Literature summary for 3.2.1.132 extracted from

Fukamizo, T.; Yoshikawa, T.; Katsumi, T.; Amano, S.; Saito, J.; Miki, K.; Ando, A.; Brzezinski, R.
Substrate-binding mode of bacterial chitosanases (2005), J. Appl. Glycosci., 52, 183-189.

No PubMed abstract available

Search for more literature for 3.2.1.132

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion method at 20°C. The crystal structure of mutant K218P reveals that the main chain and side chain structures of the loop comprising Lys218 are effected by the mutation. It is concluded that the flexible loop comprising Lys128 plays an important role in substrate binding	Niallia circulans

Protein Variants

Protein Variants	Comment	Organism
D57A	mutant enzyme shows 0.5% of wild-type activity. Mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme	Streptomyces sp.
D57N	mutant enzyme shows 72% of wild-type activity	Streptomyces sp.
K218P	mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan	Niallia circulans
Y148S	mutant enzyme shows 12% of wild-type activity with acetylated chitosan	Niallia circulans

Organism

Organism	UniProt	Comment	Textmining
Niallia circulans	-	MH-K1	-
Niallia circulans MH-K1	-	MH-K1	-
Streptomyces sp.	-	N174	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetylated chitosan + H2O	-	Niallia circulans	?	-	?
acetylated chitosan + H2O	-	Streptomyces sp.	?	-	?
acetylated chitosan + H2O	-	Niallia circulans MH-K1	?	-	?
chitohexaose + H2O	-	Streptomyces sp.	chitobiose + chitotriose + chitotetraose	mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme	?
chitopentaose + H2O	-	Streptomyces sp.	?	-	?
chitotetraose + H2O	-	Streptomyces sp.	?	-	?

Synonyms

Synonyms	Comment	Organism
MH-K1 chitosanase	-	Niallia circulans
N174 chitosanase	-	Streptomyces sp.

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Release 2023.1 (January 2023)