Information on EC 2.3.1.8 - phosphate acetyltransferase

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

EC NUMBER
COMMENTARY
2.3.1.8
-
RECOMMENDED NAME
GeneOntology No.
phosphate acetyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
rapid equilibrium random bi-bi reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
evidence against an acyl-enzyme intermediate; reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
rapid equilibrium random bi-bi reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA I
-
-
acetylene degradation
-
-
gallate degradation III (anaerobic)
-
-
heterolactic fermentation
-
-
L-lysine fermentation to acetate and butanoate
-
-
methanogenesis from acetate
-
-
mixed acid fermentation
-
-
purine nucleobases degradation II (anaerobic)
-
-
pyruvate fermentation to acetate II
-
-
pyruvate fermentation to acetate IV
-
-
sulfoacetaldehyde degradation I
-
-
sulfolactate degradation II
-
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
-
acetate fermentation
-
-
purine metabolism
-
-
Taurine and hypotaurine metabolism
-
-
Pyruvate metabolism
-
-
Propanoate metabolism
-
-
Methane metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphate acetyltransferase
Also acts with other short-chain acyl-CoAs.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetyltransferase, phosphate
-
-
-
-
phosphate acetyltransferase
-
phosphoacylase
-
-
-
-
phosphotransacetylase
-
-
-
-
phosphotransacetylase
-
-
phosphotransacetylase
-
-
phosphotransacetylase
-
-
phosphotransacetylase
-
-
-
phosphotransacetylase
-
-
phosphotransacetylase EutD
-
phosphotransacetylase Pta
-
PTA
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-91-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and mutant deficient in enzyme activity
-
-
Manually annotated by BRENDA team
strain BW25113, wild-type, acs and pta deletion mutants
-
-
Manually annotated by BRENDA team
strain BW25113, wild-type, acs and pta deletion mutants
-
-
Manually annotated by BRENDA team
strain 36, IFO No. 3071
-
-
Manually annotated by BRENDA team
Lactobacillus fermentum 36
strain 36, IFO No. 3071
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
serovar typhimurium LT2
-
-
Manually annotated by BRENDA team
wild-type and mutant strains
-
-
Manually annotated by BRENDA team
hyperthermophilic eubacterium
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the substrate-binding site is located at the C-terminal PTA-PTB domain. The N-terminal P-loop NTPase domain is involved in expression of the maximal catalytic activity, stabilization of the hexameric native state, and phosphate acetyltransferase activity regulation by NADH, ATP, phosphoenolpyruvate, and pyruvate. The truncated protein Pta-F3 is able to complement the growth on acetate of an Escherichia coli mutant defective in acetyl-CoA synthetase and phosphate acetyltransferase activity
physiological function
-
expression of phosphate acetyltransferase eutD restOres the ability of a strain lacking phosphate acetyltransferase pta and acetate kinase to grow on acetate as sole carbon source
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-dephospho-CoA + acetyl phosphate
acetyl-3'-dephospho-CoA + phosphate
show the reaction diagram
Lactobacillus fermentum, Lactobacillus fermentum 36
-
rate is about one tenth of the activity with CoA
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
-
r
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
r
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
with isoform Pta-2, reaction is irreversible, no acetyl phosphate forming reaction can be detected
-
r
acetyl-CoA + arsenate
CoA + acetyl arsenate
show the reaction diagram
-
-
-
?
acetyl-CoA + arsenate
CoA + acetyl arsenate
show the reaction diagram
-
-
-
?
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
formation of acetyl-CoA is favored
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
rate of acetyl-CoA synthesis is 6.5times greater than rate of acetyl phosphate synthesis
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
in reverse reaction specific for CoA
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
in reverse reaction specific for CoA
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
rate of acetyl-CoA synthesis is 10times greater than rate of acetyl phosphate synthesis
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
enables growth on acetate as carbon and energy source, required for ethanolamine catabolism
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
integral role in acetate metabolism
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
Lactobacillus fermentum 36
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
-
?
acetyl-phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
?
acetyl-phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order
-
r
arsenate + acetyl-CoA
acetyl arsenate + CoA
show the reaction diagram
-
-
-
?
arsenate + acetyl-CoA
acetyl arsenate + CoA
show the reaction diagram
-
-
-
?
arsenate + acetyl-CoA
acetyl arsenate + CoA
show the reaction diagram
-
-
-
?
arsenate + acetyl-CoA
acetyl arsenate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + phosphate
CoA + butyryl phosphate
show the reaction diagram
-
-
-
?
butyryl-CoA + phosphate
CoA + butyryl phosphate
show the reaction diagram
-
-
-
?
butyryl-CoA + phosphate
CoA + butyryl phosphate
show the reaction diagram
-
at a rate 0.01 as rapid as acetyl-CoA
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
-
-
-
r
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
involved in taurine catabolism
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
show the reaction diagram
-
-
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
show the reaction diagram
-
-
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
show the reaction diagram
-
-
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
show the reaction diagram
-
at a rate 0.1 to 0.5 as rapid as acetyl-CoA
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
?
additional information
?
