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Literature summary for 3.6.1.7 extracted from

  • 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 (2011), PLoS Biol., 9, e1001027 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.7

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
G91A at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii P84142
-
-
Pyrococcus horikoshii OT-3 P84142
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl phosphate + H2O
-
 Pyrococcus horikoshii benzoate + phosphate
-
 ?
benzoyl phosphate + H2O
-
 Pyrococcus horikoshii OT-3 benzoate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PhAcP
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 assay at Pyrococcus horikoshii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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 Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
211
-
 benzoyl phosphate pH 5.3, 25°C, mutant enzyme GG91A Pyrococcus horikoshii
228
-
 benzoyl phosphate pH 5.3, 25°C, wild-type enzyme Pyrococcus horikoshii
520
-
 benzoyl phosphate pH 5.3, 45°C, mutant enzyme GG91A Pyrococcus horikoshii
760
-
 benzoyl phosphate pH 5.3, 45°C, wild-type enzyme Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3
-
 assay at Pyrococcus horikoshii