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Article

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.

The FEBS journal - 1 Dec 2016

Brocca Stefania, Ferrari Cristian, Barbiroli Alberto, Pesce Alessandra, Lotti Marina, Nardini Marco

Abstract excerpt

Life in cold environments requires an overall increase in the flexibility of macromolecular and supramolecular structures to allow biological processes to take place at low temperature. Conformational flexibility supports high catalytic rates of enzymes in the cold but in several cases is also a cause of instability. The three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 27739253
DOI: 10.1111/febs.13925

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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