-
-
arsenolysis
-
-
-
additional information
?
-
-
physiological function in anaerobic metabolism of eukaryotic green algae rather than in aerobic acetate activation
-
-
-
additional information
?
-
-
mutation of phosphotransacetylase reduces the virulence of Salmonella enterica serovar typhimurium in mice
-
-
-
additional information
?
-
carnitine acetyltransferases catalyse the reversible reaction between carnitine and acetyl-CoA to form acetylcarnitine and free CoA. This reaction is important in transferring activated acetyl groups to the mitochondria and in regulating the acetyl-CoA/CoA pools within the cell
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
-
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
enables growth on acetate as carbon and energy source, required for ethanolamine catabolism
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
integral role in acetate metabolism
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
P41790, Q8ZND6
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
Lactobacillus fermentum 36
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
-
-
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
Q5LMK3
involved in taurine catabolism
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
P41790, Q8ZND6
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
?
additional information
?
-
-
physiological function in anaerobic metabolism of eukaryotic green algae rather than in aerobic acetate activation
-
-
-
additional information
?
-
-
mutation of phosphotransacetylase reduces the virulence of Salmonella enterica serovar typhimurium in mice
-
-
-
additional information
?
-
P32796
carnitine acetyltransferases catalyse the reversible reaction between carnitine and acetyl-CoA to form acetylcarnitine and free CoA. This reaction is important in transferring activated acetyl groups to the mitochondria and in regulating the acetyl-CoA/CoA pools within the cell
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
-
-
acetyl-CoA
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
required, Fe2+ or Mn2+, Mn2+ is 50-75% as effective as Fe2+
K+
-
enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
K+
-
activates; rate of arsenolysis increases with increasing potassium or ammonium salt concentration and reaches a maximum rate at 0.02 to 0.03 M salt concentration
K+
-
enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
K+
-
activates; KCl activates
K+
-
K+ or NH4+ at concentration above 10 mM required for maximum activity
K+
-
3.4fold stimulation at 10 mM
KCl
-
stimulates; stimulates enzyme activity 2.5-fold
Na+
-
less effective than NH4+ and K+
NH4+
-
K+ or NH4+ at concentration above 10 mM required for maximum activity, enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
NH4+
-
required for maximum activity, optimum at 7 mM (NH4)2SO4
NH4+
-
rate of arsenolysis increases with increasing potassium or ammonium salt concentration and reaches a maximum rate at 0.02 to 0.03 M salt concentration
NH4+
-
enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
NH4+
-
no effect
NH4+
-
activates; NH4Cl activates
NH4+
-
above 10 mM
NH4+
-
5.2fold stimulation at 10 mM
NH4+
-
activates
phosphate
-
1 mM, weak activation
Rb+
-
stimulates
Tris
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
Mn2+
-
required, Fe2+ or Mn2+, Mn2+ is 50-75% as effective as Fe2+
additional information
-
mechanism of activation by univalent cations
additional information
-
no activity with: Fe3+, Zn2+, Mg2+, Co2+, Ni2+, Sn2+, Cu2+, Mo6+, K+, NH4+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
activation at low concentration, inhibition at high concentration
(NH4)2SO4
-
above 10 mM
2,2'-dipyridyl
-
-
2,3-Butanedione
-
almost complete loss of wild-type enzyme activity after 10 min at 10 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
acetyl phosphate
-
-
acetyl phosphate
-
substrate inhibition; substrate inhibition
acetyl-CoA
-
competitive
acetyl-CoA
-
competitive
acetyl-CoA
-
competitive
acetyl-CoA
-
competitive inhibitor versus CoA when acetyl phosphate is at subsaturating levels but it does not inhibit versus CoA when acetyl phosphate is at saturating levels. Acetyl-CoA is a competitive inhibitor versus acetyl phosphate when CoA is at subsaturating levels but it does not inhibit versus acetyl phosphate when CoA is at saturating levels
ADP
-
no effect
ADP
-
50% inhibition at 6 mM, MgCl2 reverses inhibition
ADP
-
inhibitory at 1 mM
AMP
-
