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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA I
-
acetylene degradation
-
Carbon fixation pathways in prokaryotes
-
gallate degradation III (anaerobic)
-
heterolactic fermentation
-
lysine fermentation to acetate and butyrate
-
Metabolic pathways
-
Methane metabolism
-
methanogenesis from acetate
-
Microbial metabolism in diverse environments
-
mixed acid fermentation
-
Propanoate metabolism
-
purine nucleobases degradation II (anaerobic)
-
pyruvate fermentation to acetate II
-
pyruvate fermentation to acetate IV
-
Pyruvate metabolism
-
sulfoacetaldehyde degradation I
-
sulfolactate degradation II
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
Taurine and hypotaurine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphate acetyltransferase
Also acts with other short-chain acyl-CoAs.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetyltransferase, phosphate
-
-
-
-
phosphate acetyltransferase
Q5LMK3
-
phosphoacylase
-
-
-
-
phosphotransacetylase
-
-
-
-
phosphotransacetylase
-
-
phosphotransacetylase
-
-
phosphotransacetylase
-
-
phosphotransacetylase
-
-
-
phosphotransacetylase
-
-
phosphotransacetylase EutD
P41790
-
phosphotransacetylase Pta
Q8ZND6
-
PTA
-
-
-
-
PTA
P0A9M8
-
PTA
Q5LMK3
-
CAS REGISTRY NUMBER
COMMENTARY
9029-91-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-, P0A9M8
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 ACCESSION NO.
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
P0A9M8
-
-
-
r
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-, C1DER7, C1DQG8
-
-
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-, C1DER7, C1DQG8
with isoform Pta-2, reaction is irreversible, no acetyl phosphate forming reaction can be detected
-
-
i
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
P32796
-
-
-
?
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
-
-
-
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
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
-
-
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
P0A9M8
-
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-, C1DER7, C1DQG8
-
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
P38503
-
-
-
?
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
-
-
-
?
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
Q5LMK3
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
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
?
-
-
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
?
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
-
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
-
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
-
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
-
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
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
additional information
-
inhibition by various buffer systems
-
additional information
-
overview: product inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
-
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.024
-
acetyl phosphate
-
-
0.043
-
acetyl phosphate
-
R87Q mutant
0.073
-
acetyl phosphate
-
R133Q mutant
0.094
-
acetyl phosphate
P38503
23C, pH 7.2, mutant enzyme S309A
0.096
-
acetyl phosphate
-
25C, pH 7.2
0.129
-
acetyl phosphate
-
30C
0.143
-
acetyl phosphate
P38503
23C, pH 7.2, mutant enzyme D316E
0.166
-
acetyl phosphate
-
R287Q mutant
0.17
-
acetyl phosphate
-
wild tpye
0.175
-
acetyl phosphate
P38503
23C, pH 7.2, mutant enzyme S309T
0.18
-
acetyl phosphate
-
wild-type after expression in E. coli
0.185
-
acetyl phosphate
P38503
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
P38503
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
P38503
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
P38503
23C, pH 7.2, mutant enzyme R310Q
0.9
-
acetyl phosphate
-, P0A9M8
wild-type, pH 8.0, 30C
1
-
acetyl phosphate
-
pH 7.2, 35C
1.1
-
acetyl phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.3
-
acetyl phosphate
-
-
1.32
-
acetyl phosphate
-
R28Q mutant
1.7
-
acetyl phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
2.4
-
acetyl phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
4.7
-
acetyl phosphate
-
-
22.5
-
acetyl phosphate
P38503
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
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C S0.5-value, Hill constant 2.1
0.039
-
acetyl-CoA
-, P0A9M8
