Amino acid residues involved in the action of endo-(1→3)-β- d-glucanase II from Flavobacterium dormitator var. glucanolyticae FA-5

The pH-dependence of the kinetic parameters for the hydrolysis of yeast glucan with endo-(1→3)-β- d-glucanase II from Flav. dormitator var. glucanolyticae FA-5 suggests that two residues (histidyl and carboxyl) are involved in the enzyme action. Chemical modification of the enzyme has been studied i...

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Published in:Carbohydrate research 1983-03, Vol.114 (1), p.137-145
Main Authors: Yamamoto, Shinpei, Miyagi, Masamitsu, Nagasaki, Susumu
Format: Article
Language:English
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Summary:The pH-dependence of the kinetic parameters for the hydrolysis of yeast glucan with endo-(1→3)-β- d-glucanase II from Flav. dormitator var. glucanolyticae FA-5 suggests that two residues (histidyl and carboxyl) are involved in the enzyme action. Chemical modification of the enzyme has been studied in order to identify the kinds and the number of amino acid residues involved in enzyme action. Photo-oxidation and carbethoxylation of the enzyme indicated that the decomposition of a histidine residue is responsible for the loss of activity. Modification of the enzyme with Woodward's reagent K indicated that ∼ 12 carboxyl residues in the enzyme are involved in the catalytic and/or substrate binding-site.
ISSN:0008-6215
1873-426X
DOI:10.1016/0008-6215(83)88179-8