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1,3-diphosphoglycerate phosphatase
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acetic phosphatase
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acetyl phosphatase
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acetylphosphatase
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acyl phosphate phosphohydrolase
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Acylphosphatase, erythrocyte isozyme
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Acylphosphatase, erythrocyte/testis isozyme
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Acylphosphate phosphohydrolase
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acylphosphate phosphomonohydrolase
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carbamoylphosphate phosphatase
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carbamyl phosphate phosphatase
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GP 1-3
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multiple forms of guinea pig acylphosphatase
GP1
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multiple forms of guinea pig acylphosphatase, major form
GP2
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multiple forms of guinea pig acylphosphatase
GP3
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multiple forms of guinea pig acylphosphatase
Ho 1-3
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multiple forms of horse acylphosphatase
Ho1
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multiple forms of horse acylphosphatase
Ho2
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multiple forms of horse acylphosphatase
Ho3
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multiple forms of horse acylphosphatase
human common-type acylphosphatase
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muscle-type acylphosphatase 2
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phosphatase, acyl
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T1
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multiple forms of turkey acylphosphatase
ACP
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Acyp
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Ch1
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Ch1 and Ch2 are different genetically specified isozymes
Ch1
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multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters
Ch2
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Ch1 and Ch2 are different genetically specified isozymes
Ch2
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multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters
PhAcP
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Sso AcP
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SSO0887
locus name
TT0497
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additional information
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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
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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
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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
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 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
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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
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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
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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
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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
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
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 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
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 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
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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
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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
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(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
1,3-bisphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
acetyl phosphate + H2O
acetate + phosphate
acetylphosphate + H2O
acetate + phosphate
-
-
-
?
acylphosphate + H2O
a carboxylate + phosphate
-
-
-
-
?
acylphosphate + H2O
carboxylate + phosphate
benzoyl phosphate + H2O
benzoate + phosphate
benzoylphosphate + H2O
benzoate + phosphate
beta-aspartyl phosphate + H2O
aspartate + phosphate
Ca2+-ATPase phosphoenzyme intermediate + H2O
?
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
diphosphate + H2O
2 phosphate
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
nucleoside diphosphate + H2O
nucleoside phosphate + phosphate
nucleoside triphosphate + H2O
nucleoside diphosphate + phosphate
-
-
-
?
p-nitrobenzoyl phosphate + H2O
p-nitrobenzoate + phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
succinoyl phosphate + H2O
succinate + phosphate
succinyl phosphate + H2O
succinate + phosphate
additional information
?
-
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
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-
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-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
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phospho-aspartyl intermediate
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-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
-
acylphosphorylated intermediates of Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum and heart sarcolemma
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-
?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
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?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
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acylphosphate bond in phosphorylated intermediate
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?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
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?
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O
?
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erythrocyte type enzyme, acylphosphorylated intermediates from human erythrocyte membrane
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-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
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-
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-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
?
acetyl phosphate + H2O
acetate + phosphate
-
-
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
erythrocyte isoenzyme shows hydrolytic activity on acyl phosphates with higher affinity than the muscle enzyme
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
hydrolysis of acylphosphates both synthetic and physiologically relevant
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
acylphosphate + H2O
carboxylate + phosphate
-
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
-
?
ATP + H2O
?
-
muscle enzyme, very low activity
-
-
?
ATP + H2O
?
-
liver enzyme, no activity
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoyl phosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoylphosphate + H2O
benzoate + phosphate
-
-
-
-
?
benzoylphosphate + H2O
benzoate + phosphate
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
-
-
-
-
?
beta-aspartyl phosphate + H2O
aspartate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
muscle enzyme, poor substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
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
-
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
-
possible physiological substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
erythrocyte enzyme: not a substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
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
-
role in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
possible physiological substrate
-
-
?
diphosphate + H2O
2 phosphate
-
muscle enzyme, very low activity
-
-
?
diphosphate + H2O
2 phosphate
-
liver enzyme, no activity
-
-
?
diphosphate + H2O
2 phosphate
-
erythrocyte enzyme, inorganic diphosphate: not a substrate
-
-
?
DNA + H2O
?
-
-
-
-
?
DNA + H2O
?
-
DNAase activity, nucleolytic activity, exonucleolytic and endonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
DNA + H2O
?