inhibitory at 1 mM
arsenate
-
50% inhibition at 10 mM
ATP
-
no effect
ATP
-
50% inhibition at 1.5 mM, MgCl2 reverses inhibition
ATP
-
inhibitory at 1 mM
Ba2+
-
15% inhibition at 1 mM, 76% inhibition at 10 mM
Ca2+
-
50% inhibition at 1 mM
citrate buffer
-
0.1 M, pH 8.0
CoA
-
substrate inhibition; substrate inhibition
coenzyme A
-
competitive
coenzyme A
-
-
coenzyme A
-
competitive
coenzyme A
-
strong substrate inhibition
coenzyme A
-
competitive with respect to acetyl-CoA, non competitive with respect to phosphate
desulfo-CoA
-
competitive
desulfo-CoA
-
-
desulfo-CoA
-
strong competitive inhibitor
desulfo-CoA
-
competitive inhibitor with respect to CoA, noncompetitive inhibitor with respect to acetyl phosphate
Diethylbarbiturate
-
potassium diethylbarbiturate buffer, 0.1 M, pH 8.0
Diethylbarbiturate
-
-
diphosphate
-
non competitive
diphosphate
-
50% inhibition at 12 mM
iodoacetamide
-
70% inactivation after 1 min at 5 mM
iodoacetic acid
-
76% inactivation after 4 min at 5 mM
Li+
-
23% inhibition
MgCl2
-
activation at low concentration, inhibition at high concentration
Mn2+
-
50% inhibition at 1 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
above 0.1 mM
N-ethylmaleimide
-
-
Na+
-
85% inhibition
Na+
-
acts as inhibitor in the presence of NH4+ or K+, competitive inhibition
NADH
-
inhibits by changing enzyme conformation, pyruvate counteracts the inhibitory effect of NADH; inhibits by changing the conformation of the enzyme
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
above 0.1 mM
palmitoyl-CoA
-
competitive
Phenylglyoxal
-
33% inhibition after preincubation with phenylglyoxal
phosphate
-
inhibition of arsenolysis
phosphate
-
competitive
phosphate
-
competitive with respect to acyl phosphate, non competitive with respect to CoA
phosphate
-
end product inhibitor
phosphate
-
competitive inhibitor versus acetyl phosphate when CoA is at saturating or subsaturating levels. Phosphate is a noncompetitive inhibitor versus CoA when acetyl phosphate is at a subsaturating level (0.15 mM), but it does not inhibit versus CoA when acetyl phosphate is at a saturating level (4 mM)
phosphate
-
substrate inhibition; substrate inhibition
potassium diphosphate
-
0.1 M, pH 8.0
potassium phosphate
-
above 10 mM
S-Dimethylarsino-CoA
-
irreversible inhibition, phosphate protects
S-Dimethylarsino-CoA
-
-
Tris(hydroxymethyl)aminomethane
-
weak
Tris-citrate
-
-
additional information
-
inhibition by various buffer systems
-
additional information
-
overview: product inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-dimercaptopropanol
-
activates at 0.01 M
cysteine
-
activates at 0.01 M
NH4Cl
-
3fold stimulation at 40 mM. No significant increase in activity above 40 mM; maximal stimulation at 40 mM, 3fold
PPIB
-
cytoplasmic cytophilin, interaction with phosphate acetyltransferase leads to enhanced activity and alteration in Km value. PPIase activity is not essential for these interactions, as PPIB F99A active site mutant still interacts with phosphate acetyltransferase, but PPIB activity is responsible for the observed phosphate acetyltransferase activity enhancement; cytoplasmic cytophilin, interaction with phosphate acetyltransferase leads to enhanced activity and alteration in Km value. PPIase activity is not essential for these interactions, as PPIB F99A active site mutant still interacts with phosphate acetyltransferase, but PPIB activity is responsible for the observed phosphate acetyltransferase activity enhancement
-
pyruvate
-
-
pyruvate
-
stimulates activity of wild-type enzyme 0.2fold over control, and the activity of the mutant enzyme R252H 3fold over control; stimulates wild-type activity, its effect is potentiated in the variants, being most pronounced on R252H
pyruvate
-
156% of activation at 5 mM
thiolglycolic acid
-
activates at 0.01 M
hydrogen sulfide
-
activates at 0.01 M
additional information
-
not significant efects: NADH, ATP, phosphoenol pyruvate and aspartate, even at concentrations as high as 10 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.024
acetyl phosphate
-
-
0.043
acetyl phosphate
-
R87Q mutant
0.073
acetyl phosphate
-
R133Q mutant
0.094
acetyl phosphate
23C, pH 7.2, mutant enzyme S309A
0.096
acetyl phosphate
-
25C, pH 7.2
0.129
acetyl phosphate
-
30C
0.143
acetyl phosphate
23C, pH 7.2, mutant enzyme D316E
0.166
acetyl phosphate
-
R287Q mutant
0.17
acetyl phosphate
-
wild tpye
0.175
acetyl phosphate
23C, pH 7.2, mutant enzyme S309T
0.18
acetyl phosphate
-
