, 15°C, recombinant enzyme
250
ATP
-
with acetate as cosubstrate, at pH 5.7 and 37°C
305
ATP
pH 7.5, 20°C, recombinant enzyme
347
ATP
-
mutant V93G, pH 7.0
350
ATP
pH 7.5, 25°C, recombinant enzyme
374
ATP
37°C, pH 7.0-7.5, mutant enzyme N211A
395
ATP
pH 6.5, 30°C, recombinant mutant N337E
434
ATP
-
acetate kinase EutQ, at 40°C, pH not specified in the publication
565
ATP
pH 7.5, 10°C, recombinant enzyme
657
ATP
-
acetate kinase EutP, at 40°C, pH not specified in the publication
711
ATP
wild type enzyme, at pH 5.5 and 45°C
715
ATP
37°C, pH 7.0-7.5, wild-type enzyme
745
ATP
pH 7.5, 15°C, recombinant enzyme
844
ATP
-
mutant V93A, pH 7.0
870
ATP
co-substrate: formate, pH 7.5, 37°C
900
ATP
co-substrate: propionate, pH 7.5, 37°C
908
ATP
pH 6.5, 30°C, recombinant wild-type enzyme
913
ATP
wild-type, pH 7.0
1055
ATP
-
wild-type, pH 7.0
1130
ATP
pH 7.5, 20°C, recombinant enzyme
1170
ATP
co-substrate: acetate, pH 7.5, 37°C
1500
ATP
pH 7.5, 25°C, recombinant enzyme
0.18
Butyrate
-
wild-type, pH 7.0
42.4
Butyrate
-
mutant V93A, pH 7.0
118
Butyrate
-
at pH 5.7 and 37°C
294
Butyrate
-
mutant V93G, pH 7.0
2.1
CTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
17
CTP
37°C, pH 7.0-7.5, mutant enzyme G331A
460
CTP
37°C, pH 7.0-7.5, wild-type enzyme
8.6
GTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
67
GTP
37°C, pH 7.0-7.5, mutant enzyme G331A
571
GTP
37°C, pH 7.0-7.5, wild-type enzyme
11
ITP
37°C, pH 7.0-7.5, mutant enzyme G331Q
84
ITP
37°C, pH 7.0-7.5, mutant enzyme G331A
742
ITP
37°C, pH 7.0-7.5, wild-type enzyme
0.37
propionate
-
mutant F179A, pH 7.0
6.7
propionate
-
mutant L122A, pH 7.0
8.5
propionate
-
mutant P232A, pH 7.0
172
propionate
-
at pH 5.7 and 37°C
218
propionate
-
wild-type, pH 7.0
840
propionate
-
mutant V93G, pH 7.0
940
propionate
pH 7.5, 37°C
1029
propionate
-
mutant V93A, pH 7.0
2.8
TTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
20
TTP
37°C, pH 7.0-7.5, mutant enzyme G331A
540
TTP
37°C, pH 7.0-7.5, wild-type enzyme
2.8
UTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
43
UTP
37°C, pH 7.0-7.5, mutant enzyme G331A
415
UTP
37°C, pH 7.0-7.5, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.2 - 6300
acetyl phosphate
4.8
Butyrate
-
at pH 5.7 and 37°C
0.6
Isobutyrate
-
at pH 5.7 and 37°C
5.6
valerate
-
at pH 5.7 and 37°C
0.057
acetate
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
3.3
acetate
-
at pH 5.7 and 37°C
15.5
acetate
pH 7.5, 10°C, recombinant enzyme
23.5
acetate
pH 7.5, 15°C, recombinant enzyme
37.2
acetate
pH 7.5, 20°C, recombinant enzyme
39
acetate
wild type enzyme, at pH 5.5 and 45°C
48.5
acetate
pH 7.5, 25°C, recombinant enzyme
127
acetate
pH 7.5, 10°C, recombinant enzyme
144
acetate
pH 7.5, 15°C, recombinant enzyme
178
acetate
pH 7.5, 20°C, recombinant enzyme
198
acetate
pH 7.5, 25°C, recombinant enzyme
454
acetate
-
acetate kinase EutQ, at 40°C, pH not specified in the publication
778
acetate
-
acetate kinase EutP, at 40°C, pH not specified in the publication
2500
acetate
pH 8.0, 30°C
7.2
acetyl phosphate
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
1290
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme
1294
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
1650
acetyl phosphate
pH 7.5, 10°C, recombinant enzyme
2183
acetyl phosphate
pH 7.5, 15°C, recombinant enzyme
2528
acetyl phosphate
pH 7.5, 15°C, recombinant enzyme
2879
acetyl phosphate
pH 8.0, 30°C
3207
acetyl phosphate
pH 7.5, 20°C, recombinant enzyme
3209
acetyl phosphate
pH 7.5, 20°C, recombinant enzyme
4200
acetyl phosphate
pH 7.5, 25°C, recombinant enzyme
6102
acetyl phosphate
pH 7.5, 25°C, recombinant enzyme
6300
acetyl phosphate
pH 7.5, 37°C
2
ADP
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
1073
ADP
wild type enzyme, at pH 7.0 and 37°C
1351
ADP
pH 7.5, 10°C, recombinant enzyme
1768
ADP
pH 7.5, 10°C, recombinant enzyme
2445
ADP
pH 7.5, 15°C, recombinant enzyme
2700
ADP
pH 7.5, 15°C, recombinant enzyme
3470
ADP
pH 7.5, 20°C, recombinant enzyme
