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Article

Demonstration of the importance and usefulness of manipulating non-active-site residues in protein design.

Journal of biochemistry - 1 Jun 2001

Shimotohno A, Oue S, Yano T, Kuramitsu S, Kagamiyama H

Abstract excerpt

Do non-active-site residues participate in protein function in a more direct way than just by holding the static framework of the protein molecule? If so, how important are they? As a model to answer these questions, ATB17, which is a mutant of aspartate aminotransferase created by directed evolution, is an ideal system because it shows a 10(6)-fold increase in the catalytic efficiency for valine but most of its...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11388910
DOI: 10.1093/oxfordjournals.jbchem.a002941

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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