wild-type after expression in E. coli
0.185
acetyl phosphate
23C, pH 7.2, wild-type enzyme
0.186
acetyl phosphate
-
25C, pH 7.2
0.187
acetyl phosphate
-
C277A mutant
0.191
acetyl phosphate
-
C159S mutant
0.198
acetyl phosphate
-
C312A mutant
0.206
acetyl phosphate
-
C159A mutant
0.222
acetyl phosphate
-
C159A/C277A/C312A/C325A mutant
0.23
acetyl phosphate
-
C325A mutant
0.254
acetyl phosphate
-
C277A/C312A/C325A mutant
0.255
acetyl phosphate
23C, pH 7.2, mutant enzyme S309C
0.311
acetyl phosphate
-
-
0.312
acetyl phosphate
-
pH 7.8, 30C
0.464
acetyl phosphate
-
pH 7.2, 35C, presence of 10fold molar excess of activator PPIB
0.5
acetyl phosphate
-
pH 7.2, 35C
0.531
acetyl phosphate
23C, pH 7.2, mutant enzyme R310K
0.59
acetyl phosphate
-
-
0.616
acetyl phosphate
-
pH 7.2, 35C, presence of 10fold molar excess of activator PPIB
0.66
acetyl phosphate
-
-
0.66
acetyl phosphate
-
-
0.775
acetyl phosphate
-
R310Q mutant
0.775
acetyl phosphate
23C, pH 7.2, mutant enzyme R310Q
0.9
acetyl phosphate
wild-type, pH 8.0, 30C
1
acetyl phosphate
-
pH 7.2, 35C
1.1
acetyl phosphate
mutant Pta-F1, pH 8.0, 30C
1.3
acetyl phosphate
-
-
1.32
acetyl phosphate
-
R28Q mutant
1.7
acetyl phosphate
mutant Pta-F1, pH 8.0, 30C
2.4
acetyl phosphate
mutant Pta-F1, pH 8.0, 30C
4.7
acetyl phosphate
-
-
22.5
acetyl phosphate
23C, pH 7.2, mutant enzyme R310A
0.0086
acetyl-CoA
-
-
0.0095
acetyl-CoA
-
pH 7.8, 30C
0.0231
acetyl-CoA
-
-
0.029
acetyl-CoA
mutant Pta-F1, pH 8.0, 30C S0.5-value, Hill constant 2.1
0.039
acetyl-CoA
mutant Pta-F1, pH 8.0, 30C, S0.5-value, Hill constant 1.3
0.041
acetyl-CoA
-
pH 7.2, 35C, presence of 10fold molar excess of activator PPIB
0.045
acetyl-CoA
wild-type, pH 8.0, 30C, S0.5-value, Hill constant 1.3
0.05
acetyl-CoA
-
pH 7.2, 35C
0.058
acetyl-CoA
mutant Pta-F1, pH 8.0, 30C, S0.5-value, Hill constant 1.8
0.06
acetyl-CoA
-
-
0.078
acetyl-CoA
-
-
0.2812
acetyl-CoA
-
37C, pH 7.5, mutant enzyme G273D; mutant enzyme G273D
0.2814
acetyl-CoA
-
37C, pH 7.5, mutant enzyme M294I; mutant enzyme M294I
0.3293
acetyl-CoA
-
37C, pH 7.5, wild-type enzyme; wild-type enzyme
0.5297
acetyl-CoA
-
37C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
0.058
Butyryl-CoA
-
-
0.0327
CoA
-
pH 7.8, 30C
0.034
CoA
-
R287Q mutant
0.037
CoA
-
R310Q mutant
0.037
CoA
23C, pH 7.2, mutant enzyme S309T
0.046
CoA
-
30C
0.059
CoA
mutant Pta-F1, pH 8.0, 30C
0.062
CoA
mutant Pta-F1, pH 8.0, 30C
0.065
CoA
23C, pH 7.2, wild-type enzyme
0.065
CoA
-
25C, pH 7.2
0.066
CoA
mutant Pta-F1, pH 8.0, 30C, Hill-constant 1.6
0.067
CoA
23C, pH 7.2, mutant enzyme S309A
0.067
CoA
wild-type, pH 8.0, 30C, Hill-constatn 1.7
0.07
CoA
-
wild-type
0.071
CoA
-
C159S mutant
0.073
CoA
-
C159A/C277A/C312A/C325A mutant
0.074
CoA
23C, pH 7.2, mutant enzyme D316E
0.078
CoA
-
C325A mutant
0.086
CoA
-
C277A/C312A/C325A mutant
0.089
CoA
-
wild-type after expression in E. coli
0.09
CoA
-
arsenolysis
0.09
CoA
-
wild tpye
0.092
CoA
-
C312A mutant
0.093
CoA
-
C159A mutant; C277A mutant
0.094
CoA
23C, pH 7.2, mutant enzyme S309C
0.11
CoA
-
R133K mutant
0.116
CoA
23C, pH 7.2, mutant enzyme R310K
0.12
CoA
23C, pH 7.2, mutant enzyme R310A
0.13
CoA
-
pH 7.2, 35C, presence of 10fold molar excess of activator PPIB
0.1621
CoA
-
37C, pH 7.5, wild-type enzyme; wild-type enzyme
0.163
CoA
-
37C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
0.168
CoA
-
37C, pH 7.5, mutant enzyme G273D
0.1683
CoA
-
mutant enzyme G273D
0.185
CoA
23C, pH 7.2, mutant enzyme R310Q
0.192
CoA
-
37C, pH 7.5, mutant enzyme M294I; mutant enzyme M294I
0.2
CoA
-
pH 7.2, 35C
0.219
CoA
-
pH 7.2, 35C, presence of 10fold molar excess of activator PPIB
0.253
CoA
-
R28Q mutant
0.27
CoA
-
R87E mutant
0.3
CoA
-
pH 7.2, 35C
0.36
CoA
-
R133A mutant
0.7
CoA
-
R133E mutant; R133Q mutant
0.747
CoA
-
R87Q mutant
0.75
CoA
-
R87K mutant
0.9
CoA
-
R87A mutant
1.1
CoA
-
R87Q mutant
1.694
CoA
-
R133Q mutant
0.8
desulfo-CoA
-
R133K mutant; R87E mutant
1
desulfo-CoA
-
R133E mutant
1.3
desulfo-CoA
-
R133A mutant; R87Q mutant
1.4
desulfo-CoA
-
wild-type
3.9
desulfo-CoA
-
R87K mutant
4
desulfo-CoA
-
R133Q mutant
0.111
phosphate
-
-
0.742
phosphate
-
25C, pH 7.2
1.1
phosphate
-
37C, pH 7.5, mutant enzyme G273D; mutant enzyme G273D
1.3
phosphate
-
37C, pH 7.5, mutant enzyme M294I; mutant enzyme M294I
1.5
phosphate
-
37C, pH 7.5, wild-type enzyme; wild-type enzyme
1.5
phosphate
mutant Pta-F1, pH 8.0, 30C
1.9
phosphate
mutant Pta-F1, pH 8.0, 30C
2.1
phosphate
wild-type, pH 8.0, 30C
2.8
phosphate
-
