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Article

Stability for function trade-offs in the enolase superfamily "catalytic module".

Biochemistry - 12 Jun 2007

Nagatani Ray A, Gonzalez Ana, Shoichet Brian K, Brinen Linda S, Babbitt Patricia C

Abstract excerpt

Enzyme catalysis reflects a dynamic interplay between charged and polar active site residues that facilitate function, stabilize transition states, and maintain overall protein stability. Previous studies show that substituting neutral for charged residues in the active site often significantly stabilizes a protein, suggesting a stability trade-off for functionality. In the enolase superfamily, a set of conserved...

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Identifiers

PMID: 17503785
DOI: 10.1021/bi700507d

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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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