-
muscle type and common type hydrolyze double stranded DNA, high molecular weight human genomic DNA
-
-
?
DNA + H2O
?
-
DNAase activity, nucleolytic activity, exonucleolytic and endonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
DNA + H2O
?
-
endonucleolytic activity on plasmid DNA, pRcCMV plasmid DNA, closed circular plasmid DNA, exonucleolytic activity on linear plasmid DNA
-
-
?
DNA + H2O
?
-
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
?
-
-
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
sarcolemma Na+,K+-ATPase phosphorylated intermediate
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphatase significantly enhances the rate of strophantidine-sensitive ATP hydrolysis, it uncouples erythrocyte membrane N+,K+ pump
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphatase hydrolyzes phosphoenzyme intermediate of heart sarcolemma Na+,K+-ATPase
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
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
?
-
acylphosphorylated phosphoenzyme intermediate, enzyme has a high affinity for this substrate
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
-
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
mechanism
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphatase can actively hydrolyze Na+/K+-ATPase phosphoenzyme
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphatase produces a modification in the stoichiometry of the ATP driven cation transport by the Na+,K+ pump
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
from erythrocyte membrane
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphatase significantly enhances the rate of strophantidine-sensitive ATP hydrolysis, it uncouples erythrocyte membrane N+,K+ pump
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphatase markedly affects the functional properties of Na+,K+ pump, notably the rate of ATP hydrolysis and of cation, Na+,Rb+, transport
-
-
?
Na+/K+-ATPase phosphoenzyme intermediate + H2O
?
-
acylphosphorylated phosphoenzyme intermediate, enzyme has a high affinity for this substrate
-
-
?
nucleic acids + H2O
?
-
nucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
nucleic acids + H2O
?
-
nucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
nucleic acids + H2O
?
-
nucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
nucleoside diphosphate + H2O
nucleoside phosphate + phosphate
-
-
-
?
nucleoside diphosphate + H2O
nucleoside phosphate + phosphate
-
-
-
?
p-nitrobenzoyl phosphate + H2O
p-nitrobenzoate + phosphate
-
-
-
-
?
p-nitrobenzoyl phosphate + H2O
p-nitrobenzoate + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
liver enzyme, no activity at pH 5.3 and 10.4
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
muscle enzyme, very low activity at pH 5.3, no activity at pH 10.4
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
erythrocyte enzyme, not a substrate
-
-
?
phosphocreatine + H2O
?
-
muscle enzyme, very low activity
-
-
?
phosphocreatine + H2O
?
-
liver enzyme, no activity
-
-
?
poly (rA) + H2O
?
-
ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
poly (rA) + H2O
?
-
ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
poly (rA) + H2O
?
-
ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
RNA + H2O
?
-
RNAase activity, ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
RNA + H2O
?
-
Mg2+ dependent activity
-
-
?
RNA + H2O
?
-
RNAase activity, ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
RNA + H2O
?
-
Mg2+ dependent activity
-
-
?
RNA + H2O
?
-
RNAase activity, ribonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
RNA + H2O
?
-
Mg2+ dependent activity
-
-
?
succinoyl phosphate + H2O
succinate + phosphate
-
-
-
-
?
succinoyl phosphate + H2O
succinate + phosphate
-
-
-
-
?
succinoyl phosphate + H2O
succinate + phosphate
-
-
-
-
?
succinyl phosphate + H2O
succinate + phosphate
-
-
-
-
?
succinyl phosphate + H2O
succinate + phosphate
-
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
hydrolyzes specific only acylphosphates
-
-
?
additional information
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
?
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
?
-
-
specific phosphomonohydrolase activity
-
-
?
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
?
-
-
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
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
?
-
-
enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and production of ribonucleotides
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
additional information
?
-
-
acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
acetyl-AMP: not a substrate
-
-
?
additional information
?
-
-
acetyl-AMP: not a substrate
-
-
?
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
?
-
-
liver enzyme and muscle enzyme, no activity with acetyl-AMP, phosphoenolpyruvate and phosvitin
-
-
?
additional information
?
-
-
liver enzyme and muscle enzyme, no activity with acetyl-AMP, phosphoenolpyruvate and phosvitin
-
-
?
additional information
?
-
-
no activity with phosphoenolpyruvate and phosvitin
-
-
?
additional information
?
-
-
relative hydrolysis rates
-
-
?
