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
3.6.1.7
-
RECOMMENDED NAME
GeneOntology No.
acylphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
reaction mechanism
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
reaction mechanism
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
reaction mechanism
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
thermodynamic data
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
thermodynamic data
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
thermodynamic data
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
catalytic mechanism
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
catalytic mechanism
-
an acylphosphate + H2O = a carboxylate + phosphate
show the reaction diagram
thermodynamic analysis, studies and data
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate fermentation
-
-
Aminobenzoate degradation
-
-
Microbial metabolism in diverse environments
-
-
Pyruvate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
acylphosphate phosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,3-diphosphoglycerate phosphatase
-
-
-
-
acetic phosphatase
-
-
-
-
acetyl phosphatase
-
-
-
-
acetylphosphatase
-
-
-
-
ACP
-
-
-
-
ACP
Pyrococcus horikoshii OT-3
-
;
-
acyl phosphatase
-
-
-
-
acyl phosphate phosphohydrolase
-
-
-
-
Acylphosphatase, erythrocyte isozyme
-
-
-
-
Acylphosphatase, erythrocyte/testis isozyme
-
-
-
-
Acylphosphate phosphohydrolase
-
-
-
-
acylphosphate phosphomonohydrolase
-
-
-
-
carbamoylphosphate phosphatase
-
-
-
-
carbamyl phosphate phosphatase
-
-
-
-
Ch1
-
Ch1 and Ch2 are different genetically specified isozymes; multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters
Ch1
-
multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters
Ch2
-
Ch1 and Ch2 are different genetically specified isozymes; multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters
Ch2
-
multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters
GP 1-3
-
multiple forms of guinea pig acylphosphatase
GP1
-
multiple forms of guinea pig acylphosphatase, major form
GP2
-
multiple forms of guinea pig acylphosphatase
GP3
-
multiple forms of guinea pig acylphosphatase
Ho 1-3
-
multiple forms of horse acylphosphatase
Ho1
-
multiple forms of horse acylphosphatase
Ho2
-
multiple forms of horse acylphosphatase
Ho3
-
multiple forms of horse acylphosphatase
human common-type acylphosphatase
-
-
Isozyme CH1
-
-
-
-
Isozyme CH2
-
-
-
-
native acylphosphatase
-
-
phosphatase, acyl
-
-
-
-
SSO0887
Q97ZL0
locus name
SSO0887
Q97ZL0
locus name
-
T1
-
multiple forms of turkey acylphosphatase
TT0497
Q5SKS6
-
Isozyme TU1
-
-
-
-
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues
additional information
-
two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues; two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
each individual of mammals and aves contains two types of acylphosphatase: 1. the muscle-type enzyme, which is localized mainly in skeletal muscle, 2. the common-type enzyme, which is widely distributed in the body, i.e., in skeletal muscle, erythrocyte, brain, heart, liver, kidney, and spleen
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues
additional information
-
two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues; two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues
additional information
-
two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues; two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
additional information
-
two isoenzymes: 1. skeletal muscle type, is present in skeletal muscle, heart, brain, liver, and in minor amounts in other tissues, 2. erythrocyte type, from red cells. The two isoenzymes clearly originated from a common ancestral gene, because about 56% of their amino acid positions in sequence are homologous
additional information
-
two isoenzymes in all tissues, organs, and cell types checked: 1. muscular isoenzyme, IM, and 2. erythrocyte isoenzyme, IE, on the basis of the cell-type in which they are mostly represented and from which they are purified for the first time
CAS REGISTRY NUMBER
COMMENTARY
9012-34-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene yflL
-
-
Manually annotated by BRENDA team
bovine; common type, CT, isoenzyme
-
-
Manually annotated by BRENDA team
bovine; ox
-
-
Manually annotated by BRENDA team
bovine; two isoenzymatic forms: one prevalent in skeletal and cardiac muscle, the other in red blood cells
-
-
Manually annotated by BRENDA team
bovine; two isoenzymes: muscular isoenzyme, IM, and erythrocyte isoenzyme, IE
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
guinea pig; three molecular forms: GP1, GP2 and GP3
-
-
Manually annotated by BRENDA team
small amounts
-
-
Manually annotated by BRENDA team
multiple molecular forms: Ho1, Ho2 and Ho3
-
-
Manually annotated by BRENDA team
Ch1 and Ch2 are genetically specified isozymes; two different isozymes: Ch1 and Ch2
-
-
Manually annotated by BRENDA team
two different isozymes: Ch1 and Ch2
-
-
Manually annotated by BRENDA team
C21S mutant; human
-
-
Manually annotated by BRENDA team
human; recombinant and mutants, R23Q mutant
-
-
Manually annotated by BRENDA team
human; several mutants, wild-type, DELTA6 deletion mutant: lacking residues 1-6 at the N-terminus and mutated, R97Q and Y98Q, recombinant; two different isoenzymes: skeletal muscle and erythrocyte enzyme
-
-
Manually annotated by BRENDA team
human; two different isoenzymes: skeletal muscle and erythrocyte enzyme
-
-
Manually annotated by BRENDA team
human; two isoenzymatic forms: one prevalent in skeletal and cardiac muscle, the other in red blood cells
-
-
Manually annotated by BRENDA team
human; wild-type and Cys21 mutants: C21A and C21S
-
-
Manually annotated by BRENDA team
muscle type, MT, isoenzyme; turkey
-
-
Manually annotated by BRENDA team
turkey; two isoenzymes: muscular isoenzyme, IM, and erythrocyte isoenzyme, IE
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii DSM 12428
-
Uniprot
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
two isoenzymes: skeletal muscle type and erythrocyte type
-
-
Manually annotated by BRENDA team
two different isozymes in testis and skeletal muscle
-
-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
-
-
-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
-
-
-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
-
-
-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
phospho-aspartyl intermediate
-
-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
acylphosphate bond in phosphorylated intermediate
-
-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
erythrocyte type enzyme, acylphosphorylated intermediates from human erythrocyte membrane
-
-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
show the reaction diagram
-
acylphosphorylated intermediates of Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum and heart sarcolemma
-
-
?
1,3-bisphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
P84142
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
-
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
P84142
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
erythrocyte isoenzyme shows hydrolytic activity on acyl phosphates with higher affinity than the muscle enzyme
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
ATP + H2O
?
show the reaction diagram
-
muscle enzyme, very low activity
-
-
?
ATP + H2O
?
show the reaction diagram
-
liver enzyme, no activity
-
-
-
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428
P84142
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
?
benzoylphosphate + 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
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
show the reaction diagram
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
show the reaction diagram
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
show the reaction diagram
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
-
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
P84142
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
erythrocyte enzyme: not a substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
muscle enzyme, poor substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
acylphosphatase could have a function of controlling the intracellular levels of carbamoylphosphate by preventing the accumulation of this compound mainly in those tissues lacking the urea cycle enzymes. It could avoid the carbamylation of many proteins which results in modifications, inhibition of their functional properties
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
role in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
liver enzyme, carbamoyl phosphate can reach high concentrations in liver and its level may be partly controlled by acyl phosphatase
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
muscle enzyme, very low activity
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
liver enzyme, no activity
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
erythrocyte enzyme, inorganic diphosphate: not a substrate
-
-
-
DNA + H2O
?
show the reaction diagram
-
muscle type and common type hydrolyze double stranded DNA, high molecular weight human genomic DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
DNAase activity, nucleolytic activity, exonucleolytic and endonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
-
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
-
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
mechanism
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
sarcolemma Na+,K+-ATPase phosphorylated intermediate
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
acylphosphatase can actively hydrolyze Na+/K+-ATPase phosphoenzyme, acylphosphatase produces a modification in the stoichiometry of the ATP driven cation transport by the Na+,K+ pump, from erythrocyte membrane, acylphosphatase significantly enhances the rate of strophantidine-sensitive ATP hydrolysis, it uncouples erythrocyte membrane N+,K+ pump
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
acylphosphatase significantly enhances the rate of strophantidine-sensitive ATP hydrolysis, it uncouples erythrocyte membrane N+,K+ pump, acylphosphatase hydrolyzes phosphoenzyme intermediate of heart sarcolemma Na+,K+-ATPase, acylphosphatase increases the rate of Na+,K+-dependent ATP hydrolysis, acylphosphatase significantly stimulates the rate of ATP driven Na+ transport into sarcolemma vesicles: accelerated hydrolysis of the phosphoenzyme may result in an enhanced activity of heart sarcolemma Na+,K+ pump, suggesting a potential role of acylphosphatase in the control of this active transport system
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
acylphosphatase markedly affects the functional properties of Na+,K+ pump, notably the rate of ATP hydrolysis and of cation, Na+,Rb+, transport, acylphosphorylated phosphoenzyme intermediate, enzyme has a high affinity for this substrate
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
show the reaction diagram
-
acylphosphorylated phosphoenzyme intermediate, enzyme has a high affinity for this substrate
-
-
?
