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Streptomyces matensis laminaripentaose hydrolase is an ‘inverting’ β‐1,3‐glucanase
Author(s) -
Nishimura T.,
Big C.,
Allouch J.,
Czjzek M.,
Darbon H.,
Watanabe T.,
Henrissat B.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02551-0
Subject(s) - glycoside hydrolase , glucanase , hydrolase , chemistry , streptomyces , enzyme , stereochemistry , anomer , recombinant dna , biochemistry , biology , genetics , gene , bacteria
The laminaripentaose‐producing β‐1,3‐glucanase of Streptomyces matensis is a member of the glycoside hydrolase family GH‐64. We have constructed and purified a recombinant hexahistidine‐tagged form of the enzyme for characterisation. The enzyme, which exists as a monomer in solution, hydrolyses β‐1,3‐glucan by a mechanism leading to overall inversion of the anomeric configuration. This is the first determination of the mechanism prevailing in glycoside hydrolase family GH‐64 and this is the first characterisation of an ‘inverting’ β‐1,3‐glucanase.