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
?
-
-
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
?
-
-
hydrolytic activity by this enzyme on the phosphorylated intermediate is possible involved in Ca2+ transport in sarcoplasmic reticulum
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
additional information
?
-
-
enzyme could control acylation and carbamylation of proteins by regulation the levels of reactive acyl and carbamoyl phosphates
-
-
?
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 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
?
-
-
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
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
?
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
?
-
-
possible role of acylphosphatase in cell differentiation
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
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
?
-
-
hydrolyzes the beta-aspartylphosphate formed during the action of membrane pumps
-
-
?
additional information
?
-
-
hydrolyzes the beta-aspartylphosphate formed during the action of membrane pumps
-
-
?
additional information
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
?
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
?
-
-
specific phosphomonohydrolase activity
-
-
?
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 acyphosphatase involvement in the regulation of ion transport, and of calcium uptake 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
nucleolytic, ribonucleolytic and deoxyribonucleolytic, activity, exonucleolytic and endonucleolytic activity, in both muscle type, MT, and erythrocyte or common type, CT, isoenzymes
-
-
?
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates
-
-
?
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
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
?
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
?
-
-
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
?
-
-
specific phosphomonohydrolase activity
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
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
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
?
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
acts specifically by splitting off the carboxyl phosphate bond
-
-
?
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
acetylphosphate + H2O
acetate + phosphate
-
-
-
?
acylphosphate + H2O
a carboxylate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
additional information
?
-
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
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
-
-
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
possible physiological substrate
-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
-
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
-
1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
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
-
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
-
possible physiological substrate
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
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
-
role in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
-
-
-
?
carbamoyl phosphate + H2O
carbamate + phosphate
-
possible physiological substrate
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
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
?
-
-
enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and production of ribonucleotides
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
additional information
?
-
-
acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
hydrolytic activity by this enzyme on the phosphorylated intermediate is possible involved in Ca2+ transport in sarcoplasmic reticulum
-
-
?
additional information
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
additional information
?
-
-
enzyme could control acylation and carbamylation of proteins by regulation the levels of reactive acyl and carbamoyl phosphates
-
-
?
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 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
?
-
-
possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate
-
-
?
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
?
-
-
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 acyphosphatase involvement in the regulation of ion transport, and of calcium uptake 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates
-
-
?
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
?
-
-
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 isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
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
?
-
-
acylphosphatase isoenzymes are probably involved in membrane ion transport, and glycolysis control
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adrenaline
-
brain enzyme, at high concentrations, 12.5 mM: 65% inhibition
benzyl phosphate
-
moderate competitive inhibition, Ki: 11 mM
Carbamoyl phosphate
-
erythrocyte enzyme, competitive inhibition, Ki: 6.9 mM
dinitrophenol
-
brain enzyme, 0.25 mM: 50% inhibition
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
methyl phosphate
-
moderate competitive inhibition, Ki: 3.5 mM
Pepsin
-
brain enzyme, 2%: inactivation
-
Phenylglyoxal
-
6 mM: inhibition, inhibition partially removed by 35 mM phosphate
Phosphorylated compounds
-
-
-
Sodium thioglycollate
-
muscle enzyme, 0.12 M, 3 h: 30% inhibition
thyroxine
-
brain enzyme, more inhibitory when preincubation is conducted at 16°C than at 25°C
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