37C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
3
phosphate
mutant Pta-F1, pH 8.0, 30C
5.44
phosphate
-
-
9.3
phosphate
-
-
11
phosphate
-
pH 7.2, 35C
12.3
phosphate
-
pH 7.2, 35C, presence of 10fold molar excess of activator PPIB
0.15
propionyl-CoA
-
-
6
desulfo-CoA
-
R87A mutant
additional information
additional information
-
effects of monovalent kations
-
additional information
additional information
-
kinetic studies
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
acetyl phosphate
Escherichia coli
P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.32
acetyl phosphate
Methanosarcina thermophila
-
C159A mutant
1.56
acetyl phosphate
Escherichia coli
P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.63
acetyl phosphate
Methanosarcina thermophila
-
R310Q mutant
2.16
acetyl phosphate
Escherichia coli
P0A9M8
mutant Pta-F1, pH 8.0, 30C
3.03
acetyl phosphate
Methanosarcina thermophila
-
C159A/C277A/C312A/C325A mutant
4.93
acetyl phosphate
Methanosarcina thermophila
-
R87Q mutant
5.45
acetyl phosphate
Methanosarcina thermophila
-
mutant R287Q
12.5
acetyl phosphate
Methanosarcina thermophila
-
R133Q mutant
24.1
acetyl phosphate
Methanosarcina thermophila
-
mutant R28Q
40.6
acetyl phosphate
Methanosarcina thermophila
-
wild type
44.5
acetyl phosphate
Methanosarcina thermophila
-
C312A mutant
51.6
acetyl phosphate
Methanosarcina thermophila
-
C277A/C312A/C325A mutant
57.6
acetyl phosphate
Methanosarcina thermophila
-
C325A mutant
66.3
acetyl phosphate
Methanosarcina thermophila
-
C159S mutant
68.5
acetyl phosphate
Methanosarcina thermophila
-
wild-type after expression in E. coli
94.9
acetyl phosphate
Methanosarcina thermophila
-
C277A mutant
227
acetyl phosphate
Escherichia coli
P0A9M8
wild-type, pH 8.0, 30C
403.5
acetyl phosphate
Salmonella enterica
-
mutant enzyme M294I
415
acetyl phosphate
Escherichia coli
-
pH 7.8, 30C
574.5
acetyl phosphate
Salmonella enterica
-
wild-type enzyme
1301
acetyl phosphate
Salmonella enterica
-
mutant enzyme G273D
1480
acetyl phosphate
Salmonella enterica
-
mutant enzyme R252H
1500
acetyl phosphate
Methanosarcina thermophila
-
25C, pH 7.2
1927
acetyl phosphate
Salmonella enterica
-
30C, calculated per monomer
5190
acetyl phosphate
Methanosarcina thermophila
-
25C, pH 7.2
0.03
acetyl-CoA
Escherichia coli
P0A9M8
mutant Pta-F1, pH 8.0, 30C
0.23
acetyl-CoA
Escherichia coli
P0A9M8
mutant Pta-F1, pH 8.0, 30C
0.43
acetyl-CoA
Escherichia coli
P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.73
acetyl-CoA
Salmonella enterica
-
37C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
25
acetyl-CoA
Salmonella enterica
-
37C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
29.6
acetyl-CoA
Escherichia coli
P0A9M8
wild-type, pH 8.0, 30C
57.9
acetyl-CoA
Salmonella enterica
-
37C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme; mutant enzyme M294I
83.1
acetyl-CoA
Salmonella enterica
-
wild-type enzyme
120
acetyl-CoA
Escherichia coli
-
pH 7.8, 30C
208.9
acetyl-CoA
Salmonella enterica
-
mutant enzyme R252H
252.5
acetyl-CoA
Salmonella enterica
-
37C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme; mutant enzyme G273D
4500
acetyl-CoA
Methanosarcina thermophila
-
-
0.283
CoA
Methanosarcina thermophila
-
R87E mutant
0.733
CoA
Methanosarcina thermophila
-
R133E mutant
1.42
CoA
Methanosarcina thermophila
-
R310Q mutant
1.48
CoA
Methanosarcina thermophila
-
C159A mutant
3.3
CoA
Methanosarcina thermophila
-
C159A/C277A/C312A/C325A mutant
5.95
CoA
Methanosarcina thermophila
-
mutant R287Q
6.1
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme S309C
6.22
CoA
Methanosarcina thermophila
-
R87K mutant
6.97
CoA
Methanosarcina thermophila
-
R133K mutant
10.5
CoA
Methanosarcina thermophila
-
R133A mutant
11
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme R310K
14.5
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme S309A
15.4
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme S309T
19.1
CoA
Methanosarcina thermophila
-
R133Q mutant
20.4
CoA
Methanosarcina thermophila
-
R87A mutant
23.2
CoA
Methanosarcina thermophila
-
R87Q mutant
24.6
CoA
Methanosarcina thermophila
-
R87Q mutant
26
CoA
Methanosarcina thermophila
-
mutant R28Q
45.6
CoA
Methanosarcina thermophila
-
R133Q mutant
53.6
CoA
Methanosarcina thermophila
-
C277A/C312A/C325A mutant
53.8
CoA
Methanosarcina thermophila
-
wild type
55.4
CoA
Methanosarcina thermophila
-
C312A mutant
59.9
CoA
Methanosarcina thermophila
-
C325A mutant
69
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme R310Q