3513
ADP
pH 7.5, 20°C, recombinant enzyme
4542
ADP
pH 7.5, 25°C, recombinant enzyme
5762
ADP
pH 7.5, 25°C, recombinant enzyme
17650
ADP
co-substrate: acetate, pH 7.5, 37°C
0.9
ATP
37°C, pH 7.0-7.5, mutant enzyme G331Q
1.5
ATP
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
1.9
ATP
37°C, pH 7.0-7.5, mutant enzyme N211S
3.9
ATP
37°C, pH 7.0-7.5, mutant enzyme G239S
4.5
ATP
37°C, pH 7.0-7.5, mutant enzyme N211T
8.9
ATP
37°C, pH 7.0-7.5, mutant enzyme G331A
45.7
ATP
37°C, pH 7.0-7.5, mutant enzyme G239A
63
ATP
37°C, pH 7.0-7.5, mutant enzyme N211A
80.5
ATP
-
with acetate as cosubstrate, at pH 5.7 and 37°C
180
ATP
37°C, pH 7.0-7.5, wild-type enzyme
390
ATP
pH 7.5, 10°C, recombinant enzyme
421
ATP
wild type enzyme, at pH 5.5 and 45°C
510
ATP
pH 7.5, 15°C, recombinant enzyme
625
ATP
pH 7.5, 20°C, recombinant enzyme
785
ATP
pH 7.5, 25°C, recombinant enzyme
868
ATP
-
acetate kinase EutQ, at 40°C, pH not specified in the publication
869
ATP
pH 7.5, 10°C, recombinant enzyme
1164
ATP
pH 7.5, 15°C, recombinant enzyme
1314
ATP
-
acetate kinase EutP, at 40°C, pH not specified in the publication
1982
ATP
pH 7.5, 20°C, recombinant enzyme
2542
ATP
pH 7.5, 25°C, recombinant enzyme
10240
ATP
co-substrate: formate, pH 7.5, 37°C
11350
ATP
co-substrate: propionate, pH 7.5, 37°C
16860
ATP
co-substrate: acetate, pH 7.5, 37°C
0.2
CTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
1.1
CTP
37°C, pH 7.0-7.5, mutant enzyme G331A
148
CTP
37°C, pH 7.0-7.5, wild-type enzyme
1.2
GTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
12.6
GTP
37°C, pH 7.0-7.5, mutant enzyme G331A
80
GTP
37°C, pH 7.0-7.5, wild-type enzyme
1
ITP
37°C, pH 7.0-7.5, mutant enzyme G331Q
7.8
ITP
37°C, pH 7.0-7.5, mutant enzyme G331A
158
ITP
37°C, pH 7.0-7.5, wild-type enzyme
6.7
propionate
-
at pH 5.7 and 37°C
85
propionate
pH 7.5, 37°C
0.2
TTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
1.8
TTP
37°C, pH 7.0-7.5, mutant enzyme G331A
202
TTP
37°C, pH 7.0-7.5, wild-type enzyme
0.2
UTP
37°C, pH 7.0-7.5, mutant enzyme G331Q
152
UTP
37°C, pH 7.0-7.5, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
G332D
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
G333Q
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
I334M
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
N213T
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
N213T/G332D/E336L/T385N
site-directed mutagenesis, the mutant shows unaltered Km for ATP and highly reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
N337E
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
D148A
-
site-directed mutagenesis
D148E
-
site-directed mutagenesis
D148N
-
site-directed mutagenesis
E384A
-
site-directed mutagenesis
E384D
-
site-directed mutagenesis
E384Q
-
site-directed mutagenesis
E97D
-
reduction of both Km and kcat-value
F179A
-
reduced catalytic efficiency with all substrates tested
G239A
14.5fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. The mutant enzyme shows a shift in NTP utilization. It displays substantially higher activity with TTP than with ATP, and activity (as a percentage of that observed with ATP) increased greatly with CTP as well. A weak increase in activity is observed with UTP. Activity with the purines GTP and ITP versus ATP decreases
G239S
192fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. The mutant enzyme shows a shift in NTP utilization. It displays substantially higher activity with TTP than with ATP, and activity (as a percentage of that observed with ATP) increased greatly with CTP as well. A weak increase in activity is observed with UTP. Activity with the purines GTP and ITP versus ATP decreases
G331A
15.2fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. Activity of mutant enzyme with the pyrimidine nucleotides CTP, TTP, and UTP is significantly reduced, with each displaying less than 12% activity versus ATP. Activity with GTP and ITP is also reduced, but to a much lesser extent
G331Q
