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Article

The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.

The Journal of biological chemistry - 4 Oct 2013

Weber Brandon W, Kimani Serah W, Varsani Arvind, Cowan Donald A, Hunter Roger, Venter Gerhard A, Gumbart James C, Sewell B Trevor

Abstract excerpt

All known nitrilase superfamily amidase and carbamoylase structures have an additional glutamate that is hydrogen bonded to the catalytic lysine in addition to the Glu, Lys, Cys "catalytic triad." In the amidase from Geobacillus pallidus, mutating this glutamate (Glu-142) to a leucine or aspartate renders the enzyme inactive. X-ray crystal structure determination shows that the structural integrity of the enzyme...

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Identifiers

PMID: 23946488
DOI: 10.1074/jbc.M113.503284
PMCID: PMC3789952

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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