73.5
CoA
Methanosarcina thermophila
-
C159S mutant
81.3
CoA
Methanosarcina thermophila
-
wild-type
87.5
CoA
Methanosarcina thermophila
-
wild-type after expression in E. coli
100
CoA
Methanosarcina thermophila
-
C277A mutant
230
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme R310A
403
CoA
Salmonella enterica
-
37C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme
574.5
CoA
Salmonella enterica
-
37C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
1301
CoA
Salmonella enterica
-
37C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme
1480
CoA
Salmonella enterica
-
37C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
2150
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, mutant enzyme D316E
5190
CoA
Methanosarcina thermophila
P38503
23C, pH 7.2, wild-type enzyme
5190
CoA
Methanosarcina thermophila
-
25C, pH 7.2
0.00467
desulfo-CoA
Methanosarcina thermophila
-
R133E mutant
0.0125
desulfo-CoA
Methanosarcina thermophila
-
R133A mutant
0.133
desulfo-CoA
Methanosarcina thermophila
-
R133K mutant
0.383
desulfo-CoA
Methanosarcina thermophila
-
R87E mutant
0.467
desulfo-CoA
Methanosarcina thermophila
-
R133Q mutant
0.683
desulfo-CoA
Methanosarcina thermophila
-
R87K mutant
1.63
desulfo-CoA
Methanosarcina thermophila
-
R87Q mutant
3.07
desulfo-CoA
Methanosarcina thermophila
-
R87A mutant
4.53
desulfo-CoA
Methanosarcina thermophila
-
wild-type
1500
phosphate
Methanosarcina thermophila
-
25C, pH 7.2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1300
acetyl phosphate
Escherichia coli
-
pH 7.8, 30C
358
12600
acetyl-CoA
Escherichia coli
-
pH 7.8, 30C
29
12600
CoA
Escherichia coli
-
pH 7.8, 30C
18
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.2
acetyl phosphate
-
pH 7.2, 35C
12
acetyl phosphate
-
pH 7.2, 35C
0.04
CoA
-
pH 7.2, 35C
0.1
CoA
-
pH 7.2, 35C
0.001
desulfo-CoA
-
-
0.0013
desulfo-CoA
-
25C, pH 7.2, with respect to CoA
0.0028
desulfo-CoA
-
25C, pH 7.2, with respect to acetyl phosphate
0.004
desulfo-CoA
-
-
0.02
desulfo-CoA
-
-
1.1
NADH
-
37C, pH 7.5, wild-type enzyme; wild type enzyme
0.32
phosphate
-
R133Q mutant
0.52
phosphate
-
R87Q mutant
0.81
phosphate
-
wild-type enzyme
19
phosphate
-
pH 7.2, 35C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9100
-
after crystallization
additional information
-
assay methods
additional information
-
assay methods
additional information
-
-
additional information
-
specific activities of recombinant plasmids expressed in Escherichia coli and Clostridium acetobutylicum
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
-
both directions
7.6
-
Tris buffer
7.8
-
activity assay
additional information
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.8
-
90% loss of activity at pH 6.5, 25% loss of activity at pH 7.8
6.6 - 8.2
-
about 50% of activity maximum at pH 6.6 pH and 8.2
6.8 - 8.6
-
pH 6.8: about 25% of activity maximum, pH 8.6: about 90% of activity maximum
7 - 8.5
-
pH 7.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
7 - 8.7
-
pH 7.0: about 10% of activity maximum, pH 8.7: about 20% of activity maximum
additional information
-
pH effects on enzymatic reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
-
both directions
37
-
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 40
-
only small effect of temperature in this range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
-
calculated from the deduced amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
effectively absent in acetate grown cells, also absent in cysteate-grown cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35200
-
calculated from amino acid sequence
487541
35500
-
calculated from amino acid sequence
487540
36200
-
calculated from amino acid sequence
487538
38000 - 41000
-
ultracentrifugation
487514
40000
-
SDS-PAGE
487540
52000
-
gel filtration
487526
54500
-
gel filtration
487525
63000 - 75000
-
gel filtration
487529
68000
-
gel filtration
487533
70400
-
calculated from the deduced amino acid sequence
660521
71000
-
gel filtration
660521
71000
-
dynamic light scattering
674263
71300
-
calculated from hydrodynamic radius obtained from dynamic light scattering
657448
75000 - 80000
-
gel filtration
487523
76000
-
gel filtration
487543
79500
-
gel filtration
720217
88000
-
gel filtration
487524
90000
-
gel filtration
487527
170000
-
gel filtration
487537
280000
-
gel filtration, SDS-PAGE
487517
490000
-
gel filtration
674792
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 70000, SDS-PAGE
?