118fold reduced specific activity. The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. Activity of mutant enzyme with the pyrimidine nucleotides CTP, TTP, and UTP is significantly reduced, with each displaying less than 12% activity versus ATP. Activity with GTP and ITP is also reduced, but to a much lesser extent
G331Q/I332M
the mutations result in substantial reductions in kcat compared to the wild type enzyme. In the acetate-forming direction, catalysis is reduced over 100fold, and in the acetyl phosphate-forming direction, kcat is reduced about 50fold. This alteration results in about 5fold increase in Km for ADP and ATP, and a 15fold increase in Km for acetate but no substantial change in the Km for acetyl phosphate
H123A
-
site-directed mutagenesis
H152A
-
site-directed mutagenesis
H180A
-
site-directed mutagenesis
H180R
-
site-directed mutagenesis
H184A
-
site-directed mutagenesis
H208A
-
site-directed mutagenesis
H60A
-
site-directed mutagenesis
H90A
-
site-directed mutagenesis
H94A
-
site-directed mutagenesis
K14A
-
site-directed mutagenesis
K14R
-
site-directed mutagenesis
L122A
-
reduced catalytic efficiency with all substrates tested
N211S
200fold reduced specific activity (with ATP as substrate). The percentage activity observed with CTP and ITP versus ATP is similar to that observed with the wild type enzyme. Activity with GTP and UTP decreases somewhat, and activity with TTP shows an increase
N211T
44fold reduced specific activity (with ATP as substrate). Mutant enzyme shows little change in percentage activity observed with CTP and ITP. Activity with TTP is greatly enhanced and nearly equal to that observed with ATP, whereas the reduction in activity with UTP is stronger than that observed with the N211A
N7A
-
site-directed mutagenesis
P232A
-
reduced catalytic efficiency with all substrates tested
Q43W
site-directed mutagenesis, single mutant
R175K
-
site-directed mutagenesis
R241A
severe decrease in kinetic parameters
R241A/Q43W
site-directed mutagenesis, double mutant
R241K/Q43W
site-directed mutagenesis, double mutant
R241L
severe decrease in kinetic parameters
R285A
-
site-directed mutagenesis
R285K
-
site-directed mutagenesis
R285L
-
site-directed mutagenesis
R340K
-
site-directed mutagenesis
R340L
-
site-directed mutagenesis
R91A
severe decrease in kinetic parameters
R91A/Q43W
site-directed mutagenesis, double mutant
R91K/Q43W
site-directed mutagenesis, double mutant
R91L
severe decrease in kinetic parameters
S10A
-
site-directed mutagenesis
S11A
-
site-directed mutagenesis
S12A
-
site-directed mutagenesis
V93A
-
improved catalytic efficiency with propionate and butyrate
V93G
-
improved catalytic efficiency with propionate and butyrate
R241A
the mutant shows 3.9% of wild type activity
R91A
the mutant shows about 0.6% of wild type activity
R241A
-
the mutant shows 3.9% of wild type activity
-
R91A
-
the mutant shows about 0.6% of wild type activity
-
N211A
-
site-directed mutagenesis
N211A
6fold reduced specific activity (with ATP as substrate). The percentage activity observed with CTP and ITP versus ATP is similar to that observed with the wild type enzyme. Activity with GTP and UTP decreases somewhat, and activity with TTP shows an increase
R91K
-
site-directed mutagenesis
R91K
severe decrease in kinetic parameters
additional information
-
mutant with no enzymic activity, fails to grow in xylose minimal medium under anaerobic conditions but grows anaerobically with arabinose
additional information
development of a one-pot process of enzymatic synthesis of deoxythymidine-5'-triphosphate (5'-dTTP) employing whole cells of recombinant Escherichia coli coexpressing thymidylate kinase (TMKase, EC 2.7.4.9) and acetate kinase (ACKase). The relative residual specific activities of TMKase and ACKase, pretreated with 20 mM EDTA, are 94% and 96%, respectively. The yield of 5'-dTTP reaches above 94% from 5 mM 5'-dTMP and 15 mM acetyl phosphate catalyzed with intact cells of the recombinant strain pretreated with EDTA. The process is so effective that only 0.125 mM ATP is sufficient to deliver the phosphate group from acetyl phosphate to dTMP and dTDP