nucleic acids + H2O
?
show the reaction diagram
-
nucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
nucleoside diphosphate + H2O
nucleoside phosphate + phosphate
show the reaction diagram
P84142
-
-
-
?
nucleoside triphosphate + H2O
nucleoside diphosphate + phosphate
show the reaction diagram
P84142
-
-
-
?
p-nitrobenzoyl phosphate + H2O
p-nitrobenzoate + 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
-
liver enzyme, no activity at pH 5.3 and 10.4
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
erythrocyte enzyme, not a substrate
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
muscle enzyme, very low activity at pH 5.3, no activity at pH 10.4
-
-
?
phosphocreatine + H2O
?
show the reaction diagram
-
muscle enzyme, very low activity
-
-
?
phosphocreatine + H2O
?
show the reaction diagram
-
liver enzyme, no activity
-
-
-
poly (rA) + H2O
?
show the reaction diagram
-
ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
RNA + H2O
?
show the reaction diagram
-
RNAase activity, ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
RNA + H2O
?
show the reaction diagram
-
Mg2+ dependent activity
-
-
?
succinoyl phosphate + H2O
succinate + phosphate
show the reaction diagram
-
-
-
-
?
succinoyl phosphate + H2O
succinate + phosphate
show the reaction diagram
-
-
-
-
?
succinoyl phosphate + H2O
succinate + phosphate
show the reaction diagram
-
-
-
-
?
succinyl phosphate + H2O
succinate + phosphate
show the reaction diagram
-
-
-
-
?
succinyl phosphate + H2O
succinate + phosphate
show the reaction diagram
P84142
-
-
-
?
DNA + H2O
?
show the reaction diagram
-
endonucleolytic activity on plasmid DNA, pRcCMV plasmid DNA, closed circular plasmid DNA, exonucleolytic activity on linear plasmid DNA
-
-
?
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
-
-
additional information
?
-
-
no activity with 3-phosphoglycerate, phosphocreatine, DL-3-glycerophosphate, fructose 1,6-diphosphate, glucose 6-phosphate, fructose 6-phosphate, phosphoenolpyruvate, ATP, ADP, AMP, cyclic-AMP, 6-phosphogluconate phosphoserine
-
-
-
additional information
?
-
-
hydrolyzes phosphorylated intermediate formed during activity of membrane pump ATPase
-
-
-
additional information
?
-
-
acetyl-AMP: not a substrate
-
-
-
additional information
?
-
-
hydrolyzes the beta-aspartylphosphate formed during the action of membrane pumps
-
-
-
additional information
?
-
-
hydrolyzes specific only acylphosphates
-
-
-
additional information
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
-
additional information
?
-
-
phosphorylated intermediates of (Ca2+ + Mg2+)-ATPase and phosphorylated peptides obtained by pepsin digestion of labeled phosphorylated microsomes are completely hydrolyzed by acylphosphatase
-
-
-
additional information
?
-
-
nucleolytic, ribonucleolytic and deoxyribonucleolytic, activity, exonucleolytic and endonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
-
additional information
?
-
-
liver enzyme and muscle enzyme, no activity with acetyl-AMP, phosphoenolpyruvate and phosvitin
-
-
-
additional information
?
-
-
specific phosphomonohydrolase activity
-
-
-
additional information
?
-
-
specific phosphomonohydrolase activity
-
-
-
additional information
?
-
-
specific phosphomonohydrolase activity
-
-
-
additional information
?
-
-
no activity with phosphoenolpyruvate and phosvitin
-
-
-
additional information
?
-
-
relative hydrolysis rates, carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate
-
-
-
additional information
?
-
-
possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate
-
-
-
additional information
?
-
-
role of acylphosphatase in pathologic situations
-
-
-
additional information
?
-
-
possible regulatory role of the enzyme in ion transport systems, proceeding via the formation of a phosphorylated protein intermediate with an acylphosphate bond
-
-
-
additional information
?
-
-
possible acyphosphatase involvement in the regulation of ion transport, and of calcium uptake in sarcoplasmic reticulum
-
-
-
additional information
?
-
-
hydrolytic activity by this enzyme on the phosphorylated intermediate is possible involved in Ca2+ transport in sarcoplasmic reticulum
-
-
-
additional information
?
-
-
nucleolytic activity of muscle and common type isoform acylphosphatase on RNA and DNA is possible physiological activity of these isoenzymes in the cell
-
-
-
additional information
?
-
-
since acylphosphatase hydrolyzes the high-energy phosphorylated compounds its action is probably involved in the regulation of cell energy metabolism
-
-
-
additional information
?
-
-
possible role of acylphosphatase in cell differentiation
-
-
-
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
-
additional information
?
-
-
enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine
-
-
-
additional information
?
-
-
enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine
-
-
-
additional information
?
-
-
acylphosphatase is active as a nuclease at pH ranging from 5.5 to 6.8 suggests that enzymes could play some role in apoptotic mechanisms
-
-
-
additional information
?
-
-
enzyme could control acylation and carbamylation of proteins by regulation the levels of reactive acyl and carbamoyl phosphates
-
-
-
additional information
?
-
-
acylphosphatase increases the rate of Na+,K+-dependent ATP hydrolysis, acylphosphatase significantly stimulates the rate of ATP driven Na+ transport into sarcolemma vesicles: accelerrated hydrolysis of the phosphoenzyme may result in an enhanced activity of heart sarcolemma Na+,K+ pump, suggesting a potential role of acylphosphatase in the control of this active transport system
-
-
-
additional information
?
-
-
acylphosphatase increases the rate of Na+,K+-dependent ATP hydrolysis, acylphosphatase significantly stimulates the rate of ATP driven Na+ transport into sarcolemma vesicles: accelerrated hydrolysis of the phosphoenzyme may result in an enhanced activity of heart sarcolemma Na+,K+ pump, suggesting a potential role of acylphosphatase in the control of this active transport system
-
-
-
additional information
?
-
-
possible role in regulating the glycolytic pathway, ureogenesis and pyrimidine biosynthesis
-
-
-
additional information
?
-
-
possible physiological role for acylphosphatase activity may be regulation of metabolic pathways involving 1,3-diphosphoglycerate and carbamoyl phosphate, e.g. glycolytic pathway and pyrimidine biosynthesis, by its ability to hydrolyze these substrates
-
-
-
additional information
?
-
-
possible regulatory role of this enzyme in vivo on the calcium transport process by sarcoplasmic reticulum
-
-
-
additional information
?
-
-
acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates
-
-
-
additional information
?
-
-
enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and production of ribonucleotides
-
-
-
additional information
?
-
-
the partially folded ensemble of AcP displays enzymatic activity, but the early enzymatic activity of AcP is not contributed by the unfolded or native states
-
-
-
additional information
?
-
-
acylphosphatase, a small enzyme that catalyzes the hydrolysis of acylphosphates and participates in ion transport across biological membranes, is involved in genetic incompatibilities leading to male sterility in hybrids between Drosophila simulans and Drosophila mauritiana. There is a strong association between Acyp alleles as genotype and the sterility/fertility pattern as phenotype, as well as between the phenotype, the genotype and its transcriptional activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
show the reaction diagram
-
1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
acylphosphatase could have a function of controlling the intracellular levels of carbamoylphosphate by preventing the accumulation of this compound mainly in those tissues lacking the urea cycle enzymes. It could avoid the carbamylation of many proteins which results in modifications, inhibition of their functional properties
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
role in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
liver enzyme, carbamoyl phosphate can reach high concentrations in liver and its level may be partly controlled by acyl phosphatase
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
show the reaction diagram
-
possible physiological substrate
-
-
?
additional information
?