x * 77000, SDS-PAGE, recombinant protein
?
-
x * 76000, SDS-PAGE, recombinant protein; x * 77000, SDS-PAGE, recombinant protein
dimer
-
2 * 35000-40000, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE
dimer
-
in solution, dynamic light scattering
dimer
-
crystal structure analysis
dimer
-
in solution and in crystals
dimer
-
dynamic light scattering
dimer
-
2 * 36000, SDs-PAGE, recombinant protein
hexamer
-
6 * 44000, SDS-PAGE
hexamer
-
it is possible that native Pta is a dimer of trimers
monomer
-
1 * 52500, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
tetramer
-
4 * 20000, SDS-PAGE
tetramer
-
alpha4, homotetramer, 4 * 34000, SDS-PAGE
trimer
-
wild-type enzyme is a trimer. Pta variants formmore hexamer than the wild-typ protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structures of the enzyme at 2.75 A resolution and its complex with acetyl phosphate at 2.85 A resolution
-
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method. Crystal structures of phosphotransacetylase in complex with the substrate CoA reveals one CoA (CoA(1)) bound in the proposed active site cleft and an additional CoA (CoA(2)) bound at the periphery of the cleft. The crystal structures indicat that binding of CoA(1) is mediated by a series of hydrogen bonds and extensive van der Waals interactions with the enzyme and that there are fewer of these interactions between CoA(2) and the enzyme
hanging-drop vapor diffusion method
-
hanging drop vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, 40C, 5 min, stable
487514
7 - 10
-
stable
487540
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
50% loss of activity within 5 min
659038
37
-
half-life: 20 min
487523
40
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, stable
487514
45
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 15% loss of activity
487514
45
-
unstable, can be stabilized by ammonium sulfate
487533
45
-
90% loss of activity within 5 min
659038
50
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 48% loss of activity
487514
50
-
t1/2 18 min
487517
60
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 98% loss of activity
487514
60
-
pH 8.0, 50 mM Tris/HCl, complete loss of activity after 1 min
487525
60
-
inactivation after 15 min
487540
70
-
5 min, stable up to 70C in absence of additional salts
487526
80
-
5 min, complete inactivation in absence of additional salts
487526
80
-
stable for 120 min
487537
88
-
60 min, 44% loss of activity
487529
90
-
60% loss of activity after 120 min
487537
100
-
2 min, complete inactivation after boiling
487524
100
-
60% loss of activity after 120 min
487537
additional information
-
sulfate and phosphate partially protect against heat inactivation
487526
additional information
-
-
487533
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized by addition of 200 mM ammonium sulfate and 2-5 mM mercaptans to the extraction buffer
-
activity is lost upon dialysis and cannot be restored by addition of known cofactors or crude boiled extracts
-
dilute solutions are instable, in frozen state stable
-
50-60% loss of activity after dialysis for 8 h against 0.05 M Tris buffer, Fe2+ and dithiothreitol stabilize
-
lyophilization causes almost complete loss of enzyme activity
-
sulfate and phosphate partially protect against heat inactivation
-
(NH4)2SO4, Na2SO4, NaCl or KCl stabilizes
-
ammonium sulfate and potassium phosphate stabilize
-
ethylene glycol 20% v/v stabilizes
-
labile in dilute solutions or at elevated temperatures
-
MgCl2 destabilizes
-
NH4Cl sligthly stabilizes
-
repeated freezing and thawing inactivates
-
divalent cations, e.g. FeSO4, Fe(NH4)2SO4, MgCl2, MnCl2, MgSO4 or ATP increase lability
-
increased stability is obtained by adding a reducing agent and a component of the reaction
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to air
-
487526
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, stable for several months
-
-20C, 0.2 M phosphate or Tris-HCl, pH 8.0, several months
-
0-4C, 2.7-3.0 M ammonium sulfate, months
-
stable for at least 3 h when stored on ice
-
-24C, (NH4)2SO4, 50-70% loss of activity after some months
-
-20C, no loss of activity for several weeks
-
4C or -20C, protein concentration 0.5 mg/ml, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme is associated with the pyruvate dehydrogenase complex
-
fusion protein with beta-galactosidase
-
affinity chromatography, 73% pure
-
homogeneity, biotinylated fusion protein
-
recombinant enzyme from Escherichia coli
-
recombinant protein using His-tag
-
recombinant protein using His-tag
-
apparent homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in soluble form in Escherichia coli BL21-DE3
-
