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Article

Mutational analysis of target enzyme recognition of the beta-trefoil fold barley alpha-amylase/subtilisin inhibitor.

The Journal of biological chemistry - 15 Apr 2005

Bønsager Birgit C, Nielsen Peter K, Abou Hachem Maher, Fukuda Kenji, Praetorius-Ibba Mette, Svensson Birte

Abstract excerpt

The barley alpha-amylase/subtilisin inhibitor (BASI) inhibits alpha-amylase 2 (AMY2) with subnanomolar affinity. The contribution of selected side chains of BASI to this high affinity is discerned in this study, and binding to other targets is investigated. Seven BASI residues along the AMY2-BASI interface and four residues in the putative protease-binding loop on the opposite side of the inhibitor were mutated....

Topics

Amino Acid Sequence
Binding Sites
Calcium
Catalytic Domain
DNA Mutational Analysis
Electrophoresis, Polyacrylamide Gel
Glycoside Hydrolases
Hordeum
Isoelectric Focusing
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Mutation

Peptide Hydrolases

Protein Binding

Protein Conformation

Protein Folding

Protein Structure, Secondary

Source

Identifiers

PMID: 15657043
DOI: 10.1074/jbc.M412222200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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