-
-
carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate
-
-
-
additional information
?
-
-
possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate
-
-
-
additional information
?
-
-
role of acylphosphatase in pathologic situations
-
-
-
additional information
?
-
-
possible regulatory role of the enzyme in ion transport systems, proceeding via the formation of a phosphorylated protein intermediate with an acylphosphate bond
-
-
-
additional information
?
-
-
possible acyphosphatase involvement in the regulation of ion transport, and of calcium uptake in sarcoplasmic reticulum
-
-
-
additional information
?
-
-
hydrolytic activity by this enzyme on the phosphorylated intermediate is possible involved in Ca2+ transport in sarcoplasmic reticulum
-
-
-
additional information
?
-
-
nucleolytic activity of muscle and common type isoform acylphosphatase on RNA and DNA is possible physiological activity of these isoenzymes in the cell
-
-
-
additional information
?
-
-
since acylphosphatase hydrolyzes the high-energy phosphorylated compounds its action is probably involved in the regulation of cell energy metabolism
-
-
-
additional information
?
-
-
possible role of acylphosphatase in cell differentiation
-
-
-
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
-
additional information
?
-
-
enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine
-
-
-
additional information
?
-
-
enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine
-
-
-
additional information
?
-
-
acylphosphatase is active as a nuclease at pH ranging from 5.5 to 6.8 suggests that enzymes could play some role in apoptotic mechanisms
-
-
-
additional information
?
-
-
enzyme could control acylation and carbamylation of proteins by regulation the levels of reactive acyl and carbamoyl phosphates
-
-
-
additional information
?
-
-
acylphosphatase increases the rate of Na+,K+-dependent ATP hydrolysis, acylphosphatase significantly stimulates the rate of ATP driven Na+ transport into sarcolemma vesicles: accelerrated hydrolysis of the phosphoenzyme may result in an enhanced activity of heart sarcolemma Na+,K+ pump, suggesting a potential role of acylphosphatase in the control of this active transport system
-
-
-
additional information
?
-
-
acylphosphatase increases the rate of Na+,K+-dependent ATP hydrolysis, acylphosphatase significantly stimulates the rate of ATP driven Na+ transport into sarcolemma vesicles: accelerrated hydrolysis of the phosphoenzyme may result in an enhanced activity of heart sarcolemma Na+,K+ pump, suggesting a potential role of acylphosphatase in the control of this active transport system
-
-
-
additional information
?
-
-
possible role in regulating the glycolytic pathway, ureogenesis and pyrimidine biosynthesis
-
-
-
additional information
?
-
-
possible physiological role for acylphosphatase activity may be regulation of metabolic pathways involving 1,3-diphosphoglycerate and carbamoyl phosphate, e.g. glycolytic pathway and pyrimidine biosynthesis, by its ability to hydrolyze these substrates
-
-
-
additional information
?
-
-
possible regulatory role of this enzyme in vivo on the calcium transport process by sarcoplasmic reticulum
-
-
-
additional information
?
-
-
acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates
-
-
-
additional information
?
-
-
enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and production of ribonucleotides
-
-
-
additional information
?
-
-
acylphosphatase, a small enzyme that catalyzes the hydrolysis of acylphosphates and participates in ion transport across biological membranes, is involved in genetic incompatibilities leading to male sterility in hybrids between Drosophila simulans and Drosophila mauritiana. There is a strong association between Acyp alleles as genotype and the sterility/fertility pattern as phenotype, as well as between the phenotype, the genotype and its transcriptional activity
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Divalent cations
-
nucleolytic activity, depends on
KCl
-
brain enzyme, 15 mM: activation, substrate: Tris salt of acetyl phosphate
Mg2+
-
Mg2+ dependent deoxyribonuclease and ribonuclease activity, required for nucleolytic activity
MgCl2
-
brain enzyme, 5 mM: activation, substrate: Tris salt of acetyl phosphate
MgCl2
-
-
MgCl2
-
Mg2+ dependent deoxyribonuclease and ribonuclease activity, required for activity
Zn2+
-
DNAase activity, activation of nucleolytic activity, less effective compared with Mg2+
Mn2+
-
DNAase activity, able to completely substitute Mg2+, required for nucleolytic activity
additional information
-
muscle enzyme, no metal ion requirement
additional information
-
Ca2+ has no activating effect on the nucleolytic activity of acylphosphatase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-diphosphoglycerate
-
competitive inhibition, Ki erythrocyte enzyme: 0.41 mM, Ki skeletal muscle enzyme: 3.74 mM
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
heart enzyme, 2 mM: 12% inhibition, substrate: 1,3-diphosphoglycerate
2,3-diphosphoglycerate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 0.24 mM
3-phosphoglycerate
-
-
3-phosphoglycerate
-
heart enzyme, 5 mM: 8% inhibition, substrate: 1,3-diphosphoglycerate
3-phosphoglycerate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 1.70 mM
adrenaline
-
brain enzyme, at high concentrations, 12.5 mM: 65% inhibition
ATP
-
noncompetitive inhibition, Ki: 0.57 mM
ATP
-
erythrocyte enzyme, competitive inhibition, Ki: 4.4 mM
ATP
-
heart enzyme, 5 mM: 11% inhibition, substrate: 1,3-diphosphoglycerate
benzyl phosphate
-
moderate competitive inhibition, Ki: 11 mM
Carbamoyl phosphate
-
erythrocyte enzyme, competitive inhibition, Ki: 6.9 mM
Cl-
-
competitive inhibition, Ki erythrocyte enzyme: 51.70 mM, Ki skeletal muscle enzyme: 42.10 mM
Cl-
-
competitive inhibition; GP1, Ki: 29.1 mM
Cl-
-
competitive inhibition; Ho1, Ki: 40.0 mM
Cl-
-
competitive inhibition; T1, Ki: 40.0 mM
Cl-
-
competitive inhibition; Ho1, Ki: 40.0 mM; Ho2, Ki: 50.0 mM; Ho3, Ki: 40.0 mM
Cl-
-
muscular isoenzyme, Ki: 40.0 mM, erythrocyte isoenzyme, Ki: 31.0 mM
Cl-
-
erythrocyte isoenzyme, competitive inhibition, Ki: 18.0 mM
ClO4-
-
-
Dinitrophenol
-
brain enzyme, 0.25 mM: 50% inhibition
EDTA
-
inhibition of ribonucleolytic and deoxyribonucleolytic activity of acylphosphatase
EDTA
-
1 mM: 100% inhibition of endonucleolytic activity of both isoforms; inhibition of ribonucleolytic and deoxyribonucleolytic activity of acylphosphatase
EDTA
-
inhibition of ribonucleolytic and deoxyribonucleolytic activity of acylphosphatase
fructose 1,6-diphosphate
-
noncompetitive inhibition, Ki: 3.2 mM
glucose
-
glucose buffer, pH 11.2-12.0, progressive inactivation, complete after 1 h
guanidine
-
brain enzyme, 5 M: 100% reversible inhibition, 95% of original activity is recovered upon lowering the guanidine concentration by dilution
Hg2+
-
muscle enzyme, 0.1 mM, 30 min: 30% inhibition
Hg2+
-
inhibition partially reactivated in the absence of Hg2+, mutant enzymes regained 65-85% of original activity, wild-type enzyme regained less than 50%
iodoacetate
-
brain enzyme, 4 mM: no inhibition
iodoacetate
-
heart enzyme, 10 mM: very low, less than 5%, inhibition
NaClO4
-
-
Orotic acid
-
liver enzyme, noncompetitive inhibition
p-chloromercuribenzoate
-
heart enzyme, 1 mM: very low, less than 5%, inhibition
p-chloromercuribenzoate
-
muscle enzyme, 1 mM: no inhibition
Pepsin
-
brain enzyme, 2%: inactivation
-
Phenylglyoxal
-
6 mM: inhibition, inhibition partially removed by 35 mM phosphate
phosphate
-
competitive inhibition, Ki erythrocyte enzyme: 0.30 mM, Ki skeletal muscle enzyme: 2.72 mM
phosphate
-
competitive inhibition; GP1, Ki: 1.73 mM
phosphate
-
competitive inhibition; Ho1, Ki: 1.7 mM
phosphate
-
competitive inhibition; T1, Ki: 2.8 mM
phosphate
-
competitive inhibition; Ho1, Ki: 1.7 mM; Ho2, Ki: 2.3 mM; Ho3, Ki: 1.6 mM
phosphate
-
phosphate: high competitive inhibition, mechanism of inhibition
