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Article

Enzyme stabilisation due to incorporation of a fluorinated non-natural amino acid at the protein surface.

Scientific reports - 14 Nov 2024

Mukhopadhyay Arka, Li Yiwen, Cliff Matthew J, Golovanov Alexander P, Dalby Paul A

Abstract excerpt

We have previously engineered E. coli transketolase (TK) enzyme variants that accept new substrates such as aliphatic or aromatic aldehydes, and also with improved thermal stability. Irreversible aggregation is the primary mechanism of deactivation for TK in the buffers used for biocatalysis, and so we were interested in determining the extent to which this remains true in more complex media, crude cell lysates...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 39543195
DOI: 10.1038/s41598-024-79711-6
PMCID: PMC11564776

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