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Literature summary for 3.6.1.7 extracted from

  • 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 (2005), Biochemistry, 44, 4601-4611.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Pyrococcus horikoshii
expression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Pyrococcus horikoshii
sitting-drop-vapor-diffusion with sodium formate as precipitant at pH 6.0 Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
benzoyl phosphate at 25°C and pH 5.3 Pyrococcus horikoshii
0.12
-
benzoyl phosphate 25-45°C, pH 5.3 Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
10128
-
1 * 10128, enzyme in solution Pyrococcus horikoshii
10128
-
2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds Pyrococcus horikoshii
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 Pyrococcus horikoshii
10130
-
mass spectrometry Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii P84142
-
-
Pyrococcus horikoshii DSM 12428 P84142
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,3-diphosphoglycerate + H2O
-
Pyrococcus horikoshii 3-phosphoglycerate + phosphate
-
?
1,3-diphosphoglycerate + H2O
-
Pyrococcus horikoshii DSM 12428 3-phosphoglycerate + phosphate
-
?
acetyl phosphate + H2O
-
Pyrococcus horikoshii acetate + phosphate
-
?
acetyl phosphate + H2O
-
Pyrococcus horikoshii DSM 12428 acetate + phosphate
-
?
benzoyl phosphate + H2O
-
Pyrococcus horikoshii benzoate + phosphate
-
?
benzoyl phosphate + H2O
-
Pyrococcus horikoshii DSM 12428 benzoate + phosphate
-
?
carbamoyl phosphate + H2O
-
Pyrococcus horikoshii carbamate + phosphate
-
?
carbamoyl phosphate + H2O
-
Pyrococcus horikoshii DSM 12428 carbamate + phosphate
-
?
nucleoside diphosphate + H2O
-
Pyrococcus horikoshii nucleoside phosphate + phosphate
-
?
nucleoside diphosphate + H2O
-
Pyrococcus horikoshii DSM 12428 nucleoside phosphate + phosphate
-
?
nucleoside triphosphate + H2O
-
Pyrococcus horikoshii nucleoside diphosphate + phosphate
-
?
succinyl phosphate + H2O
-
Pyrococcus horikoshii succinate + phosphate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds Pyrococcus horikoshii
monomer 1 * 10128, enzyme in solution Pyrococcus horikoshii
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 Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
PhAcP
-
Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
98
-
-
Pyrococcus horikoshii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 45 turnover number increases 4fold by an increase of temperature from 25 to 45°C Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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. Pyrococcus horikoshii
100
-
stable up to Pyrococcus horikoshii
112
-
melting temperature: 111.5°C Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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 Pyrococcus horikoshii
93.5
-
benzoyl phosphate at 25°C and pH 5.3 Pyrococcus horikoshii
93.5
-
benzoyl phosphate 25°C, pH 5.3 Pyrococcus horikoshii
191
-
benzoyl phosphate at 30°C and pH 5.3 Pyrococcus horikoshii
191
-
benzoyl phosphate 30°C, pH 5.3 Pyrococcus horikoshii
275
-
benzoyl phosphate at 35°C and pH 5.3 Pyrococcus horikoshii
275
-
benzoyl phosphate 35°C, pH 5.3 Pyrococcus horikoshii
290
-
benzoyl phosphate at 40°C and pH 5.3 Pyrococcus horikoshii
290
-
benzoyl phosphate 40°C, pH 5.3 Pyrococcus horikoshii
467
-
benzoyl phosphate at 45°C and pH 5.3 Pyrococcus horikoshii
467
-
benzoyl phosphate 45°C, pH 5.3 Pyrococcus horikoshii
10000
-
benzoyl phosphate at 98°C and pH 5.3, estimation by linear extrapolation Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3
-
-
Pyrococcus horikoshii
5.3
-
at 25°C Pyrococcus horikoshii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
779
-
benzoyl phosphate 25 °C, pH 5.3 Pyrococcus horikoshii