phosphate
-
eryhrocyte enzyme, competitive inhibition, Ki: 3.4 mM
phosphate
-
heart enzyme, 5 mM: 37% inhibition, substrate: 1,3-diphosphoglycerate; heart enzyme, competitive inhibition
phosphate
-
strong inhibition
phosphate
-
phosphate, competitive inhibition
phosphate
-
-
phosphate
-
brain enzyme 20 mM: 50-60% inhibition, 40 mM: 70-80% inhibition
phosphate
-
muscular isoenzyme, Ki: 2.8 mM, erythrocyte isoenzyme, Ki: 0.68 mM
phosphate
-
competitive inhibition, Ki: 3 mM
phosphate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 0.41 mM
phosphate
-
phosphate: competitive inhibition, muscular enzyme, native Ki: 2.29 mM, recombinant, expressed as fusion protein with glutathione S-transferase, Ki: 3.05
phosphate
-
phosphate, competitive inhibition, muscular isoenzyme, wild-type, Ki: 0.98 mM, R97Q Ki: 1.79 mM, Y98Q Ki: 1.17 mM, DELTA6 deletion mutant Ki: 1.19 mM
phosphate
-
phosphate, competitive inhibition, muscular isoenzyme, wild-type, Ki: 0.9 mM, C21A Ki: 0.9 mM, C21S Ki: 0.7 mM
phosphate
-
phosphate: inhibition of nucleolytic activity
phosphate
-
phosphate, 1 mM: competitive inhibition of DNAase activity of muscle and common type acylphosphatase, no inhibition of ribonucleolytic activity; phosphate: inhibition of nucleolytic activity
phosphate
-
phosphate: inhibition of nucleolytic activity
phosphate
-
competitive inhibition; phosphate: competitive inhibition, addition of very low concentrations of phosphate causes a strong stabilisation of AcP against chemical denaturation
phosphate
-
-
phosphate
-
competitive inhibition
phosphate
-
competitive inhibition; phosphate: competitive inhibition, muscular enzyme, native Ki: 2.29 mM, recombinant, expressed as fusion protein with glutathione S-transferase, Ki: 3.05
phosphate
-
competitive inhibition
phosphate
-
competitive
phosphoenolpyruvate
-
competitive inhibition, Ki erythrocyte enzyme: 0.38 mM, Ki skeletal muscle enzyme: 2.23 mM
phosphoenolpyruvate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 0.21 mM
Phosphorylated compounds
-
-
-
pyridoxal 5'-phosphate
-
muscle enzyme, pH-dependent competitive, reversible inhibition, Ki: 0.32 mM
pyridoxal 5'-phosphate
-
at pH 7.6, inhibition is reversed by addition of lysine or dilution; mechanism of inhibition; muscle enzyme, pH-dependent competitive, reversible inhibition, Ki: 0.32 mM; muscle enzyme, pH-dependent inhibition, maximum inhibition at about pH 7.6
Sodium thioglycollate
-
muscle enzyme, 0.12 M, 3 h: 30% inhibition
sulfate
-
Si, heart enzyme, competitive inhibition
sulfate
-
-
thyroxine
-
brain enzyme, more inhibitory when preincubation is conducted at 16C than at 25C
trifluoroethanol
-
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
Urea
-
8 M: 100% inhibition
Urea
-
brain enzyme, 5 M: 100% reversible inhibition, 95% of original activity is recovered upon lowering the urea concentration by dilution
Urea
-
8 M: 100% inhibition; 8 M: 100% reversibel inhibition, 60% reactivation in the absence of urea
Urea
-
2.7 M: 50% inhibition, 8M: 100% inhibition, 90% of its original activity regained in the absence of urea
Urea
-
reversibel inhibition, wild-type and DELTA6 deletion mutant, 4.2 M: 50% inhibition, Y98Q, 3.8 M: 50% inhibition, R97Q, at low urea concentration sharp activation, maximum activation at 3 M: 50% activation, followed by rapid inactivation, 6 M: 80% inhibition, 8 M 100% inhibition; wild-type and mutants, urea inactivation studies
Urea
-
8 M: 100% inhibition; wild-type and mutants, urea inactivation studies
methyl phosphate
-
moderate competitive inhibition, Ki: 3.5 mM
additional information
-
brain enzyme, no inhibition by 0.04 mM HgCl2 and 4 mM iodoacetate
-
additional information
-
no inhibition by adenosine monophosphate, phosphoethanolamine and alpha-glycerophosphate
-
additional information
-
-
-
additional information
-
heart enzyme, no inhibition by 2.0 mM HgCl2
-
additional information
-
muscle enzyme, no inhibition by pyridoxamine 5'-phosphate and pyridoxine 5'-phosphate
-
additional information
-
no inhibition by carboxylic acid, acetic acid, acetate, Na+
-
additional information
-
brain enzyme, no inhibition by caffeine, inosinic acid, 0.5% trypsin and 1% papain
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Bovine serum albumin
-
activation
-
inosinic acid
-
brain enzyme, no effect up to 2.3 mM, 4.6 mM: 33% activation, further increase in concentration, does not produce further activation
Papain
-
brain enzyme, slight, 15%, activation
-
Urea
-
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
LITERATURE
IMAGE
0.12
1,3-diphosphoglycerate
-
erythrocyte enzyme
0.55
1,3-diphosphoglycerate
-
erythrocyte enzyme
0.62
1,3-diphosphoglycerate
-
skeletal muscle enzyme
1.6
1,3-diphosphoglycerate
-
muscle
1.08
acetyl phosphate
-
GP1
2.9
acetyl phosphate
-
erythrocyte enzyme
4.23
acetyl phosphate
-
erythrocyte enzyme
6.2
acetyl phosphate
-
skeletal muscle enzyme
0.12
benzoyl phosphate
-
erythrocyte enzyme
0.12
benzoyl phosphate
P84142
25-45C, pH 5.3; at 25C and pH 5.3
0.14
benzoyl phosphate
-
brain, erythrocyte enzyme
0.15
benzoyl phosphate
-
erythrocyte enzyme
0.16
benzoyl phosphate
-
-
0.17
benzoyl phosphate
-
Ch2
0.18
benzoyl phosphate
-
erythrocyte isoenzyme
0.3
benzoyl phosphate
-
-
0.36
benzoyl phosphate
-
0.1 M acetate buffer, pH 5.3, 25C
0.39
benzoyl phosphate
-
Ch1 monomer
0.4
benzoyl phosphate
-
C21A
0.41
benzoyl phosphate
-
Y98Q
0.48
benzoyl phosphate
-
Ch1 dimer
0.5
benzoyl phosphate
-
wild-type, muscle
0.51
benzoyl phosphate
-
wild-type, muscle
0.55
benzoyl phosphate
-
DELTA6 deletion mutant
0.57
benzoyl phosphate
-
GP1
0.7
benzoyl phosphate
-
muscular isoenzyme
0.8
benzoyl phosphate
-
C21S
0.8
benzoyl phosphate
-
muscular isoenzyme
0.8
benzoyl phosphate
-
-
0.81
benzoyl phosphate
-
muscle enzyme
0.81
benzoyl phosphate
-
skeletal muscle enzyme
0.85
benzoyl phosphate
-
muscular enzyme recombinant, expressed as fusion protein with glutathione S-transferase
0.85
benzoyl phosphate
-
-
0.95
benzoyl phosphate
-
brain, muscular isoenzyme
1
benzoyl phosphate
-
T1
1
benzoyl phosphate
-
muscular isoenzyme
1.1
benzoyl phosphate
-
Ho3
1.14
benzoyl phosphate
-
R97Q
1.53
benzoyl phosphate
-
muscular enzyme
2
benzoyl phosphate
-
Ho1
2.1
benzoyl phosphate
-
Ho2
0.8
benzoylphosphate
-
-
0.0000034
Ca2+-ATPase phosphoenzyme
-
erythrocyte isoenzyme, phosphorylated intermediate of erythrocyte membrane Ca2+-ATPase
-
4.2
Carbamoyl phosphate
-
skeletal muscle enzyme
0.000069
Na+/K+-ATPase phosphoenzyme
-
cardiac muscle, phoshoenzyme intermediate of heart sarcolemma Na+,K+-ATPase
-
0.000069
Na+/K+-ATPase phosphoenzyme
-
-
-
0.000147
Na+/K+-ATPase phosphoenzyme
-
high affinity for this substrate
-
0.000147
Na+/K+-ATPase phosphoenzyme
-
-
-
5.42
Carbamoyl phosphate
-
erythrocyte enzyme
additional information
additional information
-
kinetic characterization, kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data; kinetic parameters of Ho1 and Ho3 are quite similar
-
additional information
additional information
-
kinetic characterization, kinetic data; kinetic data; kinetic studies
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic characterization, kinetic data; kinetic studies
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic characterization, kinetic data
-
additional information
additional information
-
thermodynamic and kinetic parameters
-
additional information
additional information
-
hydrodynamic parameters by dynamic light scattering, kinetics, wild-type and mutant enzymes, overview
-
additional information
additional information
P0AB65
kinetics and thermodynamics of wild-type and mutant enzymes,overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
93.5
benzoyl phosphate
P84142
25C, pH 5.3; at 25C and pH 5.3
117
benzoyl phosphate
-
-
191
benzoyl phosphate
P84142
30C, pH 5.3; at 30C and pH 5.3
198
benzoyl phosphate
-
0.1 M acetate buffer, pH 5.3, 25C
275
benzoyl phosphate
P84142
35C, pH 5.3; at 35C and pH 5.3
290
benzoyl phosphate
P84142
