Literature summary for 3.2.1.132 extracted from

Lyu, Q.; Shi, Y.; Wang, S.; Yang, Y.; Han, B.; Liu, W.; Jones, D.N.; Liu, W.
Structural and biochemical insights into the degradation mechanism of chitosan by chitosanase OU01 (2015), Biochim. Biophys. Acta, 1850, 1953-1961 .

Search for more literature for 3.2.1.132

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas sp. A-01

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion at 15°C	Pseudomonas sp. A-01

Protein Variants

Protein Variants	Comment	Organism
D235A	with chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme	Pseudomonas sp. A-01
D25A	with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01
D40A	with polymeric substrate the mutant enzyme shows less than 10% of the activity as compared to wild-type enzyme. With chitohexaose as substrate the mutant enzyme shows about 70% of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01
D43A	with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01
D60E	with chitohexaose as substrate the mutant enzyme shows about 5% of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01
D91A	with polymeric substrate the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme. With chitohexaose as substrate the mutant enzyme shows about 70% of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01
E120A	with polymeric substrate the mutant enzyme shows about 40% enhanced activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 40% enhanced activity as compared to wild-type enzyme	Pseudomonas sp. A-01
E39A	with polymeric substrate the mutant enzyme shows about 50% enhanced activity as compared to wild-type enzyme	Pseudomonas sp. A-01
E63A	with polymeric substrate the mutant enzyme shows about 35% enhanced activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 20% enhanced activity as compared to wild-type enzyme	Pseudomonas sp. A-01
H203A	with chitohexaose as substrate the mutant enzyme shows no activity	Pseudomonas sp. A-01
T58A	with chitohexaose as substrate the mutant enzyme shows about 90% of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01
Y233A	with polymeric substrate the mutant enzyme shows less than 10% of the activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme	Pseudomonas sp. A-01
Y37F	with chitohexaose as substrate the mutant enzyme shows about 95 % of the activity as compared to wild-type enzyme	Pseudomonas sp. A-01

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp. A-01	Q8KZM5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
chitohexaose + H2O	-	Pseudomonas sp. A-01	?	-	?
chitosan + H2O	substrate recognition mechanismis for non-processive chitosanase is decribed	Pseudomonas sp. A-01	?	-	?

Synonyms

Synonyms	Comment	Organism
chitosanase OU01	-	Pseudomonas sp. A-01

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)