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 0.24 mM
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
3-phosphoglycerate
-
-
3-phosphoglycerate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 1.70 mM
3-phosphoglycerate
-
heart enzyme, 5 mM: 8% inhibition, substrate: 1,3-diphosphoglycerate
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
Cl-
-
erythrocyte isoenzyme, competitive inhibition, Ki: 18.0 mM
Cl-
-
competitive inhibition; GP1, Ki: 29.1 mM
Cl-
-
competitive inhibition; Ho1, Ki: 40.0 mM
Cl-
-
competitive inhibition; Ho1, Ki: 40.0 mM; Ho2, Ki: 50.0 mM; Ho3, Ki: 40.0 mM
Cl-
-
competitive inhibition, Ki erythrocyte enzyme: 51.70 mM, Ki skeletal muscle enzyme: 42.10 mM
Cl-
-
competitive inhibition; T1, Ki: 40.0 mM
Cl-
-
muscular isoenzyme, Ki: 40.0 mM, erythrocyte isoenzyme, Ki: 31.0 mM
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
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
Orotic acid
-
liver enzyme, noncompetitive inhibition
p-chloromercuribenzoate
-
muscle enzyme, 1 mM: no inhibition
p-chloromercuribenzoate
-
heart enzyme, 1 mM: very low, less than 5%, inhibition
phosphate
-
-
phosphate
-
brain enzyme 20 mM: 50-60% inhibition, 40 mM: 70-80% inhibition
phosphate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 0.41 mM
phosphate
-
phosphate: inhibition of nucleolytic activity
phosphate
-
competitive inhibition; GP1, Ki: 1.73 mM
phosphate
-
competitive inhibition
phosphate
-
competitive inhibition; Ho1, Ki: 1.7 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
-
strong inhibition
phosphate
-
competitive inhibition
phosphate
-
phosphate, competitive inhibition
phosphate
-
competitive inhibition, Ki erythrocyte enzyme: 0.30 mM, Ki skeletal muscle enzyme: 2.72 mM
phosphate
-
eryhrocyte enzyme, competitive inhibition, Ki: 3.4 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, 1 mM: competitive inhibition of DNAase activity of muscle and common type acylphosphatase, no inhibition of ribonucleolytic activity; 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
-
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; T1, Ki: 2.8 mM
phosphate
-
muscular isoenzyme, Ki: 2.8 mM, erythrocyte isoenzyme, Ki: 0.68 mM
phosphate
-
phosphate: inhibition of nucleolytic activity
phosphate
-
competitive inhibition
phosphate
-
competitive inhibition, Ki: 3 mM
phosphate
-
heart enzyme, 5 mM: 37% inhibition, substrate: 1,3-diphosphoglycerate; heart enzyme, competitive inhibition
phosphoenolpyruvate
-
erythrocyte isoenzyme, competitive inhibition, Ki: 0.21 mM
phosphoenolpyruvate
-
competitive inhibition, Ki erythrocyte enzyme: 0.38 mM, Ki skeletal muscle enzyme: 2.23 mM
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
sulfate
-
Si, heart enzyme, competitive inhibition
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
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
Urea
-
8 M: 100% inhibition; 8 M: 100% reversibel inhibition, 60% reactivation in the absence of urea
additional information
-
brain enzyme, no inhibition by 0.04 mM HgCl2 and 4 mM iodoacetate
-
additional information
-
brain enzyme, no inhibition by caffeine, inosinic acid, 0.5% trypsin and 1% papain
-
additional information
-
no inhibition by adenosine monophosphate, phosphoethanolamine and alpha-glycerophosphate
-
additional information
-
muscle enzyme, no inhibition by pyridoxamine 5'-phosphate and pyridoxine 5'-phosphate
-
additional information
-
-
-
additional information
-
no inhibition by carboxylic acid, acetic acid, acetate, Na+
-
additional information
-
heart enzyme, no inhibition by 2.0 mM HgCl2
-
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C5A/C49A
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
DELTA1-6 deletion mutant
-
N-terminus truncated mutant lacks the first six residues: reduced specific activity and native-like structure
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
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
F98L
-
site-directed mutagenesis, thermodynamic and kinetic parameters
G93A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
I42V
-
site-directed mutagenesis, thermodynamic and kinetic parameters
K47A
single substitution of residue from the flexible region 44-61
L49A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
L68A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
M16A
-
site-directed mutagenesis, 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
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
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
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
-
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
R23Q
-
mutant inactive on DNA, Arg23 possible has a central role for muscle type acylphosphatase activity on DNA
G91A
at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme
G91A
-
at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme
-
A46G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states
A46G
-
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
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
G52A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
I72V
single-point mutant from nonflexible regions
I72V
-
site-directed mutagenesis, thermodynamic and kinetic parameters
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
K92A
-
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
L65A
-
site-directed mutagenesis, thermodynamic and kinetic parameters
L65A
