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Article

Mutation of active site residues of insulin-degrading enzyme alters allosteric interactions.

The Journal of biological chemistry - 6 May 2005

Song Eun Suk, Daily Abigail, Fried Michael G, Juliano Maria Aparecida, Juliano Luiz, Hersh Louis B

Abstract excerpt

The active site glutamate (Glu(111)) and the active site histidine (His(112)) of insulin-degrading enzyme (IDE) were mutated. These mutant enzymes exhibit, in addition to a large decrease in catalytic activity, a change in the substrate-velocity response from a sigmoidal one seen with the native enzyme (Hill coefficient > 2), to a hyperbolic response. With...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 15749695
DOI: 10.1074/jbc.M501896200

Genes

IDE

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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