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Article

Site-directed mutagenesis of a thermostable alpha-amylase from Bacillus stearothermophilus: putative role of three conserved residues.

Journal of biochemistry - 1 Feb 1990

Vihinen M, Ollikka P, Niskanen J, Meyer P, Suominen I, Karp M, Holm L, Knowles J, Mäntsälä P

Abstract excerpt

The relationship between structure, activity, and stability of the thermostable Bacillus stearothermophilus alpha-amylase was studied by site-directed mutagenesis of the three most conserved residues. Mutation of His-238 to Asp involved in Ca2+ and substrate binding reduced the specific activity and thermal stability, but did not affect the pH and temperature optima. Replacement of Asp-331 by Glu in the active...

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PMID: 1694530
DOI: 10.1093/oxfordjournals.jbchem.a123037

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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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