40C, pH 5.3; at 40C and pH 5.3
467
benzoyl phosphate
P84142
45C, pH 5.3; at 45C and pH 5.3
850
benzoyl phosphate
-
0.1 M acetate buffer, pH 5.3, 81C
10000
benzoyl phosphate
P84142
at 98C and pH 5.3, estimation by linear extrapolation
735
benzoylphosphate
-
-
additional information
additional information
P84142
experimentally, it is impossible to assay the enzyme activity of the enzyme directly at 98C because the uncatalyzed hydrolysis of the acyl-phosphate substrate is too fast at high temperatures to allow an accurate measurement of kinetic parameters. Instead, the kinetic parameters of the enzyme are measured at 25-45 C and the kcat value of the enzyme at 98 C is estimated by linear extrapolation of the Arrhenius plot. The estimated kcat value is 10000/s
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
779
benzoyl phosphate
P84142
25 C, pH 5.3
1406
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
benzyl phosphate
-
moderate competitive inhibition
6.9
Carbamoyl phosphate
-
erythrocyte enzyme, competitive inhibition
0.25
Dinitrophenol
-
brain enzyme
3.2
fructose 1,6-diphosphate
-
noncompetitive inhibition
3.5
methyl phosphate
-
moderate competitive inhibition
1.78
phosphate
-
0.1 M acetate buffer, pH 5.3, 25C
1.94
phosphate
-
-
2700
Urea
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
substrate carbamoyl phosphate, muscle isoenzyme
12
-
erythrocyte
22
-
substrate carbamoyl phosphate, erythrocyte isoenzyme
33
-
substrate acetyl phosphate, muscle isoenzyme
35
-
substrate acetyl phosphate, erythrocyte isoenzyme
600
-
heart
1250
-
brain
1570
-
substrate 1,3-diphosphoglycerate, muscle enzyme
2500
-
DELTA6 deletion mutant
2638
-
brain
3000 - 3200
-
muscle
3000
-
Ho2
3000
-
muscle
3281
-
skeletal muscle, erythrocyte type enzyme
3300
-
GP2
3500
-
GP3
3500
-
Ho3
3500
-
muscular isoenzyme
3500
-
muscular isoenzyme
3600
-
GP1
3600
-
Y98Q
3600
-
muscle isoenzyme
3650
-
heart, cardiac muscle
3650
-
-
3650
-
muscle enzyme
3700
-
muscle enzyme
3744
-
brain, muscle enzyme
3800
-
Ho1
3900
-
Ho1
4300
-
C21A
4500
-
muscular isoenzyme
4700
-
R97Q
5000
-
muscular isoenzyme, recombinant, expressed as fusion protein with glutathione S-transferase
5900
-
C21S
5960
-
Ch1
5960
-
muscle enzyme
6000
-
Ch1, substrate benzoyl phosphate, 25C
6800
-
erythrocyte form isoenzyme
6900
-
substrate 1,3-diphosphoglycerate, erythrocyte enzyme
7000
-
wild-type, muscle
7000
-
erythrocyte isoenzyme
7000
-
-
7160
-
skeletal muscle, substrate benzoyl phosphate, 25C
7200
-
skeletal muscle, substrate benzoyl phosphate, 25C
7200
-
-
7500
-
erythrocyte isoenzyme, substrate benzoyl phosphate, 25C
7500
-
muscle enzyme, SH form
8500
-
Ch2
8500
-
muscle, erythrocyte isoenzyme
9000
-
erythrocyte isoenzyme
10800
-
testis, substrate benzoyl phosphate, 25C
10800
-
testis, erythrocyte enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.7 - 4.4
-
R97Q
4.5 - 5.5
-
C21A
4.7 - 5.6
-
muscular enzyme
4.7 - 5.6
-
C21S
4.7 - 5.7
-
0.1 M acetate buffer
4.7 - 5.9
-
DELTA6 deletion mutant
4.8 - 5.8
-
muscular enzyme, recombinant, expressed as fusion protein with glutathione S-transferase
4.8 - 5.8
-
wild-type, muscle
4.8 - 5.8
-
-
5 - 5.9
-
Y98Q
5 - 6
-
-
5
-
dimer of Ch1, and Ch2
5
-
erythrocyte enzyme, substrate: acetyl phosphate
5.2
-
erythrocyte isoenzyme
5.3
-
assay at; skeletal muscle enzyme
5.3
-
assay at; monomer of Ch1
5.3
-
assay at
5.3
-
assay at; Ho1
5.3
-
assay at; T1
5.3
-
assay at; Ho1, Ho2 and Ho3
5.3
-
assay at; muscle and liver
5.3
-
muscular and erythrocyte isoenzyme
5.3
-
assay at; pH-optimum
5.3
-
assay at
5.3
-
skeletal muscle enzyme
5.3
P84142
; at 25C
5.3
-
substrate benzoylphosphate
5.4 - 5.6
-
heart enzyme, substrate: acetyl phosphate
5.4
-
erythrocyte, assay at
5.4
-
muscle, assay at
5.5
-
nucleolytic activity, assay at
5.5
-
erythrocyte enzyme
6
-
assay at
7.4 - 7.6
-
brain, substrate: acetyl phosphate
additional information
-
-
additional information
-
pI testis enzyme: 8.3, pI muscle enzyme: 10.6
additional information
-
muscle, pI: 11.4
additional information
-
-
additional information
-
erythrocyte enzyme is a basic protein; muscle, pI: 11.4
additional information
-
heart, pI: 7.25-7.3
additional information
-
muscle enzyme is very basic protein; muscle enzyme, pH analyses of reaction
additional information
-
muscle enzyme is very basic protein; muscle, pI: 11.4
additional information
-
erythrocyte enzyme is a basic protein
additional information
-
acidic pH-optimum
additional information
-
muscle enzyme is very basic protein
additional information
-
muscle, pI: 11.4
additional information
-
muscle, pI: 11.4
additional information
-
-
additional information
-
muscle, pI: 11.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 12
-
-
3.5 - 6.5
-
pH range of maximum catalytic activity
4 - 5.8
-
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
-
Mg2+ dependent deoxyribonuclease and ribonuclease activity
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
LITERATURE
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
27
-
assay at
27
-
assay at
37
-
erythrocyte, assay at
37
-
nucleolytic activity, assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
P84142
turnover number increases 4fold by an increase of temperature from 25 to 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
common-type enzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
erythrocyte isoenzyme
Manually annotated by BRENDA team
-
erythrocyte isoenzyme
Manually annotated by BRENDA team
-
common type enzyme
Manually annotated by BRENDA team
-
cardiac muscle
Manually annotated by BRENDA team
-
common-type enzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
small intestine, erythrocyte isoenzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
common-type enzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
common-type enzyme
Manually annotated by BRENDA team
-
erythrocyte isoenzyme very low
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
breast muscle
Manually annotated by BRENDA team
-
erythrocyte isoenzyme
Manually annotated by BRENDA team
-
erythrocyte isoenzyme very low in skeletal muscle
Manually annotated by BRENDA team
-
heart muscle
Manually annotated by BRENDA team
-
muscle-type and common-type enzyme
Manually annotated by BRENDA team
-
cardiac muscle
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
common-type enzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
erythrocyte isoenzyme very low
Manually annotated by BRENDA team
-
common type enzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
small amounts of muscular isoenzyme
Manually annotated by BRENDA team
-
erythrocyte isoenzyme
Manually annotated by BRENDA team
additional information
-
different distribution of each isoenzyme, erythrocyte and muscular enzyme, in different organs and tissues
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8300
-
liver, gel filtration
246781, 246784
8450 - 10300
-
muscle, low speed sedimentation equilibrium, Archibald method
246786
9400
-
muscle, low speed sedimentation equilibrium, Archibald method, and gel filtration
246781
9400
-
muscle, low speed sedimentation equilibrium, Archibald method
246786
9750
-
muscle, gel filtration
246786
10000
-
SDS-PAGE and ESI-MS
667089
10130
P84142
mass spectrometry
667658
10600
-
sedimentation equilibrium
246772
11000
-
PAGE and SDS-PAGE
246772
11000
-
SDS-PAGE
246790
11060
-
Ch2, calculated from amino acid sequence
246773
11060
-
calculated from amino acid sequence
246776
11100
-
skeletal muscle, sedimentation equilibrium
246777
11100
-
heart, gel filtration
246781
11120
-
muscle, calculated from amino acid composition
246772
11170
-
erythrocyte enzyme, calculated from amino acid sequence
246775
11300
-
calculated from sequence of cDNA
667099
11320
-
Ch1, calculated from amino acid sequence
246774
11360
-
muscle, calculated from amino acid sequence
246794
11370
-
muscle, calculated from amino acid sequence
246778, 246800
11780
-
electrospray mass spectrometry
655566
11900
-