additional information
-
development of a one-pot process of enzymatic synthesis of deoxythymidine-5'-triphosphate (5'-dTTP) employing whole cells of recombinant Escherichia coli coexpressing thymidylate kinase (TMKase, EC 2.7.4.9) and acetate kinase (ACKase). The relative residual specific activities of TMKase and ACKase, pretreated with 20 mM EDTA, are 94% and 96%, respectively. The yield of 5'-dTTP reaches above 94% from 5 mM 5'-dTMP and 15 mM acetyl phosphate catalyzed with intact cells of the recombinant strain pretreated with EDTA. The process is so effective that only 0.125 mM ATP is sufficient to deliver the phosphate group from acetyl phosphate to dTMP and dTDP
additional information
each of five candidate residue in Escherichia coli ATP-specific AK (ATP-ecoAK), which is unable to use diphosphate, is substituted with the respective diphosphate-ehiAK amino acid residue. Each variant ATP-ecoAK has an increased Km for ATP, indicating that the five residues are the determinants for the specificity to ATP in ATP-ecoAK
additional information
-
each of five candidate residue in Escherichia coli ATP-specific AK (ATP-ecoAK), which is unable to use diphosphate, is substituted with the respective diphosphate-ehiAK amino acid residue. Each variant ATP-ecoAK has an increased Km for ATP, indicating that the five residues are the determinants for the specificity to ATP in ATP-ecoAK
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bock, A.K.; Glasemacher, J.; Schmidt, R.; Schonheit, P.
Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima
J. Bacteriol.
181
1861-1867
1999
Thermotoga maritima
brenda
Rose, I.A.
Acetate kinase
The Enzymes, 2nd. Ed. (Boyer, P. D. , Lardy, H. , Myrbaeck, K. , eds. )
6
115-118
1962
Escherichia coli, Lactobacillus delbrueckii, Streptococcus pyogenes
-
brenda
Anthony, R.S.; Spector, L.B.
Exchange reactions catalyzed by acetate kinase
J. Biol. Chem.
246
6129-6135
1971
Escherichia coli
brenda
Janson, C.A.; Cleland, W.W.
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
J. Biol. Chem.
249
2567-2571
1974
Escherichia coli
brenda
Janson, C.A.; Cleland, W.W.
The specificity of chromium nucleotides as inhibitors of selected kinases
J. Biol. Chem.
249
2572-2574
1974
Escherichia coli
brenda
Schaupp, A.; Ljungdahl, L.G.
Purification and properties of acetate kinase from Clostridium thermoaceticum
Arch. Microbiol.
100
121-129
1974
Moorella thermoacetica
brenda
Bowman, C.M.; Valdez, R.O.; Nishimura, J.S.
Acetate kinase from Veillonella alcalescens. Regulation of enzyme activity by succinate and substrates
J. Biol. Chem.
251
3117-3121
1976
Veillonella parvula
brenda
Nakajima, H.; Suzuki, K.; Imahori, K.
Purification and properties of acetate kinase from Bacillus stearothermophilus
J. Biochem.
84
193-203
1978
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
brenda
Yoshimura, F.
Purification and characterization of acetate kinase from Veillonella alcalescens ATCC 17748
Arch. Biochem. Biophys.
189
424-432
1978
Veillonella parvula
brenda
Griffith, M.J.; Nishimura, J.S.
Acetate kinase from Veillonella alcalescens. Purification and physical properties
J. Biol. Chem.
254
442-446
1979
Veillonella parvula
brenda
Griffith, M.J.; Nishimura, J.S.
Acetate kinase from Veillonella alcalescens. Regulation by succinate and substrates
J. Biol. Chem.
254
6698-6702
1979
Veillonella parvula
brenda
Kahane, I.; Muhlrad, A.
Purification and properties of acetate kinase from Acholeplasma laidlawii
J. Bacteriol.
137
764-772
1979
Acholeplasma laidlawii, Acholeplasma laidlawii oral
brenda
Wong, S.S.; Wong, L.J.C.
Inactivation of Escherichia coli acetate kinase by N-ethylmaleimide. Protection by substrates and products
Biochim. Biophys. Acta
615
121-131
1980
Escherichia coli
brenda
Nishimura, J.S.; Griffith, M.J.
