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Literature summary for 3.2.1.200 extracted from

  • Hult, E.L.; Katouno, F.; Uchiyama, T.; Watanabe, T.; Sugiyama, J.
    Molecular directionality in crystalline beta-chitin: hydrolysis by chitinases A and B from Serratia marcescens 2170 (2005), Biochem. J., 388, 851-856.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Serratia marcescens

Crystallization (Commentary)

Crystallization (Comment) Organism
ChiB comprises a catalytic (beta/alpha)8 barrel domain and a C-terminal putative chitin-binding domain. The cocrystallized chito-oligosaccharide is inserted into the catalytic cleft from the non-reducing end when digested by ChiB Serratia marcescens

Organism

Organism UniProt Comment Textmining
Serratia marcescens P11797
-
-
Serratia marcescens 2170 P11797
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-chitin + H2O
-
Serratia marcescens ? ChiB is active from the nonreducing end to the reducing end ?
beta-chitin + H2O
-
Serratia marcescens 2170 ? ChiB is active from the nonreducing end to the reducing end ?

Synonyms

Synonyms Comment Organism
ChiB
-
Serratia marcescens

General Information

General Information Comment Organism
physiological function digestion of beta-chitin by ChiB occurs from the nonreducing end to the reducing end. Chitinases ChiA and ChiB show synergistic interactions in simultaneous degradation of beta-chitin, but not of glycol chitin Serratia marcescens