2.7.2.1: acetate kinase
This is an abbreviated version!
For detailed information about acetate kinase, go to the full flat file.
Word Map on EC 2.7.2.1
-
2.7.2.1
-
phosphotransacetylase
-
acetyl-coa
-
cdc42
-
methanosarcina
-
thermophila
-
sludge
-
acetogenic
-
cdc42-associated
-
acetylphosphate
-
formate-lyase
-
non-receptor
-
acetobutylicum
-
substrate-level
-
acetoin
-
tyrobutyricum
-
adp-forming
-
phosphoketolase
-
butyryl-coa
-
embden-meyerhof-parnas
-
acetate-activating
-
synthesis
-
industry
- 2.7.2.1
- phosphotransacetylase
- acetyl-coa
- cdc42
- methanosarcina
- thermophila
- sludge
-
acetogenic
-
cdc42-associated
- acetylphosphate
- formate-lyase
-
non-receptor
- acetobutylicum
-
substrate-level
- acetoin
- tyrobutyricum
-
adp-forming
- phosphoketolase
- butyryl-coa
-
embden-meyerhof-parnas
-
acetate-activating
- synthesis
- industry
Reaction
Synonyms
acetate kinase (phosphorylating), acetic kinase, acetokinase, ACK, ackA, AckA1, AckA2, ACKase, AK, ATP-ecoAK, ATP-specific AK, EAK, EutP, EutQ, MM_0495, Sak, short chain fatty acid kinase, StAckA, urkinase
ECTree
Advanced search results
Inhibitors
Inhibitors on EC 2.7.2.1 - acetate kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
diphosphate
about 70% inhibition in the acetate-forming direction and about 90% inhibition in the acetyl phosphate-forming direction
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
-
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
-
additional information
-
preincubation with butyrate does not significantly inhibit the enzyme
-
additional information
not inhibited by eugenyl acetate and pinoresinol
-
additional information
-
not inhibited by eugenyl acetate and pinoresinol
-