Acetate kinase from Veilonella alcalescens
Methods Enzymol.
71
311-316
1981
Veillonella parvula, Veillonella parvula 221 / ATCC 17745
-
brenda
Harwood, C.S.; Canale-Parola, E.
Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a spirochete
J. Bacteriol.
152
246-254
1982
Spirochaeta sp., Spirochaeta sp. MA-2
brenda
Suzuki, K.; Nakajima, H.; Imahori, K.
Acetate kinase from Bacillus stearothermophilus
Methods Enzymol.
90
179-185
1982
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
-
brenda
Ichikawa, Y.; Mori, N.; Miki, S.; Hosoi, N.; Kitamoto, Y.
Purification and properties of acetate kinase from propionibacterium freudenreichii
J. Ferment. Technol.
63
143-149
1985
Propionibacterium freudenreichii
-
brenda
Fox, D.K.; Roseman, S.
Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli
J. Biol. Chem.
261
13487-13497
1986
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Vigenschow, H.; Schwarm, H.M.; Knobloch, K.
Purification and properties of an acetate kinase from Rhodopseudomonas palustris
Biol. Chem. Hoppe-Seyler
367
951-956
1986
Rhodopseudomonas palustris
brenda
Aceti, D.J.; Ferry, J.G.
Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila
J. Biol. Chem.
249
15444-15448
1988
Methanosarcina thermophila
-
brenda
Kim, Y.S.; Park, C.
Inactivation of Acinetobacter calcoaceticus acetate kinase by diethylpyrocarbonate
Biochim. Biophys. Acta
956
103-109
1988
Acinetobacter calcoaceticus
brenda
Mannens, G.; Slegers, G.; Claeys, A.
Purification and immobilization of acetate kinase from Desulfovibrio vulgaris
Biotechnol. Lett.
10
563-568
1988
Desulfovibrio vulgaris
-
brenda
Diez-Gonzalez, F.; Russell, J.B.; Hunter, J.B.
The acetate kinase of Clostridium acetobutylicum strain P262
Arch. Microbiol.
166
418-420
1996
Clostridium acetobutylicum, Clostridium acetobutylicum P262
brenda
Buss, K.A.; Ingram-Smith, C.; Ferry, J.G.; Sanders, D.A.; Hasson, M.S.
Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold
Protein Sci.
6
2659-2662
1997
Methanosarcina thermophila
brenda
Winzer, K.; Lorenz, K.; Duerre, P.
Acetate kinase from Clostridium acetobutylicum: a highly specific enzyme that is actively transcribed during acidogenesis and solventogenesis
Microbiology
143
3279-3286
1997
Clostridium acetobutylicum
-
brenda
Lin, W.R.; Peng, Y.; Lew, S.; Lee, C.C.; Hsu, J.J.; Hamel, J.F.; Demain, A.L.
Purification and characterization of acetate kinase from Clostridium thermocellum
Tetrahedron
54
15915-15925
1998
Acetivibrio thermocellus
-
brenda
Singh-Wissmann, K.; Ingram-Smith, C.; Miles, R.D.; Ferry, J.G.
Identification of essential glutamates in the acetate kinase from Methanosarcina thermophila
J. Bacteriol.
180
1129-1134
1998
Methanosarcina thermophila
brenda
Ingram-Smith, C.; Barber, R.D.; Ferry, J.G.
The role of histidines in the acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
275
33765-33770
2000
Methanosarcina thermophila
brenda
Singh-Wissmann, K.; Miles, R.D.; Ingram-Smith, C.; Ferry, J.G.
Identification of essential arginines in the acetate kinase from Methanosarcina thermophila
Biochemistry
39
3671-3677
2000
Methanosarcina thermophila
brenda
Knorr, R.; Ehrmann, M.A.; Vogel, R.F.
Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis
Microbiol. Res.
156
267-277
2001
Fructilactobacillus sanfranciscensis (Q9F1X7), Fructilactobacillus sanfranciscensis
brenda
Miles, R.D.; Iyer, P.P.; Ferry, J.G.
Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
276
45059-45064
2001
Methanosarcina thermophila
brenda
Yu, L.; Ishida, T.; Ozawa, K.; Akutsu, H.; Horiike, K.
Purification and characterization of homo- and hetero-dimeric acetate kinases from the sulfate-reducing bacterium Desulfovibrio vulgaris
J. Biochem.
129
411-421
2001
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki F.
brenda
Ito, K.; Nakagawa, K.; Murakami, S.; Arakawa, H.; Maeda, M.
