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Article

Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.

Journal of molecular biology - 8 Dec 1995

Mace J E, Agard D A

Abstract excerpt

Gly216 in the active site of the broadly specific MA190 mutant of alpha-lytic protease has been found to be remarkably tolerant of amino acid substitutions. Side-chains as large as Trp can be accommodated within the substrate-binding pocket without abolishing catalysis, and have major effects upo...

Topics

Boron Compounds
Crystallography, X-Ray
Enzyme Inhibitors
Glycine
Kinetics
Macromolecular Substances
Models, Molecular
Mutagenesis
Mutation
Protein Conformation
Serine Endopeptidases
Structure-Activity Relationship

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Substrate Specificity

Source

Identifiers

PMID: 7500345
DOI: 10.1006/jmbi.1995.0650

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7500345-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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