Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.1.7 extracted from

  • Hu, J.; Li, D.; Su, X.D.; Jin, C.; Xia, B.
    Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis (2010), FEBS Lett., 584, 2852-2856.
    View publication on PubMed
Search for more literature for 3.6.1.7

Cloned(Commentary)

Cloned (Comment) Organism
gene yflL, expression in Escherichia coli Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 gene yflL
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by cation exchange chromatography and gel filtration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoylphosphate + H2O
-
 Bacillus subtilis benzoate + phosphate
-
 ?

Subunits

Subunits Comment Organism
More the structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH below pH 5.8 Bacillus subtilis

Synonyms

Synonyms Comment Organism
ACP
-
 Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3
-
 substrate benzoylphosphate Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
4 5.8 the activity drops sharply below pH 5.3, the enzyme is inactive above pH 5.8 and below pH 4.0. The structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH below pH 5.8 Bacillus subtilis

General Information

General Information Comment Organism
additional information the disordered active site is converted to an ordered state upon ligand binding. Only one main conformation could bind ligand, and the relative population of these states is modulated by ligand concentration, pH-dependent conformations, overview Bacillus subtilis