construction of L65A, DELTAN11, and DELTAN11-L65A enzyme mutants, site-directed mutagenesis. L65A is a strongly destabilized protein variant, in which a leucine residue in the hydrophobic core of the protein is substituted by an alanine residue. DELTAN11 Sso AcP is a variant lacking the unstructured N-terminal segment. And a protein variant with the globular unit destabilized by the L65A mutation but lacking the N-terminal segment is DELTAN11-L65A Sso AcP. Comparison of conformational stability of DELTAN11 L65A Sso AcP is assessed by means of equilibrium GndHCl-induced unfolding curves in 50 mM acetate buffer at pH 5.5 and 37°C and compared to those of wild-type Sso AcP, DELTAN11 Sso AcP, and L65A Sso AcP. NMR analysis reveals that the tested variants are folded in cell extracts before aggregation
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
V20A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states
V20A
-
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
Y86E
site-directed mutagenesis
Y86E
mutation provides protection against aggregation by the insertion of an edge negative charge
L65A
-
construction of L65A, DELTAN11, and DELTAN11-L65A enzyme mutants, site-directed mutagenesis. L65A is a strongly destabilized protein variant, in which a leucine residue in the hydrophobic core of the protein is substituted by an alanine residue. DELTAN11 Sso AcP is a variant lacking the unstructured N-terminal segment. And a protein variant with the globular unit destabilized by the L65A mutation but lacking the N-terminal segment is DELTAN11-L65A Sso AcP. Comparison of conformational stability of DELTAN11 L65A Sso AcP is assessed by means of equilibrium GndHCl-induced unfolding curves in 50 mM acetate buffer at pH 5.5 and 37°C and compared to those of wild-type Sso AcP, DELTAN11 Sso AcP, and L65A Sso AcP. NMR analysis reveals that the tested variants are folded in cell extracts before aggregation
-
L65A
-
construction of L65A, DELTAN11, and DELTAN11-L65A enzyme mutants, site-directed mutagenesis. L65A is a strongly destabilized protein variant, in which a leucine residue in the hydrophobic core of the protein is substituted by an alanine residue. DELTAN11 Sso AcP is a variant lacking the unstructured N-terminal segment. And a protein variant with the globular unit destabilized by the L65A mutation but lacking the N-terminal segment is DELTAN11-L65A Sso AcP. Comparison of conformational stability of DELTAN11 L65A Sso AcP is assessed by means of equilibrium GndHCl-induced unfolding curves in 50 mM acetate buffer at pH 5.5 and 37°C and compared to those of wild-type Sso AcP, DELTAN11 Sso AcP, and L65A Sso AcP. NMR analysis reveals that the tested variants are folded in cell extracts before aggregation
-
L65A
-
construction of L65A, DELTAN11, and DELTAN11-L65A enzyme mutants, site-directed mutagenesis. L65A is a strongly destabilized protein variant, in which a leucine residue in the hydrophobic core of the protein is substituted by an alanine residue. DELTAN11 Sso AcP is a variant lacking the unstructured N-terminal segment. And a protein variant with the globular unit destabilized by the L65A mutation but lacking the N-terminal segment is DELTAN11-L65A Sso AcP. Comparison of conformational stability of DELTAN11 L65A Sso AcP is assessed by means of equilibrium GndHCl-induced unfolding curves in 50 mM acetate buffer at pH 5.5 and 37°C and compared to those of wild-type Sso AcP, DELTAN11 Sso AcP, and L65A Sso AcP. NMR analysis reveals that the tested variants are folded in cell extracts before aggregation
-
L65A
-
construction of L65A, DELTAN11, and DELTAN11-L65A enzyme mutants, site-directed mutagenesis. L65A is a strongly destabilized protein variant, in which a leucine residue in the hydrophobic core of the protein is substituted by an alanine residue. DELTAN11 Sso AcP is a variant lacking the unstructured N-terminal segment. And a protein variant with the globular unit destabilized by the L65A mutation but lacking the N-terminal segment is DELTAN11-L65A Sso AcP. Comparison of conformational stability of DELTAN11 L65A Sso AcP is assessed by means of equilibrium GndHCl-induced unfolding curves in 50 mM acetate buffer at pH 5.5 and 37°C and compared to those of wild-type Sso AcP, DELTAN11 Sso AcP, and L65A Sso AcP. NMR analysis reveals that the tested variants are folded in cell extracts before aggregation
-
C20R
the mutant is nearly 100000 times more efficient in catalysis than the wild type protein
C20R
-
the mutant is nearly 100000 times more efficient in catalysis than the wild type protein
-
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
additional information
enzyme silencing (99%) by ACYP2 siRNA-transfected HSP cells. Polymorphisms in ACYP2 gene are associated with oxaliplatin-induced neurotoxicity and with altered telomere length/dysfunction
additional information
-
enzyme silencing (99%) by ACYP2 siRNA-transfected HSP cells. Polymorphisms in ACYP2 gene are associated with oxaliplatin-induced neurotoxicity and with altered telomere length/dysfunction
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
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
additional information
direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red
additional information
-
direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red
additional information
-
direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red
-
additional information
-
direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red
-
additional information
-
direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red
-
additional information
-
direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red
-
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Saudek, V.; Williams, R.J.P.