Ch1, sedimentation equilibrium
246776
12000
-
Ch2, sedimentation equilibrium
246773, 246776
12000
-
GP1, SDS-PAGE
246778
12000
-
brain, gel filtration
246781
12000
-
-
246781
12100
-
Ho2, SDS-PAGE
246779
12600
-
Ho1, SDS-PAGE
246778, 246779
12750
-
erythrocyte isoenzyme; SDS-PAGE
246789
13200
-
brain, ultracentrifugation
246787
13400
-
T1, SDS-PAGE
246778
13400
-
muscular isoenzyme
246789
23500
-
sedimentation equilibrium
246785
24000
-
GP3, SDS-PAGE
246778
24200
-
Ho3, SDS-PAGE
246779
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
-
dimer
-
-
dimer
-
2 * 11000, skeletal muscle, SDS-PAGE
dimer
-
Ch1, 2 * 9400, SDS-PAGE
dimer
-
Ho3, 2 * 12000, S-S dimer, SDS-PAGE with 2-mercaptoethanol
dimer
P84142
2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds
monomer
-
-
monomer
-
-
monomer
-
erythrocyte isoenzyme, 1 * 12750, SDS-PAGE
monomer
-
monomeric alpha,beta protein
monomer
-
monomeric alpha,beta protein
monomer
-
1 * 11000, SDS-PAGE
monomer
-
1 * 11000, testis, SDS-PAGE
monomer
-
Ch2, 1 * 11400, SDS-PAGE
monomer
-
liver, 1 * 8300, SDS-PAGE
monomer
-
brain enzyme, 1 * 13200, ultracentrifugation
monomer
-
Ho1, 1 * 12600, SDS-PAGE
monomer
-
Ch1, 1 * 9400, SDS-PAGE
monomer
-
Ho2, 1 * 12100, SDS-PAGE
monomer
-
skeletal muscle, 1 * 9000, SDS-PAGE
monomer
P84142
1 * 10128, enzyme in solution, 1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
monomer
-
1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
monomer
Pyrococcus horikoshii DSM 12428
-
1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
-
additional information
-
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
-
study on folding process of enzyme and comparison with other acylphosphatases. An ensemble of partially folded or misfolded species form rapidly on the submillisecond time scale after initiation of folding. Enzyme folds a rate constant of about 5 per s at pH 5.5 and 37C
additional information
-
aggregation process: mechanism, structure and topology, conversion of these initial aggregates into amyloid-like protofibrils is an intra-molecular process in which the AcP molecules undergo conformational modifications, model for the assembly of Sso AcP into amyloid-like aggregates at a molecular level, several models of aggregation are excluded, overview
additional information
-
the enzyme has the ability to aggregate via the transient formation of oligomers in which the protein molecules retain native-like conformations, enzyme secondary and three-dimensional structure, topology, and comparison with acylphosphatases from other organisms, overview. beta-Structured oligomer formation proceeds via an alternative mechanism that is independent of the transient formation of native-like aggregates
additional information
-
The partially folded ensemble of AcP displays enzymatic activity
additional information
-
mutational analysis of aggregation and disaggregation of amyloid-like protofibrils of human muscle acylphosphatase, overview
additional information
P0AB65
structure determination and protein folding analysis of wild-type and mutant enzymes by far-UV and near-UV circular dichroism and dynamic light-scattering measurements, the protein folding of AcP is enhanced by disulfide bonds, overview
additional information
Q5SKS6
structure modelling, multiple conformations of the side chains of amino-acid residues
additional information
-
rapid oligomer formation of muscle acylphosphatase induced by heparan sulfate, aggregation at pH 5.5, 25C, monitoring by stopped-flow device coupled to turbidometry detection, modeling, overview. The oligomers show bet-sheet structure
additional information
-
the structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH below pH 5.8
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
erythrocyte isoenzyme, NH2-terminus is acetylated
no modification
-
-
no modification
-
Ch1 and Ch2: no sugar, no hexose, no hexosamine
side-chain modification
-
muscular isoenzyme, acetylated at the N-terminus
side-chain modification
-
skeletal muscle, acetylated at the NH2-terminus, Ac-Ala as the NH2-terminal residue
no modification
-
-
no modification
-
less than 0.2 mol glucose equivalent per mol enzyme, no hexosamine
no modification
-
amount of sugar is insignificant
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
common-type enzyme, resolution of 1.8 A
-
crystals belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8 A, c = 98.6 A, gamma = 120, refinement to 1.5 A resolution; vapour diffusion method
-
muscle enzyme, not suitable for X-ray diffraction
-
sitting drop vapour diffusion method using polyethylene glycol 4000 as precipitant
-
muscular isoenzyme; not suitable for X-ray diffraction
-
sitting drop vapour diffusion
-
sitting-drop vapour-diffusion method using sodium formate as precipitant at 16C. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 85.65 A, c = 75.51 A. The asymmetric unit contains two molecules of enzyme; sitting drop vapour diffusion method with sodium formate as precipitant
-
sitting-drop vapour-diffusion method with postasium/sodium tartrate as the precipitant at pH 5.5. The crystals belong to space group P3(2)21, with approximate unit-cell parameters a = b = 86.7 A, c = 75.4 A and two monomers in the asymmetric unit; sitting drop vapour diffusion method with potassium/sodium tartrate at pH 5.5
-
sitting-drop-vapor-diffusion method, 1.5 A crystal structure. The enzyme forms a dimer in the crystal structure via antiparallel association of strand 4; sitting-drop-vapor-diffusion with sodium formate as precipitant at pH 6.0
P84142
resolution to 1.27 and 1.9 A
-
sitting drop vapour diffusion, crystal structures of mutant enzymes V84D, Y86E and V84P are determined
-
vapour diffusion method
-
not suitable for X-ray diffraction; skeletal muscle enzyme
-
skeletal muscle enzyme
-
purified recombinant TT0497, 0.0005 ml of 2.9 mg/ml protein in 20 mM Tris-HCl pH 8.0, 0.2 M NaCl is mixed with 0.0005 ml of precipitant solution containing 27.5% w/v PEG 4000 and 0.1 M MES, pH 6.9, X-ray diffraction structure determination and analysis at 1.3 A resolution, structural refinement based on the Fourier method, modelling, overview
Q5SKS6
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1
-
stable in acid solutions up to pH 1
246783
1.5 - 2
-
heart enzyme, 100% activity retained
246781
1.5 - 8.2
-
brain enzyme, 24 h: no decrease of activity
246787
2.5 - 11
-
stable between, enzyme is in its native state between, outside this pH range, stability of enzyme collapses abruptly, most probably due to excess of positive or negative charges present at low and high pH
246799
3 - 5.4
-
stable 12 h , 37C
246785
3.5 - 6.5
-
highest conformational stability between
246799
5.5
-
maximum stability near pH 5.5
246799
9
-
-
246781
9
-
heart enzyme, 92% activity retained
246781
9
-
1 h, 2C: 30% loss of activity
246785
9.5
-
highest stability against urea at pH 9.5
246799
11.2 - 12
-
progressive inactivation, complete inactivation after 1 h
246783
additional information
-
brain enzyme is acid stable
246781
additional information
-
liver enzyme is acid stable
246781
additional information
-
-
246781
additional information
-
muscle enzyme, unusually stable to acid
246783
additional information
-
liver enzyme is acid stable
246784
additional information
-
stable at acidic and neutral pH, somewhat unstable at alkaline pH
246785
additional information
-
brain enzyme, stable over a wide pH range
246787
additional information
-
studies on conformational stability of muscle acylphosphatase
246799
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 100
P84142
At 25C, the free energy of unfolding, midpoint of transition, and m value were 54.4 kJ/mol, 4.99 M, and 10.9 kJ/mol/M, respectively. The melting temperature is about 111.5C. These data indicate that PhAcP is an extremely thermostable protein.
667658
37
-
90% loss of activity after 10 min at, pH range 5.3-7.4
246775
37
-
