3.6.1.7: acylphosphatase
This is an abbreviated version!
For detailed information about acylphosphatase, go to the full flat file.
Word Map on EC 3.6.1.7
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3.6.1.7
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horse
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native-like
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ca2+-atpase
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solfataricus
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trifluoroethanol
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phosphoenzyme
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acylphosphates
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thioflavine
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ototoxicity
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amyloid-like
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protofibrils
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medicine
- 3.6.1.7
- horse
-
native-like
- ca2+-atpase
- solfataricus
- trifluoroethanol
- phosphoenzyme
- acylphosphates
-
thioflavine
- ototoxicity
-
amyloid-like
-
protofibrils
- medicine
Reaction
Synonyms
1,3-diphosphoglycerate phosphatase, acetic phosphatase, acetyl phosphatase, acetylphosphatase, ACP, AcPDRo2, acyl phosphatase, acyl phosphate phosphohydrolase, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, erythrocyte/testis isozyme, Acylphosphate phosphohydrolase, acylphosphate phosphomonohydrolase, Acyp, ACYP2, carbamoylphosphate phosphatase, carbamyl phosphate phosphatase, Ch1, Ch2, GP 1-3, GP1, GP2, GP3, Ho 1-3, Ho1, Ho2, Ho3, human common-type acylphosphatase, Isozyme CH1, Isozyme CH2, Isozyme TU1, More, muscle-type acylphosphatase 2, native acylphosphatase, PhAcP, phosphatase, acyl, Sso AcP, SSO0887, T1, TT0497
ECTree
3.6.1.7 acylphosphataseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.6.1.7 - acylphosphatase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
glucose
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glucose buffer, pH 11.2-12.0, progressive inactivation, complete after 1 h
guanidine
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brain enzyme, 5 M: 100% reversible inhibition, 95% of original activity is recovered upon lowering the guanidine concentration by dilution
Phenylglyoxal
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6 mM: inhibition, inhibition partially removed by 35 mM phosphate
thyroxine
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brain enzyme, more inhibitory when preincubation is conducted at 16°C than at 25°C
trifluoroethanol
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in presence of 1525% (v/v) trifluoroethanol, enzyme forms aggregates able to bind specific dyes such as thioflavine T, Congo red, and 1-anilino-8-naphthalenesulfonic acid. The monomeric form adopted by the enzyme prior to aggregation under these conditions retains enzymatic activity, in addition, folding was remarkably faster than unfolding. Electron microscopy reveals the presence of small aggregates generally referred to as amyloid protofibrils
2,3-diphosphoglycerate
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erythrocyte isoenzyme, competitive inhibition, Ki: 0.24 mM
2,3-diphosphoglycerate
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competitive inhibition, Ki erythrocyte enzyme: 0.41 mM, Ki skeletal muscle enzyme: 3.74 mM
2,3-diphosphoglycerate
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heart enzyme, 2 mM: 12% inhibition, substrate: 1,3-diphosphoglycerate
3-phosphoglycerate
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heart enzyme, 5 mM: 8% inhibition, substrate: 1,3-diphosphoglycerate
Cl-
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competitive inhibition; Ho1, Ki: 40.0 mM; Ho2, Ki: 50.0 mM; Ho3, Ki: 40.0 mM
Cl-
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competitive inhibition, Ki erythrocyte enzyme: 51.70 mM, Ki skeletal muscle enzyme: 42.10 mM
Cl-
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muscular isoenzyme, Ki: 40.0 mM, erythrocyte isoenzyme, Ki: 31.0 mM
EDTA
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inhibition of ribonucleolytic and deoxyribonucleolytic activity of acylphosphatase
EDTA
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1 mM: 100% inhibition of endonucleolytic activity of both isoforms; inhibition of ribonucleolytic and deoxyribonucleolytic activity of acylphosphatase
EDTA
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inhibition of ribonucleolytic and deoxyribonucleolytic activity of acylphosphatase
Hg2+
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inhibition partially reactivated in the absence of Hg2+, mutant enzymes regained 65-85% of original activity, wild-type enzyme regained less than 50%
phosphate
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competitive inhibition; Ho1, Ki: 1.7 mM; Ho2, Ki: 2.3 mM; Ho3, Ki: 1.6 mM
phosphate
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competitive inhibition, Ki erythrocyte enzyme: 0.30 mM, Ki skeletal muscle enzyme: 2.72 mM
phosphate
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phosphate: competitive inhibition, muscular enzyme, native Ki: 2.29 mM, recombinant, expressed as fusion protein with glutathione S-transferase, Ki: 3.05
phosphate
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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
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phosphate, competitive inhibition, muscular isoenzyme, wild-type, Ki: 0.9 mM, C21A Ki: 0.9 mM, C21S Ki: 0.7 mM
phosphate
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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
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competitive inhibition; phosphate: competitive inhibition, addition of very low concentrations of phosphate causes a strong stabilisation of AcP against chemical denaturation
phosphate
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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
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muscular isoenzyme, Ki: 2.8 mM, erythrocyte isoenzyme, Ki: 0.68 mM
phosphate
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heart enzyme, 5 mM: 37% inhibition, substrate: 1,3-diphosphoglycerate; heart enzyme, competitive inhibition
phosphoenolpyruvate
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competitive inhibition, Ki erythrocyte enzyme: 0.38 mM, Ki skeletal muscle enzyme: 2.23 mM
pyridoxal 5'-phosphate
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muscle enzyme, pH-dependent competitive, reversible inhibition, Ki: 0.32 mM
pyridoxal 5'-phosphate
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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
Urea
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brain enzyme, 5 M: 100% reversible inhibition, 95% of original activity is recovered upon lowering the urea concentration by dilution
Urea
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2.7 M: 50% inhibition, 8M: 100% inhibition, 90% of its original activity regained in the absence of urea
Urea
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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
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8 M: 100% inhibition; 8 M: 100% reversibel inhibition, 60% reactivation in the absence of urea
additional information
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brain enzyme, no inhibition by 0.04 mM HgCl2 and 4 mM iodoacetate
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additional information
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brain enzyme, no inhibition by caffeine, inosinic acid, 0.5% trypsin and 1% papain
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additional information
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no inhibition by adenosine monophosphate, phosphoethanolamine and alpha-glycerophosphate
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additional information
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muscle enzyme, no inhibition by pyridoxamine 5'-phosphate and pyridoxine 5'-phosphate
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additional information
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no inhibition by carboxylic acid, acetic acid, acetate, Na+
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