Information on EC 3.6.1.7 - acylphosphatase

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

EC NUMBER
COMMENTARY hide
3.6.1.7
-
RECOMMENDED NAME
GeneOntology No.
acylphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate fermentation
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Aminobenzoate degradation
-
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Microbial metabolism in diverse environments
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Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
acylphosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9012-34-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
gene yflL
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-
Manually annotated by BRENDA team
small amounts
-
-
Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the disordered active site is converted to an ordered state upon ligand binding. Only one main conformation could bind ligand, and the relative population of these states is modulated by ligand concentration, pH-dependent conformations, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
1,3-bisphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
acylphosphate + H2O
a carboxylate + phosphate
show the reaction diagram
-
-
-
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
ATP + H2O
?
show the reaction diagram
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
benzoylphosphate + H2O
benzoate + phosphate
show the reaction diagram
beta-aspartyl phosphate + H2O
aspartate + phosphate
show the reaction diagram
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
diphosphate + H2O
2 phosphate
show the reaction diagram
DNA + H2O
?
show the reaction diagram
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
nucleic acids + H2O
?
show the reaction diagram
nucleoside diphosphate + H2O
nucleoside phosphate + phosphate
show the reaction diagram
-
-
-
?
nucleoside triphosphate + H2O
nucleoside diphosphate + phosphate
show the reaction diagram
-
-
-
?
p-nitrobenzoyl phosphate + H2O
p-nitrobenzoate + phosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
phosphocreatine + H2O
?
show the reaction diagram
poly (rA) + H2O
?
show the reaction diagram
RNA + H2O
?
show the reaction diagram
succinoyl phosphate + H2O
succinate + phosphate
show the reaction diagram
succinyl phosphate + H2O
succinate + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
acylphosphate + H2O
a carboxylate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Divalent cations
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nucleolytic activity, depends on
KCl
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brain enzyme, 15 mM: activation, substrate: Tris salt of acetyl phosphate
Mn2+
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DNAase activity, able to completely substitute Mg2+, required for nucleolytic activity
Zn2+
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DNAase activity, activation of nucleolytic activity, less effective compared with Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-diphosphoglycerate
3-phosphoglycerate
adrenaline
-
brain enzyme, at high concentrations, 12.5 mM: 65% inhibition
benzyl phosphate
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moderate competitive inhibition, Ki: 11 mM
Carbamoyl phosphate
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erythrocyte enzyme, competitive inhibition, Ki: 6.9 mM
ClO4-
-
-
Dinitrophenol
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brain enzyme, 0.25 mM: 50% inhibition
fructose 1,6-diphosphate
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noncompetitive inhibition, Ki: 3.2 mM
glucose
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glucose buffer, pH 11.2-12.0, progressive inactivation, complete after 1 h
guanidine
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brain enzyme, 5 M: 100% reversible inhibition, 95% of original activity is recovered upon lowering the guanidine concentration by dilution
iodoacetate
methyl phosphate
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moderate competitive inhibition, Ki: 3.5 mM
NaClO4
-
-
Orotic acid
p-chloromercuribenzoate
Pepsin
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brain enzyme, 2%: inactivation
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Phenylglyoxal
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6 mM: inhibition, inhibition partially removed by 35 mM phosphate
phosphate
phosphoenolpyruvate
Phosphorylated compounds
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-
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pyridoxal 5'-phosphate
Sodium thioglycollate
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muscle enzyme, 0.12 M, 3 h: 30% inhibition
sulfate
thyroxine
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brain enzyme, more inhibitory when preincubation is conducted at 16C than at 25C
trifluoroethanol
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in presence of 1525% (v/v) trifluoroethanol, enzyme forms aggregates able to bind specific dyes such as thioflavine T, Congo red, and 1-anilino-8-naphthalenesulfonic acid. The monomeric form adopted by the enzyme prior to aggregation under these conditions retains enzymatic activity, in addition, folding was remarkably faster than unfolding. Electron microscopy reveals the presence of small aggregates generally referred to as amyloid protofibrils
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
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activation
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inosinic acid
