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Article

Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.

Proceedings of the National Academy of Sciences of the United States of America - 10 Apr 2007

Babady Ngolela Esther, Pang Yuan-Ping, Elpeleg Orly, Isaya Grazia

Abstract excerpt

The mitochondrial enzyme, dihydrolipoamide dehydrogenase (DLD), is essential for energy metabolism across eukaryotes. Here, conditions known to destabilize the DLD homodimer enabled the mouse, pig, or human enzyme to function as a protease. A catalytic dyad (S456-E431) buried at the homodimer interface was identified. Serine protease inhibitors and an S456A or an E431A point mutation abolished the proteolytic...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 17404228
DOI: 10.1073/pnas.0610618104
PMCID: PMC1851069

Genes

DLD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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