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Article

Structure-based design of a lysozyme with altered catalytic activity.

Nature structural biology - 1 Nov 1995

Kuroki R, Weaver L H, Matthews B W

Abstract excerpt

Here we show that the substitution Thr 26-->His in the active site of T4 lysozyme causes the product to change from the alpha- to the beta-anomer. This implies an alteration in the catalytic mechanism of the enzyme. From the change in product, together with inspection of relevant crystal structures, it is inferred that wild-type T4 lysozyme is an anomer-inverting enzyme with a single displacement mechanism in...

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Identifiers

PMID: 7583653
DOI: 10.1038/nsb1195-1007

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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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