Secondary structure of acylphosphatase from rabbit skeletal muscle. A nuclear magnetic resonance study [published erratum appears in J Mol Biol 1988 Oct 5;203(3):835]
J. Mol. Biol.
199
233-237
1988
Oryctolagus cuniculus
brenda
Fujita, H.; Mizuno, Y.; Shiokawa, H.
Purification and properties of porcine testis acylphosphatase
J. Biochem.
102
1405-1414
1987
Gallus gallus, Equus caballus, Sus scrofa
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Ohba, Y.; Minowa, O.; Mizuno, Y.; Shiokawa, H.
The primary structure of chicken muscle acylphosphatase isozyme Ch2
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1987
Gallus gallus
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Minowa, O.; Ohba, Y.; Mizuno, Y.; Shiokawa, H.
The primary structure of chicken muscle acylphosphatase isozyme Ch1
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1987
Gallus gallus
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Liguri, G.; Camici, G.; Manao, G.; Cappugi, G.; Nassi, P.; Modesti, A.; Ramponi, G.
A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure
Biochemistry
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Homo sapiens
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Two isozymes of chicken muscle acylphosphatase: purification and properties
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Crystallization and properties of acylphosphatase from porcine skeletal muscle
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Sus scrofa
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Liguri, G.; Nassi, P.; Camici, G.; Manao, G.; Cappugi, G.; Stefani, M.; Berti, A.; Ramponi, G.
Studies on synthesis and degradation rates and some molecular properties of guinea-pig muscle acylphosphatase
Biochem. J.
217
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1984
Cavia porcellus, Equus caballus, Meleagris gallopavo
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Manao, G.; Camici, G.; Stefani, M.; Berti, A.; Cappugi, G.; Liguri, G.; Nassi, P.; Ramponi, G.
Affinity chromatographic purification of horse muscle acylphosphatase: evidence of the existence of multiple molecular forms
Arch. Biochem. Biophys.
226
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1983
Equus caballus
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Stefani, M.; Liguri, G.; Berti, A.; Nassi, P.; Ramponi, G.
Hydrolysis by horse muscle acylphosphatase of (Ca2+ + Mg2+)-ATPase phosphorylated intermediate
Arch. Biochem. Biophys.
208
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1981
Equus caballus
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Ramponi, G.
1,3-Diphosphoglycerate phosphatase
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409-426
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Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Sus scrofa
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Ramponi, G.; Manao, G.; Camici, G.; White, G.F.
Inhibition of horse muscle acylphosphatase by pyridoxal 5'-phosphate
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391
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1975
Equus caballus
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Satchell, D.P.N.; Spencer, N.; White, G.F.
Kinetic studies with muscle acylphosphatase
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Gallus gallus
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Ramponi, G.; Nassi, P.; Cappugi, G.; Treves, C.; Manao, G.
Purification and some molecular properties of horse liver acyl phosphatase
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Equus caballus
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Isolation and crystallization of acyl phosphatase from rabbit muscle
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Oryctolagus cuniculus
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Horse muscle acyl phosphatase: purification and some properties
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Equus caballus
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Further purification and properties of brain acyl phosphatase
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Bos taurus
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Crystal structure of common type acylphosphatase from bovine testis
Structure
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Purification and characterization of acylphosphatase erythrocyte isoenzyme from turkey muscle
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Rat muscle acylphosphatase: purification, amino sequence, and immunological characterization
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Rattus norvegicus
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Acylphosphatase induced modifications in the functional properties of erythrocyte membrane sodium pump
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Purification, kinetic properties and primary structure of bovine erythrocyte acylphosphatase
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Properties of N-terminus truncated and C-terminus mutated muscle acylphosphatases
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Properties of Cys21-mutated muscle acylphosphatases
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Characterization of a novel nucleolytic activity of acylphosphatases
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Structural characterization of the transition state for folding of muscle acylphosphatase
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Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH
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Acylphosphate phosphohydrolases
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-
brenda
Miyazono, K.I.; Kudo, N.; Tanokura, M.
Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3
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Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase
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60
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Drosophila melanogaster
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Cheung, Y.Y.; Allen, M.D.; Bycroft, M.; Wong, K.B.
Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii
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60
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2004
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van Hoek, P.; Modesti, A.; Ramponi, G.; Kotter, P.; van Dijken, J.P.; Pron, J.T.
Human acylphosphatase cannot replace phosphoglycerate kinase in Saccharomyces cerevisiae
Antonie van Leeuwenhoek
80
11-17
2001
Homo sapiens
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Degl'Innocenti, D.; Ramazzotti, M.; Marzocchini, R.; Chiti, F.; Raugei, G.; Ramponi, G.
Characterization of a novel Drosophila melanogaster acylphosphatase
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Taddei, N.; Capanni, C.; Chiti, F.; Stefani, M.; Dobson, C.M.; Ramponi, G.
Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase
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276
37149-37154
2001
Homo sapiens
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Zuccotti, S.; Rosano, C.; Bemporad, F.; Stefani, M.; Bolognesi, M.
Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus
Acta Crystallogr. Sect. F
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2005
Saccharolobus solfataricus
brenda
Yeung, R.C.; Lam, S.Y.; Wong, K.B.
Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase
Acta Crystallogr. Sect. F
F62
80-82
2006
Homo sapiens
brenda
Cheung, Y.Y.; Lam, S.Y.; Chu, W.K.; Allen, M.D.; Bycroft, M.; Wong, K.B.
Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii - structural insights into enzymatic catalysis, thermostability, and dimerization
Biochemistry
44
4601-4611
2005
Pyrococcus horikoshii (P84142), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (P84142)
brenda
Miyazono, K.; Sawano, Y.; Tanokura, M.
Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
Proc. Jpn. Acad. Ser. B
80
439-442
2004
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
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brenda
Miyazono, K.; Sawano, Y.; Tanokura, M.
Crystal structure and structural stability of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
Proteins
61
196-205
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Corazza, A.; Rosano, C.; Pagano, K.; Alverdi, V.; Esposito, G.; Capanni, C.; Bemporad, F.; Plakoutsi, G.; Stefani, M.; Chiti, F.; Zuccotti, S.; Bolognesi, M.; Viglino, P.
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
Proteins
62
64-79
2006
Saccharolobus solfataricus
brenda
Plakoutsi Georgi, P.G.; Bemporad Francesc, B.F.; Monti Mari, M.M.; Pagnozzi Daniel, P.D.; Pucci Pier, P.P.; Chiti Fabrizi, C.F.
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus
Structure
14
993-1001
2006
Saccharolobus solfataricus (Q97ZL0), Saccharolobus solfataricus
brenda
Zuccotti, S.; Rosano, C.; Bemporad, F.; Stefani, M.; Bolognesi, M.
Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus
Acta Crystallogr. Sect. F
61
144-146
2005
Saccharolobus solfataricus
brenda
Bemporad, F.; Capanni, C.; Calamai, M.; Tutino, M.L.; Stefani, M.; Chiti, F.
Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily
Biochemistry
43
9116-9126
2004
Saccharolobus solfataricus
brenda
Plakoutsi, G.; Taddei, N.; Stefani, M.; Chiti, F.
Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation
J. Biol. Chem.
279
14111-14119
2004
Saccharolobus solfataricus
brenda
Bemporad, F.; Vannocci, T.; Varela, L.; Azuaga, A.I.; Chiti, F.
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state
Biochim. Biophys. Acta
1784
1986-1996
2008
Saccharolobus solfataricus (Q97ZL0), Saccharolobus solfataricus
brenda
Bemporad, F.; Gsponer, J.; Hopearuoho, H.I.; Plakoutsi, G.; Stati, G.; Stefani, M.; Taddei, N.; Vendruscolo, M.; Chiti, F.
Biological function in a non-native partially folded state of a protein
EMBO J.
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1525-1535
2008
Saccharolobus solfataricus
brenda
Soldi, G.; Bemporad, F.; Chiti, F.