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
-, P0A9M8
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
-, P0A9M8
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
P38503
23C, pH 7.2, mutant enzyme S309T
0.046
-
CoA
-
30C
0.059
-
CoA
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
0.062
-
CoA
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
0.065
-
CoA
P38503
23C, pH 7.2, wild-type enzyme
0.065
-
CoA
-
25C, pH 7.2
0.066
-
CoA
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C, Hill-constant 1.6
0.067
-
CoA
P38503
23C, pH 7.2, mutant enzyme S309A
0.067
-
CoA
-, P0A9M8
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
P38503
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
P38503
23C, pH 7.2, mutant enzyme S309C
0.11
-
CoA
-
R133K mutant
0.116
-
CoA
P38503
23C, pH 7.2, mutant enzyme R310K
0.12
-
CoA
P38503
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
P38503
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
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.9
-
phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
2.1
-
phosphate
-, P0A9M8
wild-type, pH 8.0, 30C
2.8
-
phosphate
-
37C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
3
-
phosphate
-, P0A9M8
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.15
-
acetyl phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.32
-
acetyl phosphate
-
C159A mutant
1.56
-
acetyl phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.63
-
acetyl phosphate
-
R310Q mutant
2.16
-
acetyl phosphate
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
3.03
-
acetyl phosphate
-
C159A/C277A/C312A/C325A mutant
4.93
-
acetyl phosphate
-
R87Q mutant
5.45
-
acetyl phosphate
-
mutant R287Q
12.5
-
acetyl phosphate
-
R133Q mutant
24.1
-
acetyl phosphate
-
mutant R28Q
40.6
-
acetyl phosphate
-
wild type
44.5
-
acetyl phosphate
-
C312A mutant
51.6
-
acetyl phosphate
-
C277A/C312A/C325A mutant
57.6
-
acetyl phosphate
-
C325A mutant
66.3
-
acetyl phosphate
-
C159S mutant
68.5
-
acetyl phosphate
-
wild-type after expression in E. coli
94.9
-
acetyl phosphate
-
C277A mutant
227
-
acetyl phosphate
-, P0A9M8
wild-type, pH 8.0, 30C
403.5
-
acetyl phosphate
-
mutant enzyme M294I
415
-
acetyl phosphate
-
pH 7.8, 30C
574.5
-
acetyl phosphate
-
wild-type enzyme
1301
-
acetyl phosphate
-
mutant enzyme G273D
1480
-
acetyl phosphate
-
mutant enzyme R252H
1500
-
acetyl phosphate
-
25C, pH 7.2
1927
-
acetyl phosphate
-
30C, calculated per monomer
5190
-
acetyl phosphate
-
25C, pH 7.2
0.03
-
acetyl-CoA
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
0.23
-
acetyl-CoA
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
0.43
-
acetyl-CoA
-, P0A9M8
mutant Pta-F1, pH 8.0, 30C
1.73
-
acetyl-CoA
-
37C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
25
-
acetyl-CoA
-
37C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
29.6
-
acetyl-CoA
-, P0A9M8
wild-type, pH 8.0, 30C
57.9
-
acetyl-CoA
-
37C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme; mutant enzyme M294I
83.1
-
acetyl-CoA
-
wild-type enzyme
120
-
acetyl-CoA
-
pH 7.8, 30C
208.9
-
acetyl-CoA
-
mutant enzyme R252H
252.5
-
acetyl-CoA
-
37C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme; mutant enzyme G273D
0.283
-
CoA
-
R87E mutant
0.733
-
CoA
-
R133E mutant
1.42
-
CoA
-
R310Q mutant
1.48
-
CoA
-
C159A mutant
3.3
-
CoA
-
C159A/C277A/C312A/C325A mutant
5.95
-
CoA
-
mutant R287Q
6.1
-
CoA
P38503
23C, pH 7.2, mutant enzyme S309C
6.22
-
CoA
-
R87K mutant
6.97
-
CoA
-
R133K mutant
10.5
-
CoA
-
R133A mutant
11
-
CoA
P38503
23C, pH 7.2, mutant enzyme R310K
14.5
-
CoA
P38503
23C, pH 7.2, mutant enzyme S309A
15.4
-
CoA
P38503
23C, pH 7.2, mutant enzyme S309T
19.1
-
CoA
-
R133Q mutant
20.4
-
CoA
-
R87A mutant
23.2
-
CoA
-
R87Q mutant
24.6
-
CoA
-
R87Q mutant
26
-
CoA
-
mutant R28Q
45.6
-
CoA
-
R133Q mutant
53.6
-
CoA
-
C277A/C312A/C325A mutant
53.8
-
CoA
-
wild type
55.4
-
CoA
-
C312A mutant
59.9
-
CoA
-
C325A mutant
69
-
CoA
P38503
23C, pH 7.2, mutant enzyme R310Q
73.5
-
CoA
-
C159S mutant
81.3
-
CoA
-
wild-type
87.5
-
CoA
-
wild-type after expression in E. coli
100
-
CoA
-
C277A mutant
230
-
CoA
P38503
23C, pH 7.2, mutant enzyme R310A
403
-
CoA
-
37C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme
574.5
-
CoA
-
37C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
1301
-
CoA
-
37C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme
1480
-
CoA
-
37C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
2150
-