brain enzyme, purified and dialyzed enzyme, 20 min, 27% inactivation, undialyzed enzyme: no inactivation
246787
65
-
muscular isoenzyme, fully denatured protein. Thermal denaturation is reversibel
246794
70
-
erythrocyte enzyme, 5 min: 40% loss of activity
246781
80
-
brain enzyme, partially purified, 15 min, pH 1: 100% activity retained, pH 7: 80-90% activity retained
246787
85
-
heart enzyme, pH 2.0, 5 min, 95% activity retained
246781
90
-
no disruption of three-dimensional structure when incubated at 90C for 30min
670841
100
-
2 h: heat inactivation
246791
100
-
2 h: heat inactivation
246793
100
P84142
stable up to
667658
100
-
melting temperature
670844
112
P84142
melting temperature: 111.5C
667658
additional information
-
enzyme is thermostable
246781
additional information
-
-
246781
additional information
-
muscle and brain enzymes: stable at high temperatures
246781
additional information
-
muscle enzyme, unusually thermostable
246783
additional information
-
enzyme is thermostable
246784
additional information
-
enzyme is thermostable
246787
additional information
-
enzyme is thermostable; enzyme is thermostable, thermostability is pH-dependent, turkey enzyme is less unstable at higher pH values than horse enzyme
246789
additional information
-
thermal inactivation studies
246796
additional information
-
increase of urea concentration causes reduction of the thermoresistance of the protein; no cold denaturation; studies on conformational stability of muscle acylphosphatase
246799
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
brain enzyme, stable to proteolytic enzymes
-
brain enzyme, unusually stable to prolonged storage, lyophilization and to acid treatment
-
enzyme is very stable
-
8 M urea denaturation is biphasic, being more rapid in the first min then slowing progressively
-
enzyme is very stable
-
liver enzyme, stable to acid treatment
-
muscle enzyme, stable to various denaturating agents
-
two acyl phosphatase activities in liver, one labile and the other acid, heat stable
-
enzyme is very stable
-
muscle enzyme, unusually stable to acid treatment
-
addition of very low concentrations of phosphate causes a strong stabilisation of AcP against chemical denaturation
-
glucose stabilizes, denaturation midpoint of AcP shifts towards higher urea concentration upon the progressive addition of glucose, confirming that the conformational stability of the protein is higher in the presence of sugars
-
highest stability against urea is at pH 9.5
-
in the presence of 25% (v/v) trifluoroethanol, muscle AcP unfolds rapidly into a denatured state enriched with alpha-helical structure
-
muscular enzyme, sensitive to urea: urea denaturation
-
no cold denaturation
-
studies on conformational stability of muscle acylphosphatase
-
study of unfolding and refolding kinetics, kinetic studies of stabilization
-
enzyme very sensitive to 8 M urea
-
enzyme is very stable
-
5.7 M guanidinium chloride causes 50% denaturation of Pyrococccus horikoshii AcP
-
30min stable in 20% trifluoroethanol at 25C
-
Sulfolobus solfataricus acylphosphatase (AcP) does not aggregate in phosphate buffer. AcP remains in a native-like conformation when placed in aggregating conditions (15-25% (v/v) 2,2,2-trifluoroethanol at pH 5.5)
-
enzyme is very stable
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,1,1,3,3,3-hexafluoro-2-propanol
-
most effective accelerator of both folding and unfolding, strongest stabilizer of alpha-helical structure in AcP. Strongest secondary structure stabilizer and most powerful folding accelerator when used at low concentrations, suggesting that the stabilisation of native-like secondary structure, in particular alpha-helical structure, is likely to play a role in AcP folding
1-propanol
-
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP
2,2,2-trifluoroethanol
-
most effective accelerator of both folding and unfolding, strongest stabilizer of alpha-helical structure in AcP
2-propanol
-
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP
Acetone
-
70% v/v, stable at -10C for 3 h
Ethanol
-
unstable to
Ethanol
-
unstable to
Ethanol
-
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP
Methanol
-
unstable to
Methanol
-
unstable to
Methanol
-
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C stable for at least 1 year
-
brain enzyme, unusually stable to prolonged storage
-
4C, Ch1 crystalline enzyme suspension, long-time stable
-
4C, Ch2, 70% ammonium sulfate, long-time stable
-
-10C, crystalline enzyme, 42% ammonium sulfate, stable for long periods, 1 year with no loss of activity
-
-20C, long-time stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by cation exchange chromatography and gel filtration
-
brain
-
brain; heart muscle
-
brain; ox
-
erythrocyte form isoenzyme
-
heart, cardiac muscle
-
multiple molecular forms: Ho1, Ho2 and Ho3
-
muscle and liver
-
from breast and leg muscles; two isozymes: Ch1 and Ch2
-
partially from breast muscle
-
two isozymes: Ch1 and Ch2
-
C21S mutant
-
erythrocyte isoenzyme
-
HiTrap SP HP column chromatography and Superdex 75 column chromatography
-
muscular isoenzyme as fusion protein with glutathione S-transferase, subsequently cleaved to fully active acylphosphatase and further purified
-
recombinant muscle type and common type isoenzymes
-
recombinant wild-type and Cys21 mutants: C21A and C21S
-
recombinant wild-type and mutated acylphosphatases
-
muscle, erythrocyte isoenzyme
-
; ammonium sulfate fractionation and cation exchange chromatography
-
; HiTrap SP HP column chromatography and Superdex 75 column chromatography
-
muscle, erythrocyte type enzyme
-
heart muscle
-
testis and skeletal muscle
-
recombinant TT0497 from Escherichia coli strain BL21(DE3) by two steps of ion exchange chromatography, and gel filtration
Q5SKS6
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene yflL, expression in Escherichia coli
-
the Acyp locus, CG16870, encodes acylphosphatase. There is a strong association between Acyp alleles as genotype and the sterility/fertility pattern as phenotype, as well as between the phenotype, the genotype and its transcriptional activity. Allelic expression analysis
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
the Acyp locus, CG16870, encodes acylphosphatase. There is a strong association between Acyp alleles as genotype and the sterility/fertility pattern as phenotype, as well as between the phenotype, the genotype and its transcriptional activity. Allelic expression analysis
-
C21S mutant
-
cDNA cloning, wild-type and mutated recombinant acylphosphatase, recombinant protein expression in Escherichia coli strain BL21; synthetic gene coding for human muscle enzyme, expressed in Escherichia coli strain BL21
-
cDNA, erythrocyte isoenzyme; expression in Escherichia coli using pT7.7 expression vector
-
expressed in Escherichia coli strain C41
-
expression in Escherichia coli. Human acylphosphatase cannot replace phosphoglycerate kinase in Saccharomyces cerevisiae. The enzyme is not a useful tool to modify the ATP yield of glycolysis in Saccharomyces cerevisiae
-
muscle type and common type isoenzymes, expression in Escherichia coli
-
muscular isoenzyme as fusion protein with glutathione S-transferase, synthetic gene linked to the gene for glutathione S-transferase, expression in Escherichia coli strains DB1035 and TB1
-
wild-type and Cys21 mutants: C21A and C21S, expressed in Escherichia coli strain BL21
-
; expressed in Escherichia coli strain C41
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain Rosetta; expression in Escherichia coli
-
expressed in Escherichia coli; expression in Escherichia coli
P84142
expressed in Escherichia coli
-
expressed in Escherichia coli strain DH5alpha
-
expression in Escherichia coli
-
expression of TT0497 in Escherichia coli strain BL21(DE3)
Q5SKS6
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C5A/C49A
P0AB65
