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Article

A single mutation Gln142Lys doubles the catalytic activity of VPR, a cold adapted subtilisin-like serine proteinase.

Biochimica et biophysica acta - 1 Oct 2016

Óskarsson Kristinn R, Nygaard Mads, Ellertsson Brynjar Ö, Thorbjarnardottir Sigríður H, Papaleo Elena, Kristjánsson Magnús M

Abstract excerpt

Structural comparisons of the cold adapted subtilase VPR and its thermophilic homologue, aqualysin I (AQUI) indicated the presence of additional salt bridges in the latter. Few of those appear to contribute significantly to thermal stability of AQUI. This includes a putative salt bridge between residues Lys142 and Glu172 as its deletion did not have any significant effect on its stability or activity (Jónsdóttir...

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Identifiers

PMID: 27456266
DOI: 10.1016/j.bbapap.2016.07.003

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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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