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Article

Modulation of the transglycosylation activity of plant family GH18 chitinase by removing or introducing a tryptophan side chain.

FEBS letters - 19 Aug 2015

Umemoto Naoyuki, Ohnuma Takayuki, Osawa Takuo, Numata Tomoyuki, Fukamizo Tamo

Abstract excerpt

Transglycosylation (TG) activity of a family GH18 chitinase from the cycad, Cycas revoluta, (CrChiA) was modulated by removing or introducing a tryptophan side chain. The removal from subsite +3 through mutation of Trp168 to alanine suppressed TG activity, while introduction into subsite +1 through mutation of Gly77 to tryptophan (CrChiA-G77W) enhanced TG activity. The crystal structures of an inactive double...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 26216755
DOI: 10.1016/j.febslet.2015.07.018

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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