site-directed mutagenesis, the folding of the mutant lacking the disulfide bond is impaired and conformational stability is decreased compared to the wild-type enzyme, mutEcoAcP folds about 1500fold slower and a partially folded species accumulates int he mutant expressing strain
C21A
-
reduced specific activity, 60% compared with wild-type enzyme, kinetic and structural properties similar to those of wild-type recombinant enzyme, urea and thermal stabilities reduced: Cys21 possible involved in stabilization of enzyme active-site conformation, involved in enzyme structure stabilization, not involved in substrate binding
C21S
-
-
C21S
-
reduced specific activity, 85% compared with wild-type enzyme, kinetic and structural properties similar to those of wild-type recombinant enzyme, urea and thermal stabilities reduced: Cys21 possible involved in stabilization of enzyme active-site conformation, involved in enzyme structure stabilization, not involved in substrate binding
C21S
-
the mutant avoids complexity arising from the presence of free thiol groups
R23Q
-
mutant of muscle type enzyme is totally inactive using benzoylphosphate as a substrate and not able to bind the phosphate moiety of that substrate, mutant inactive on DNA, Arg23 possible has a central role for muscle type acylphosphatase activity on DNA
R97Q
-
reduced specific activity, kinetic and structural properties of R97Q mutant indicate possible role of Arg-97 in the stabilisation of the active site correct conformation, most likely via back-bone and side chain interactions with Arg-23, the residue involved in phosphate binding by the enzyme
Y98Q
-
reduced specific activity, kinetic and structural properties of Y98Q mutant indicate possible involvement of Tyr-98 in stabilisation of acylphosphatase overall structure
A18G
-
site-directed mutagenesis, thermodynamic and kinetic parameters
A37G
-
site-directed mutagenesis, thermodynamic and kinetic parameters
A46G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, site-directed mutagenesis, thermodynamic and kinetic parameters
A58G
-
site-directed mutagenesis, thermodynamic and kinetic parameters
D6C
-
the mutant recovers enzymatic activity following refolding, suggesting reversible unfolding processes
D85C
-
the mutant recovers enzymatic activity following refolding, suggesting reversible unfolding processes
DELTAN11
-
lacking 11 residues at the N terminus
DELTAN5
-
lacking 5 residues at the N terminus
DELTAN8
-
lacking 8 residues at the N terminus
E59A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
F29L
-
single-point mutant from nonflexible regions
F29L
-
site-directed mutagenesis, thermodynamic and kinetic parameters
F88A
-
single substitution of residue from the flexible region 83-91
F88A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
F98L
-
site-directed mutagenesis, thermodynamic and kinetic parameters
G52A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters, site-directed mutagenesis, thermodynamic and kinetic parameters
G93A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
I42V
-
site-directed mutagenesis, thermodynamic and kinetic parameters
I72V
-
single-point mutant from nonflexible regions
I72V
-
site-directed mutagenesis, thermodynamic and kinetic parameters
K47A
-
single substitution of residue from the flexible region 44-61
K92A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters, site-directed mutagenesis, thermodynamic and kinetic parameters
L49A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
L65A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, site-directed mutagenesis, thermodynamic and kinetic parameters
L68A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
N48A
-
single substitution of residue from the flexible region 44-61
N48A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
P50A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
P76A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
P77A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
R15A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
R19A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
R30A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
R71A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
S89A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
V20A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, site-directed mutagenesis, thermodynamic and kinetic parameters
V24A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
V27A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
V54A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
V81A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
V84A
-
single substitution of residue from the flexible region 83-91
V84A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
V84D
-
site-directed mutagenesis
V84D
-
mutation provides protection against aggregation by the insertion of an edge negative charge
V84P
-
site-directed mutagenesis
V84P
-
mutation provides protection against aggregation in edge beta-strand B4
V9A/F10A
-
double substitution within the region 1-12 that appears to be susceptible to proteolysis
Y45A
-
single substitution of residue from the flexible region 44-61
Y61A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
Y61L
-
site-directed mutagenesis, thermodynamic and kinetic parameters
Y86A
-
single substitution of residue from the flexible region 83-91
Y86E
-
site-directed mutagenesis
Y86E
-
mutation provides protection against aggregation by the insertion of an edge negative charge
V84D
-
mutation provides protection against aggregation by the insertion of an edge negative charge
-
V84P
-
mutation provides protection against aggregation in edge beta-strand B4
-
Y86E
-
mutation provides protection against aggregation by the insertion of an edge negative charge
-
DELTA1-6 deletion mutant
-
N-terminus truncated mutant lacks the first six residues: reduced specific activity and native-like structure
additional information
-
the native state of the enzyme presents two alpha-helices. Equilibrium and kinetic measurements for folding indicate that only helix-2, spanning residues 55-67, is largely stabilized in the transition state for folding therfore playing a relevant role in this process. The aggregation rate appears to vary only for the variants in which the propensity of the region corresponding to helix-1, spanning residues 22-32, is changed. Mutations that stabilize the first helix slow down the aggregation process while those that destabilize it increase the aggregation rate
additional information
-
construction of 50 mutants with changes in hydrophobicity, secondary-structure propensity and net charge for mutational analysis of aggregation and disaggregation of amyloid-like protofibrils of human muscle acylphosphatase, overview
M16A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
additional information
-
assembly of folded protein molecules into native-like aggregates is prevented by single-point mutations that introduce structural protections within one of the most flexible region of the protein, the peripheral edge beta-strand 4. The resulting mutants do not form native-like aggregates, but can still form thioflavin T-binding and beta-structured oligomers, albeit more slowly than the wild-type protein
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
renaturation after thermal denaturation, 65C; renaturation after treatment with urea
-
folding and unfolding kinetics of wild-type and mutant enzymes at 28C and pH 5.5 as a function of GdnHCl concentration, overview
P0AB65
refolding of muscle AcP in 6 M urea
-
renaturation after heat denaturation; renaturation after treatment with urea
-
renaturation after thermal denaturation, 65C; renaturation after treatment with urea
-
renaturation after treatment with urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
protein aggregation is associated with a number of human pathologies including Alzheimers and Creutzfeldt-Jakob diseases and the systemic amyloidoses. 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