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Information on EC 3.6.1.7 - acylphosphatase and Organism(s) Pyrococcus horikoshii and UniProt Accession P84142
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3.6.1.7 acylphosphataseSpecify your search results
Word Map
- 3.6.1.7
- horse
-
native-like
- ca2+-atpase
- solfataricus
- trifluoroethanol
- phosphoenzyme
- acylphosphates
-
thioflavine
- ototoxicity
-
amyloid-like
-
protofibrils
- medicine
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acylphosphatase, acyp2, sso acp, acyl phosphatase, phacp, acetylphosphatase, acpdro2, acetyl phosphatase, human common-type acylphosphatase, isozyme ch1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,3-diphosphoglycerate phosphatase
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-
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acetic phosphatase
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-
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acetyl phosphatase
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-
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acetylphosphatase
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-
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ACP
acyl phosphatase
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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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Isozyme CH1
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Isozyme CH2
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Isozyme TU1
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phosphatase, acyl
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ACP
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
acylphosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9012-34-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
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-
-
?
nucleoside diphosphate + H2O
nucleoside phosphate + phosphate
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-
-
?
nucleoside triphosphate + H2O
nucleoside diphosphate + phosphate
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-
-
?
1,3-diphosphoglycerate + H2O
3-phosphoglycerate + phosphate
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-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10000
benzoyl phosphate
at 98°C and pH 5.3, estimation by linear extrapolation
additional information
additional information
experimentally, it is impossible to assay the enzyme activity of the enzyme directly at 98°C because the uncatalyzed hydrolysis of the acyl-phosphate substrate is too fast at high temperatures to allow an accurate measurement of kinetic parameters. Instead, the kinetic parameters of the enzyme are measured at 25-45 °C and the kcat value of the enzyme at 98 °C is estimated by linear extrapolation of the Arrhenius plot. The estimated kcat value is 10000/s
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additional information
additional information
-
experimentally, it is impossible to assay the enzyme activity of the enzyme directly at 98°C because the uncatalyzed hydrolysis of the acyl-phosphate substrate is too fast at high temperatures to allow an accurate measurement of kinetic parameters. Instead, the kinetic parameters of the enzyme are measured at 25-45 °C and the kcat value of the enzyme at 98 °C is estimated by linear extrapolation of the Arrhenius plot. The estimated kcat value is 10000/s
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
turnover number increases 4fold by an increase of temperature from 25 to 45°C
additional information
additional information
a rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity. The thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human is employed as a model to study how local rigidity of an active-site residue affects the enzymatic activity
additional information
-
a rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity. The thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human is employed as a model to study how local rigidity of an active-site residue affects the enzymatic activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10128
10129
1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
10128
2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds
monomer
monomer
1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop-vapor-diffusion method, 1.5 A crystal structure. The enzyme forms a dimer in the crystal structure via antiparallel association of strand 4
sitting-drop-vapor-diffusion with sodium formate as precipitant at pH 6.0
the structure of G91A mutant enzyme is determined by x-ray crystallography at 2.4 A resolution, and it is superimposable with the structure of wild-type enzyme
sitting drop vapour diffusion method with potassium/sodium tartrate at pH 5.5
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sitting drop vapour diffusion method with sodium formate as precipitant
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sitting-drop vapour-diffusion method using sodium formate as precipitant at 16°C. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 85.65 A, c = 75.51 A. The asymmetric unit contains two molecules of enzyme
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sitting-drop vapour-diffusion method with postasium/sodium tartrate as the precipitant at pH 5.5. The crystals belong to space group P3(2)21, with approximate unit-cell parameters a = b = 86.7 A, c = 75.4 A and two monomers in the asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G91A
at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 100
At 25°C, the free energy of unfolding, midpoint of transition, and m value were 54.4 kJ/mol, 4.99 M, and 10.9 kJ/mol/M, respectively. The melting temperature is about 111.5°C. These data indicate that PhAcP is an extremely thermostable protein.
90
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no disruption of three-dimensional structure when incubated at 90°C for 30min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5.7 M guanidinium chloride causes 50% denaturation of Pyrococccus horikoshii AcP
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap SP HP column chromatography and Superdex 75 column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miyazono, K.I.; Kudo, N.; Tanokura, M.
Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. D
60
1135-1136
2004
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
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
Acta Crystallogr. Sect. D
60
1308-1310
2004
Pyrococcus horikoshii
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)
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
-
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
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.
9
e1001027
2011
Pyrococcus horikoshii (P84142), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (P84142)
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Release 2023.1 (January 2023)
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