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Article

The role of residues R97 and Y331 in modulating the pH optimum of an insect beta-glycosidase of family 1.

European journal of biochemistry - 1 Dec 2003

Marana Sandro R, Mendonça Lúcio M F, Andrade Eduardo H P, Terra Walter R, Ferreira Clélia

Abstract excerpt

The activity of the digestive beta-glycosidase from Spodoptera frugiperda (Sfbetagly50, pH optimum 6.2) depends on E399 (pKa = 4.9; catalytic nucleophile) and E187 (pKa = 7.5; catalytic proton donor). Homology modelling of the Sfbetagly50 active site confirms that R97 and Y331 form hydrogen bonds with E399. Site-directed mutagenesis showed that the substitution of R97 by methionine or lysine increased the E399...

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PMID: 14653813
DOI: 10.1046/j.1432-1033.2003.03887.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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