The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins
J. Am. Chem. Soc.
130
4295-4302
2008
Saccharolobus solfataricus (Q97ZL0), Saccharolobus solfataricus
brenda
Nishibori, E.; Nakamura, T.; Arimoto, M.; Aoyagi, S.; Ago, H.; Miyano, M.; Ebisuzaki, T.; Sakata, M.
Application of maximum-entropy maps in the accurate refinement of a putative acylphosphatase using 1.3 A X-ray diffraction data
Acta Crystallogr. Sect. D
64
237-247
2008
Thermus thermophilus (Q5SKS6), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SKS6)
brenda
Michalak, P.; Ma, D.
The acylphosphatase (Acyp) alleles associate with male hybrid sterility in Drosophila
Gene
416
61-65
2008
Drosophila simulans, Drosophila mauritiana
brenda
Parrini, C.; Bemporad, F.; Baroncelli, A.; Gianni, S.; Travaglini-Allocatelli, C.; Kohn, J.E.; Ramazzotti, M.; Chiti, F.; Taddei, N.
The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond
J. Mol. Biol.
379
1107-1118
2008
Escherichia coli (P0AB65), Escherichia coli
brenda
Calamai, M.; Tartaglia, G.G.; Vendruscolo, M.; Chiti, F.; Dobson, C.M.
Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase
J. Mol. Biol.
387
965-974
2009
Homo sapiens
brenda
Motamedi-Shad, N.; Monsellier, E.; Torrassa, S.; Relini, A.; Chiti, F.
Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathway
J. Biol. Chem.
284
29921-29934
2009
Homo sapiens
brenda
Pagano, K.; Bemporad, F.; Fogolari, F.; Esposito, G.; Viglino, P.; Chiti, F.; Corazza, A.
Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates
J. Biol. Chem.
285
14689-14700
2010
Saccharolobus solfataricus (Q97ZL0), Saccharolobus solfataricus
brenda
Hu, J.; Li, D.; Su, X.D.; Jin, C.; Xia, B.
Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis
FEBS Lett.
584
2852-2856
2010
Bacillus subtilis
brenda
Motamedi-Shad, N.; Garfagnini, T.; Penco, A.; Relini, A.; Fogolari, F.; Corazza, A.; Esposito, G.; Bemporad, F.; Chiti, F.
Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate
Nat. Struct. Mol. Biol.
19; 547-54
S1-2
2012
Homo sapiens
brenda
de Rosa, M.; Bemporad, F.; Pellegrino, S.; Chiti, F.; Bolognesi, M.; Ricagno, S.
Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase
FEBS J.
281
4072-4084
2014
Saccharolobus solfataricus (Q97ZL0), Saccharolobus solfataricus P2 (Q97ZL0)
brenda
Fusco, G.; De Simone, A.; Hsu, S.; Bemporad, F.; Vendruscolo, M.; Chiti, F.; Dobson, C.
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
Biomol. NMR Assign.
6
27-29
2012
Homo sapiens
brenda
Nath, S.; Banerjee, R.; Sen, U.
A novel 8-nm protein cage formed by Vibrio cholerae acylphosphatase
J. Mol. Biol.
426
36-38
2014
Vibrio cholerae (A5F8G9), Vibrio cholerae, Vibrio cholerae O395 (A5F8G9), Vibrio cholerae O395
brenda
Lam, S.; Yeung, R.; Yu, T.; Sze, K.; Wong, K.
A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity
PLoS Biol.
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e1001027
2011
Pyrococcus horikoshii (P84142), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (P84142)
brenda
Elia, F.; Cantini, F.; Chiti, F.; Dobson, C.M.; Bemporad, F.
Direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies
Biophys. J.
112
2540-2551
2017
Saccharolobus solfataricus (Q97ZL0), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97ZL0), Saccharolobus solfataricus JCM 11322 (Q97ZL0), Saccharolobus solfataricus ATCC 35092 (Q97ZL0), Saccharolobus solfataricus DSM 1617 (Q97ZL0)
brenda
Degl'Innocenti, D.; Ramazzotti, M.; Sarchielli, E.; Monti, D.; Chevanne, M.; Vannelli, G.B.; Barletta, E.
Oxadiazon affects the expression and activity of aldehyde dehydrogenase and acylphosphatase in human striatal precursor cells a possible role in neurotoxicity
Toxicology
411
110-121
2019
Homo sapiens (P14621), Homo sapiens
brenda