Highly sensitive simultaneous bioluminescent measurement of acetate kinase and pyruvate phosphate dikinase activities using a firefly luciferase-luciferin reaction and its application to a tandem bioluminescent enzyme immunoassay
Anal. Sci.
19
105-109
2003
Geobacillus stearothermophilus
brenda
Hasona, A.; Kim, Y.; Healy, F.G.; Ingram, L.O.; Shanmugam, K.T.
Pyruvate formate lyase and acetate kinase are essential for anaerobic growth of Escherichia coli on xylose
J. Bacteriol.
186
7593-7600
2004
Escherichia coli
brenda
Ingram-Smith, C.; Gorrell, A.; Lawrence, S.H.; Iyer, P.; Smith, K.; Ferry, J.G.
Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase
J. Bacteriol.
187
2386-2394
2005
Methanosarcina thermophila
brenda
Gorrell, A.; Lawrence, S.H.; Ferry, J.G.
Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
280
10731-10742
2005
Methanosarcina thermophila (P38502), Methanosarcina thermophila
brenda
Iyer, P.; Ferry, J.G.
Acetate kinase from Methanosarcina thermophila, a key enzyme for methanogenesis
Methods Biotechnol.
17
239-246
2005
Methanosarcina thermophila
-
brenda
Suwannakham, S.; Huang, Y.; Yang, S.T.
Construction and characterization of ack knock-out mutants of Propionibacterium acidipropionici for enhanced propionic acid fermentation
Biotechnol. Bioeng.
94
383-395
2006
Acidipropionibacterium acidipropionici (Q5BM21), Acidipropionibacterium acidipropionici
brenda
Ren, N.Q.; Lin, H.L.; Zhang, K.; Zheng, G.X.; Duan, Z.J.; Lin, M.
Cloning, expression, and characterization of an acetate kinase from a high rate of biohydrogen bacterial strain Ethanoligenens sp. hit B49
Curr. Microbiol.
55
167-172
2007
Ethanoligenens harbinense (Q2N1I6)
brenda
Baldock, M.I.; Denger, K.; Smits, T.H.; Cook, A.M.
Roseovarius sp. strain 217: aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase
FEMS Microbiol. Lett.
271
202-206
2007
Roseovarius sp., Roseovarius sp. 217
brenda
Ingram-Smith, C.; Martin, S.R.; Smith, K.S.
Acetate kinase: not just a bacterial enzyme
Trends Microbiol.
14
249-253
2006
Aspergillus fumigatus, Aspergillus nidulans, Bacillus subtilis, Borreliella burgdorferi, Chaetomium globosum, Chlamydomonas reinhardtii, Coccidioides immitis, Coprinopsis cinerea, Cryptococcus neoformans, Cupriavidus necator, Entamoeba histolytica, Enterococcus faecalis, Fusarium graminearum, Helicobacter pylori, Histoplasma capsulatum, Lactobacillus acidophilus, Lactococcus lactis, Listeria monocytogenes, Mesoplasma florum, Methanosarcina acetivorans, Methanosarcina mazei, Methanosarcina thermophila, Mycoplasma pneumoniae, Neurospora crassa, Oceanobacillus iheyensis, Parastagonospora nodorum, Phanerodontia chrysosporium, Phytophthora ramorum, Phytophthora sojae, Pyricularia grisea, Salmonella enterica, Sclerotinia sclerotiorum, Staphylococcus aureus, Streptococcus pneumoniae, Trichoderma reesei, Uncinocarpus reesii, Ustilago maydis
brenda
Gorrell, A.; Ferry, J.G.
Investigation of the Methanosarcina thermophila acetate kinase mechanism by fluorescence quenching
Biochemistry
46
14170-14176
2007
Methanosarcina thermophila (P38502), Methanosarcina thermophila
brenda
Mukhopadhyay, S.; Hasson, M.S.; Sanders, D.A.
A continuous assay of acetate kinase activity: measurement of inorganic phosphate release generated by hydroxylaminolysis of acetyl phosphate
Bioorg. Chem.
36
65-69
2008
Thermotoga maritima (Q9WYB1), Thermotoga maritima
brenda
Halbedel, S.; Eilers, H.; Jonas, B.; Busse, J.; Hecker, M.; Engelmann, S.; Stuelke, J.
Transcription in Mycoplasma pneumoniae: analysis of the promoters of the ackA and ldh genes
J. Mol. Biol.
371
596-607
2007
Mycoplasma pneumoniae (P75245), Mycoplasma pneumoniae
brenda
Chittori, S.; Savithri, H.S.; Murthy, M.R.
Preliminary X-ray crystallographic studies on acetate kinase (AckA) from Salmonella typhimurium in two crystal forms
Acta Crystallogr. Sect. F
67
1658-1661
2011
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Chittori, S.; Savithri, H.S.; Murthy, M.R.
Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface
BMC Struct. Biol.
12
24
2012
Salmonella enterica subsp. enterica serovar Typhimurium (P63411), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ramos-Montanez, S.; Kazmierczak, K.M.; Hentchel, K.L.; Winkler, M.E.
Instability of ackA (acetate kinase) mutations and their effects on acetyl phosphate and ATP amounts in Streptococcus pneumoniae D39
J. Bacteriol.
192
6390-6400
2010
Streptococcus pneumoniae
brenda
Thaker, T.M.; Tanabe, M.; Fowler, M.L.; Preininger, A.M.; Ingram-Smith, C.; Smith, K.S.; Iverson, T.M.
Crystal structures of acetate kinases from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans
J. Struct. Biol.
181
185-189
2013
Entamoeba histolytica (C4M1C3), Entamoeba histolytica, Cryptococcus neoformans (J9W3A6), Cryptococcus neoformans
brenda
Tonouchi, A.; Nishizaki, Y.; Tohyama, H.; Takeda, K.
Cloning of a gene encoding acetate kinase from Methanosarcina mazei 2-P isolated from a Japanese paddy field soil
Curr. Microbiol.
45
390-393
2002
Methanosarcina mazei (P0CW04), Methanosarcina mazei 2-P (P0CW04), Methanosarcina mazei 2-P
brenda
Welte, C.; Krninger, L.; Deppenmeier, U.
Experimental evidence of an acetate transporter protein and characterization of acetate activation in aceticlastic methanogenesis of Methanosarcina mazei
FEMS Microbiol. Lett.
359
147-153
2014
Methanosarcina mazei (P0CW05), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (P0CW05)
brenda
Buss, K.A.; Cooper, D.R.; Ingram-Smith, C.; Ferry, J.G.; Sanders, D.A.; Hasson, M.S.
Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases
J. Bacteriol.
183
680-686
2001
Methanosarcina thermophila (P38502), Methanosarcina thermophila
brenda
Aceti, D.J.; Ferry, J.G.
Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis
J. Biol. Chem.
263
15444-15448
1988
Methanosarcina thermophila (P38502), Methanosarcina thermophila, Methanosarcina thermophila TM-1 (P38502)
brenda
Miles, R.D.; Gorrell, A.; Ferry, J.G.
Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
277
22547-22552
2002
Methanosarcina thermophila (P38502), Methanosarcina thermophila
brenda
Ingram-Smith, C.; Wharton, J.; Reinholz, C.; Doucet, T.; Hesler, R.; Smith, K.
The role of active site residues in ATP binding and catalysis in the Methanosarcina thermophila acetate kinase
Life
5
861-871
2015
Methanosarcina thermophila (P38502), Methanosarcina thermophila
brenda
Rozova, O.N.; Khmelenina, V.N.; Gavletdinova, J.Z.; Mustakhimov, I.I.; Trotsenko, Y.A.
Acetate kinase-an enzyme of the postulated phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z
Antonie van Leeuwenhoek
108
965-974
2015
Methylotuvimicrobium alcaliphilum (G4T0C7), Methylotuvimicrobium alcaliphilum, Methylotuvimicrobium alcaliphilum 20Z (G4T0C7), Methylotuvimicrobium alcaliphilum 20Z
brenda
Puri, P.; Goel, A.; Bochynska, A.; Poolman, B.
Regulation of acetate kinase isozymes and its importance for mixed-acid fermentation in Lactococcus lactis
J. Bacteriol.
196
1386-1393
2014
Lactococcus lactis (A2RNG4), Lactococcus lactis (A2RNG5), Lactococcus lactis, Lactococcus lactis MG1363 (A2RNG4), Lactococcus lactis MG1363 (A2RNG5)
brenda
Yoshioka, A.; Murata, K.; Kawai, S.
Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase
J. Biosci. Bioeng.
118
502-507
2014
Escherichia coli (P0A6A3), Escherichia coli
brenda
Asgari, S.; Shariati, P.; Ebrahim-Habibi, A.
Targeting acetate kinase: inhibitors as potential bacteriostatics
J. Microbiol. Biotechnol.
23
1544-1553
2013
Escherichia coli (P0A6A3), Escherichia coli
brenda
Zhang, J.; Qian, Y.; Ding, Q.; Ou, L.
Enzymatic manufacture of deoxythymidine-5-triphosphate with permeable intact cells of E. coli coexpressing thymidylate kinase and acetate kinase
J. Microbiol. Biotechnol.
25
2034-2042
2015
Escherichia coli (P0A6A3), Escherichia coli
brenda
Kushkevych, I.V.
