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Article

Asp577 mutations enhance the catalytic efficiency of cyclodextrin glycosyltransferase from Bacillus circulans.

International journal of biological macromolecules - 1 Feb 2016

Li Zhaofeng, Huang Min, Gu Zhengbiao, Holler Tod P, Cheng Li, Hong Yan, Li Caiming

Abstract excerpt

The amino acid residue Asp 577 is located in calcium-binding site III (CaIII) of the cyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) from Bacillus circulans STB01. In the present study, the effects of replacing Asp577 with glycine, alanine, valine, leucine, and isoleucine on the catalytic efficiency of this CGTase were investigated. Two of these replacements, D577G and D577A, increased the β-cyclization...

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PMID: 26608005
DOI: 10.1016/j.ijbiomac.2015.11.042

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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