CoA
P38503
23C, pH 7.2, mutant enzyme D316E
5190
-
CoA
P38503
23C, pH 7.2, wild-type enzyme
5190
-
CoA
-
25C, pH 7.2
0.00467
-
desulfo-CoA
-
R133E mutant
0.0125
-
desulfo-CoA
-
R133A mutant
0.133
-
desulfo-CoA
-
R133K mutant
0.383
-
desulfo-CoA
-
R87E mutant
0.467
-
desulfo-CoA
-
R133Q mutant
0.683
-
desulfo-CoA
-
R87K mutant
1.63
-
desulfo-CoA
-
R87Q mutant
3.07
-
desulfo-CoA
-
R87A mutant
4.53
-
desulfo-CoA
-
wild-type
1500
-
phosphate
-
25C, pH 7.2
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1300
-
acetyl phosphate
-
pH 7.8, 30C
6148
12600
-
acetyl-CoA
-
pH 7.8, 30C
6194
12600
-
CoA
-
pH 7.8, 30C
8729
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
-
-
both directions
37
-
-
activity assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
40
-
only small effect of temperature in this range
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.1
-
-
calculated from the deduced amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q5LMK3
effectively absent in acetate grown cells, also absent in cysteate-grown cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35200
-
-
calculated from amino acid sequence
35500
-
-
calculated from amino acid sequence
36200
-
-
calculated from amino acid sequence
38000
41000
-
ultracentrifugation
52000
-
-
gel filtration
54500
-
-
gel filtration
63000
75000
-
gel filtration
68000
-
-
gel filtration
70400
-
-
calculated from the deduced amino acid sequence
71000
-
-
gel filtration
71000
-
-
dynamic light scattering
71300
-
-
calculated from hydrodynamic radius obtained from dynamic light scattering
75000
80000
-
gel filtration
76000
-
-
gel filtration
79500
-
-
gel filtration
88000
-
-
gel filtration
90000
-
-
gel filtration
170000
-
-
gel filtration
280000
-
-
gel filtration, SDS-PAGE
490000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 70000, SDS-PAGE
?
-, P0A9M8
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 ACCESSION NO.
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
P38503
hanging-drop vapor diffusion method
-
hanging drop vapor diffusion method
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, 40C, 5 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
50% loss of activity within 5 min
37
-
-
half-life: 20 min
40
-
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, stable
45
-
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 15% loss of activity
45
-
-
unstable, can be stabilized by ammonium sulfate
45
-
-
90% loss of activity within 5 min
50
-
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 48% loss of activity
50
-
-
t1/2 18 min
60
-
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 98% loss of activity
60
-
-
pH 8.0, 50 mM Tris/HCl, complete loss of activity after 1 min
60
-
-
inactivation after 15 min
70
-
-
5 min, stable up to 70C in absence of additional salts
80
-
-
5 min, complete inactivation in absence of additional salts
80
-
-
stable for 120 min
88
-
-
60 min, 44% loss of activity
90
-
-
60% loss of activity after 120 min
100
-
-
2 min, complete inactivation after boiling
100
-
-
60% loss of activity after 120 min
additional information
-
-
sulfate and phosphate partially protect against heat inactivation
additional information
-
-
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stabilized by addition of 200 mM ammonium sulfate and 2-5 mM mercaptans to the extraction buffer
-
50-60% loss of activity after dialysis for 8 h against 0.05 M Tris buffer, Fe2+ and dithiothreitol stabilize
-
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
-
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 ACCESSION NO.
LITERATURE
stable to air
-
487526
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
P38503
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
P32796
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 ACCESSION NO.
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 ACCESSION NO.
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
P38503
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
P38503
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
P38503
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
P38503
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
P38503
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
P38503
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
P38503
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
-, P0A9M8
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