Acetate kinase activity and kinetic properties of the enzyme in Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 intestinal bacterial strains
Open Microbiol. J.
8
138-143
2014
Desulfovibrio piger, Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger Vib-7
brenda
Tang, M.A.; Motoshima, H.; Watanabe, K.
Cold adaptation: structural and functional characterizations of psychrophilic and mesophilic acetate kinase
Protein J.
33
313-322
2014
Shewanella sp. (E3W769), Escherichia coli (P0A6A3), Escherichia coli, Shewanella sp. AS-11 (E3W769)
brenda
Jiang, Y.; Tao, R.; Shen, Z.; Sun, L.; Zhu, F.; Yang, S.
Enzymatic production of glutathione by bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase coupled with in vitro acetate kinase-based ATP generation
Appl. Biochem. Biotechnol.
180
1446-1455
2016
Fructilactobacillus sanfranciscensis
brenda
Rozova, O.N.; Khmelenina, V.N.; Gavletdinova, J.Z.; Mustakhimov, I.I.; Trotsenko, Y.A.
Acetate kinase-an enzyme of the postulated phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z
Antonie van Leeuwenhoek
108
965-974
2015
Methylotuvimicrobium alcaliphilum (G4T0C7), Methylotuvimicrobium alcaliphilum, Methylotuvimicrobium alcaliphilum 20Z (G4T0C7), Methylotuvimicrobium alcaliphilum 20Z
brenda
Yoshida, Y.; Sato, M.; Nonaka, T.; Hasegawa, Y.; Kezuka, Y.
Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis
J. Oral Microbiol.
11
1588086
2019
Porphyromonas gingivalis (B2RK02), Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277 (B2RK02)
brenda
Bachochin, M.J.; Van Allen, M.; Barber, R.D.
Characterization of a Rhodobacter sphaeroides primary fatty acid kinase
Arch. Microbiol.
203
861-864
2021
Cereibacter sphaeroides
brenda
Ge, J.; Wang, J.; Ye, G.; Sun, S.; Guo, R.; Song, G.; Ping, W.
Disruption of the lactate dehydrogenase and acetate kinase genes in Klebsiella pneumoniae HD79 to enhance 2,3-butanediol production, and related transcriptomics analysis
Biotechnol. Lett.
42
537-549
2020
Klebsiella pneumoniae, Klebsiella pneumoniae HD79
brenda
Tiwari, S.; Barh, D.; Imchen, M.; Rao, E.; Kumavath, R.K.; Seenivasan, S.P.; Jaiswal, A.K.; Jamal, S.B.; Kumar, V.; Ghosh, P.; Azevedo, V.
Acetate kinase (AcK) is essential for microbial growth and betel-derived compounds potentially target AcK, PhoP and MDR proteins in M. tuberculosis, V. cholerae and pathogenic E. coli an in silico and in vitro study
Curr. Top. Med. Chem.
18
2731-2740
2018
Escherichia coli (P0A6A5), Escherichia coli, Mycobacterium tuberculosis (P9WQH1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQH1)
brenda
Yao, Y.; Ding, Q.; Ou, L.
Biosynthesis of (deoxy)guanosine-5'-triphosphate by GMP kinase and acetate kinase fixed on the surface of E. coli
Enzyme Microb. Technol.
122
82-89
2019
Escherichia coli (P0A6A3), Escherichia coli
brenda
Zhong, Z.; Hu, R.; Zhao, J.; Liu, W.; Kwok, L.Y.; Sun, Z.; Zhang, H.; Chen, Y.
Acetate kinase and peptidases are associated with the proteolytic activity of Lactobacillus helveticus isolated from fermented food
Food Microbiol.
94
103651
2021
Lactobacillus helveticus
brenda
Kaiser, S.; Hoppstaedter, L.M.; Bilici, K.; Heieck, K.; Brueckner, R.
Control of acetyl phosphate-dependent phosphorylation of the response regulator CiaR by acetate kinase in Streptococcus pneumoniae
Microbiology
166
411-421
2020
Streptococcus pneumoniae
brenda
Moore, T.; Escalante-Semerena, J.
The EutQ and EutP proteins are novel acetate kinases involved in ethanolamine catabolism Physiological implications for the function of the ethanolamine metabolosome in Salmonella enterica
Mol. Microbiol.
99
497-511
2016
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Dang, T.; Ingram-Smith, C.
Investigation of pyrophosphate versus ATP substrate selection in the Entamoeba histolytica acetate kinase
Sci. Rep.
7
5912
2017
Methanosarcina thermophila (P38502), Methanosarcina thermophila
brenda