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Article

The activity and stability of a cold-active acylaminoacyl peptidase rely on its dimerization by domain swapping.

International journal of biological macromolecules - 30 Jun 2021

Mangiagalli Marco, Barbiroli Alberto, Santambrogio Carlo, Ferrari Cristian, Nardini Marco, Lotti Marina, Brocca Stefania

Abstract excerpt

The study of enzymes from extremophiles arouses interest in Protein Science because of the amazing solutions these proteins adopt to cope with extreme conditions. Recently solved, the structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) pinpoints a mechanism of dimerization unusual for this class of enzymes. The quaternary structure of SpAAP relies on a domain-swapping...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33775759
DOI: 10.1016/j.ijbiomac.2021.03.150

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