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Article

Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions.

European journal of biochemistry - 15 Sept 1995

Davoodi J, Wakarchuk W W, Campbell R L, Carey P R, Surewicz W K

Abstract excerpt

The active site of Bacillus circulans xylanase (1,4-beta-D-xylanohydrolase, EC 3.2.1.8) contains two glutamic acid residues, Glu78 and Glu172, which are crucial for the catalytic activity of the enzyme. Fourier-transform infrared spectroscopy was used to determine the ionization state of these residues as a function of pH. For the wild-type enzyme, titration of one of the carboxylate groups occurs at pH 6.8. This...

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PMID: 7588724

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

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