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Article

Structural and enzymatic analysis of soybean beta-amylase mutants with increased pH optimum.

The Journal of biological chemistry - 20 Feb 2004

Hirata Akira, Adachi Motoyasu, Sekine Atsushi, Kang You-Na, Utsumi Shigeru, Mikami Bunzo

Abstract excerpt

Comparison of the architecture around the active site of soybean beta-amylase and Bacillus cereus beta-amylase showed that the hydrogen bond networks (Glu380-(Lys295-Met51) and Glu380-Asn340-Glu178) in soybean beta-amylase around the base catalytic residue, Glu380, seem to contribute to the lower pH optimum of soybean beta-amylase. To convert the pH optimum of soybean beta-amylase (pH 5.4) to that of the...

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PMID: 14638688
DOI: 10.1074/jbc.M309411200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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