expression in Escherichia coli
overexpressing CAT2, which encodes the major mitochondrial and peroxisomal carnitine acetyltransferase, on the formation of esters and other flavour compounds during fermentation and overexpression of a modified CAT2 that results in a protein that localizes to the cytosol. The overexpression of both forms of CAT2 resulted in a reduction in ester concentrations, especially in ethyl acetate and isoamyl acetate
expressed as His-tag fusion protein in Escherichia coli BL21(lambdaDE3)
-
expression in Escherichia coli
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)/pSJS1244
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene is expressed during exponential growth on glucose or acetate and is downregulated in the stationary phase; gene is expressed during exponential growth on glucose or acetate and is downregulated in the stationary phase
-
availabity of ammonium during growth on acetate results in upregulation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C159A
-
Km similar to wild-type enzyme
C159A/C277A/C312A/C325A
-
Km similar to wild-type enzyme
C159S
-
Km similar to wild-type enzyme
C277A
-
Km similar to wild-type enzyme
C277A/C312A/C325A
-
Km similar to wild-type enzyme
C312A
-
Km similar to wild-type enzyme
C325A
-
Km similar to wild-type enzyme
D316E
kcat for the reaction of acetyl phosphate and CoA is 2.4fold lower than wild-type value, Km for CoA is 1.1fold higher than wild-type value, Km for acetyl phosphate is 1.4fold lower than wild-type value
R133A
-
altered kinetic properties, increased Km for CoA
R133E
-
altered kinetic properties, increased Km for CoA
R133K
-
altered kinetic properties, increased Km for CoA
R133Q
-
altered kinetic properties, increased Km for CoA
R133Q
-
increased Km for CoA, decreased Km for acetyl phosphate
R287Q
-
decreased Km for CoA
R28Q
-
increased Km
R310A
kcat for the reaction of acetyl phosphate and CoA is 22.6fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 122fold higher than wild-type value
R310K
kcat for the reaction of acetyl phosphate and CoA is 472fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 2.9fold higher than wild-type value
R310Q
-
decreased Km for CoA
R310Q
kcat for the reaction of acetyl phosphate and CoA is 75.2fold lower than wild-type value, Km for CoA is 2.8fold higher than wild-type value, Km for acetyl phosphate is 4.2fold higher than wild-type value
R87A
-
altered kinetic properties, increased Km for CoA
R87E
-
altered kinetic properties, increased Km for CoA
R87K
-
altered kinetic properties, increased Km for CoA
R87Q
-
altered kinetic properties, increased Km for CoA
R87Q
-
increased Km for CoA, decreased Km for acetyl phosphate
S309A
kcat for the reaction of acetyl phosphate and CoA is 358fold lower than wild-type value, Km for CoA is nearly identical to wild-type value, Km for acetyl phosphate is 1.96fold lower than wild-type value
S309C
kcat for the reaction of acetyl phosphate and CoA is 851fold lower than wild-type value, Km for CoA is1.4 fold higher than wild-type value, Km for acetyl phosphate is 1.4fold higher than wild-type value
S309T
kcat for the reaction of acetyl phosphate and CoA is 337fold lower than wild-type value, Km for CoA is 1.8fold lower than wild-type value, Km for acetyl phosphate is nearly identical to wild-type value
G273D
-
kcat for reaction with acetyl-CoA and phosphate is 3fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.3fold higher than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme; kcat/Km for CoA is 2.2fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 3.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
M294I
-
kcat for reaction with acetyl-CoA and phosphate is 143fold lower than wild-type value, kcat for reaction with CoA and acetyl phosphate is 1.4fold lower than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme; kcat/Km for CoA is 1.7fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.2lower higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
R252H
-
kcat for reaction with acetyl-CoA and phosphate is 2.5fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.5fold higher than wild-type value. No inhibition by NADH. Mutant enzyme shows less aggregation than wild type enzyme; kcat/Km for CoA is 2.6fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
additional information
construction of truncated mutants Pta-F1, consisting of the PTA-PTB domains, mutant Pta-F2, consisting of the PTA-PTB domains plus part of the DRTGG motif, and Pta-F3, consisting of the PTA-PTB domains plus the complete DRTGG motif. CD spectra for Pta-F1, Pta-F2 and Pta-F3 are comparable, but not identical, to the spectrum of the entire protein