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

BRENDA support

Literature summary 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 .
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.132 D235A with chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme Pseudomonas sp. A-01
3.2.1.132 D25A with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme Pseudomonas sp. A-01
3.2.1.132 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
3.2.1.132 D43A with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme Pseudomonas sp. A-01
3.2.1.132 D60E with chitohexaose as substrate the mutant enzyme shows about 5% of the activity as compared to wild-type enzyme Pseudomonas sp. A-01
3.2.1.132 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
3.2.1.132 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
3.2.1.132 E39A with polymeric substrate the mutant enzyme shows about 50% enhanced activity as compared to wild-type enzyme Pseudomonas sp. A-01
3.2.1.132 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
3.2.1.132 H203A with chitohexaose as substrate the mutant enzyme shows no activity Pseudomonas sp. A-01
3.2.1.132 T58A with chitohexaose as substrate the mutant enzyme shows about 90% of the activity as compared to wild-type enzyme Pseudomonas sp. A-01
3.2.1.132 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
3.2.1.132 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

EC Number Organism UniProt Comment Textmining
3.2.1.132 Pseudomonas sp. A-01 Q8KZM5
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.2.1.132 chitosanase OU01
-
 Pseudomonas sp. A-01