Literature summary for 3.4.21.62 extracted from

Cianci, M.; Tomaszewski, B.; Helliwell, J.R.; Halling, P.J.
Crystallographic analysis of counterion effects on subtilisin enzymatic action in acetonitrile (2010), J. Am. Chem. Soc., 132, 2293-2300.

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Activating Compound

Activating Compound	Comment	Organism	Structure
choline	increases the enzyme activity	Bacillus licheniformis

Crystallization (Commentary)

Crystallization (Comment)	Organism
by the batch method from buffer solution saturated with Na2SO4 ca. 13% (w/v) as precipitant. Placement of several Cs+ and Cl- ions in crystals of subtilisin Carlsberg. The protein conformation is very similar to that of the enzyme without CsCl in acetonitrile. 11 defined sites for Cs+ cations and 8 Cl- anions around the protein molecule, although most of these have partial occupancy and may represent nonspecific binding sites. Two Cs+ and two Cl- ions are close to the mouth of the active site cleft, where they may affect catalysis. CsCl-treated subtilisin crystals transferred to acetonitrile show catalytic activity several fold higher than the reference crystals containing Na+	Bacillus licheniformis

Crystallization (Comment)

Organism

by the batch method from buffer solution saturated with Na2SO4 ca. 13% (w/v) as precipitant. Placement of several Cs+ and Cl- ions in crystals of subtilisin Carlsberg. The protein conformation is very similar to that of the enzyme without CsCl in acetonitrile. 11 defined sites for Cs+ cations and 8 Cl- anions around the protein molecule, although most of these have partial occupancy and may represent nonspecific binding sites. Two Cs+ and two Cl- ions are close to the mouth of the active site cleft, where they may affect catalysis. CsCl-treated subtilisin crystals transferred to acetonitrile show catalytic activity several fold higher than the reference crystals containing Na+

Bacillus licheniformis

Metals/Ions

Metals/Ions	Comment	Organism
Cl-	treatment with CsCl increases the activity several fold. Two Cl- ions are close to the mouth of the active site cleft, where they may affect catalysis	Bacillus licheniformis
Cs+	treatment with CsCl increases the activity several fold. Two Cs+ ions are close to the mouth of the active site cleft, where they may affect catalysis	Bacillus licheniformis
KCl	increases enzymatic activity somewhat, while choline-Cl has a larger effect	Bacillus licheniformis
additional information	enzymatic activity of subtilisin crystals in acetonitrile is sensitive to the type of counterions present before transfer to the organic solvent. Larger cations increase the enzyme activity	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	P00780	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetyl-Tyr ethyl ester + H2O	-	Bacillus licheniformis	N-acetyl-Tyr + ethanol	-	?

Synonyms

Synonyms	Comment	Organism
subtilisin Carlsberg	-	Bacillus licheniformis