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brain enzyme, no effect up to 2.3 mM, 4.6 mM: 33% activation, further increase in concentration, does not produce further activation
papain
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brain enzyme, slight, 15%, activation
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Urea
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R97Q mutant, at low urea concentration, sharp activation with maximum, about 50% activation at 3 M urea, followed by rapid inactivation: 6 M: 80% inhibition, 8 M: 100% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 1.6
1,3-diphosphoglycerate
1.08 - 8.53
acetyl phosphate
0.12 - 2.1
benzoyl phosphate
0.8
benzoylphosphate
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-
0.0000034
Ca2+-ATPase phosphoenzyme
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erythrocyte isoenzyme, phosphorylated intermediate of erythrocyte membrane Ca2+-ATPase
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4.2 - 5.42
Carbamoyl phosphate
0.000069 - 0.000147
Na+/K+-ATPase phosphoenzyme
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000155 - 0.043
acetyl phosphate
93.5 - 10000
benzoyl phosphate
735
benzoylphosphate
Drosophila melanogaster
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-
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
779
benzoyl phosphate
Pyrococcus horikoshii
P84142
25 C, pH 5.3
1406
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
benzyl phosphate
-
moderate competitive inhibition
6.9
Carbamoyl phosphate
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erythrocyte enzyme, competitive inhibition
0.25
Dinitrophenol
-
brain enzyme
3.2
fructose 1,6-diphosphate
-
noncompetitive inhibition
3.5
methyl phosphate
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moderate competitive inhibition
1.78 - 1.94
phosphate
2700
Urea
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
substrate carbamoyl phosphate, muscle isoenzyme
12
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erythrocyte
22
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substrate carbamoyl phosphate, erythrocyte isoenzyme
33
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substrate acetyl phosphate, muscle isoenzyme
35
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substrate acetyl phosphate, erythrocyte isoenzyme
600
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heart
1250
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brain
1570
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substrate 1,3-diphosphoglycerate, muscle enzyme
2500
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DELTA6 deletion mutant
2638
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brain
3000 - 3200
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muscle
3281
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skeletal muscle, erythrocyte type enzyme
3300
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GP2
3700
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muscle enzyme
3744
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brain, muscle enzyme
3800
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Ho1
3900
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Ho1
4300
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C21A
4500
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muscular isoenzyme
4700
-
R97Q
5000
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muscular isoenzyme, recombinant, expressed as fusion protein with glutathione S-transferase
5900
-
C21S
6000
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Ch1, substrate benzoyl phosphate, 25C
6800
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erythrocyte form isoenzyme
6900
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substrate 1,3-diphosphoglycerate, erythrocyte enzyme
7160
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skeletal muscle, substrate benzoyl phosphate, 25C
9000
-
erythrocyte isoenzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7 - 4.4
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R97Q
4.5 - 5.5
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C21A
4.7 - 5.6
4.7 - 5.9
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DELTA6 deletion mutant
4.7 - 5.7
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0.1 M acetate buffer
4.8 - 5.8
5 - 6
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-
5 - 5.9
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Y98Q
5.2
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erythrocyte isoenzyme
5.4 - 5.6
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heart enzyme, substrate: acetyl phosphate
7.4 - 7.6
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brain, substrate: acetyl phosphate
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 12
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-
3.5 - 6.5
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pH range of maximum catalytic activity
4 - 5.8
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the activity drops sharply below pH 5.3, the enzyme is inactive above pH 5.8 and below pH 4.0. The structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH below pH 5.8
4.5 - 6.5
-
Mg2+ dependent ribonucleolytic activity
5 - 6.8
7
-
Mg2+ dependent ribonucleolytic and deoxyribonucleolytic activity: no activity above pH 7.0
additional information
-
erythrocyte isoenzyme, retains activity over a broad range of pH values
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
turnover number increases 4fold by an increase of temperature from 25 to 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
erythrocyte isoenzyme
Manually annotated by BRENDA team
additional information