Active site mutations change the cleavage specificity of neprilysin.

doi:10.1371/journal.pone.0032343

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Article

Active site mutations change the cleavage specificity of neprilysin.

PloS one - 1 Jan 2012

Sexton Travis, Hitchcook Lisa J, Rodgers David W, Bradley Luke H, Hersh Louis B

Abstract excerpt

Neprilysin (NEP), a member of the M13 subgroup of the zinc-dependent endopeptidase family is a membrane bound peptidase capable of cleaving a variety of physiological peptides. We have generated a series of neprilysin variants containing mutations at either one of two active site residues, Phe(563) and Ser(546). Among the mutants studied in detail we observed changes in their activity towards...

Topics

Catalysis
Catalytic Domain
Endopeptidases
Genetic Vectors
Humans
Hydrolysis
Insulin
Mutagenesis, Site-Directed
Mutation
Neprilysin
Peptides
Protein Binding
Protein Structure, Tertiary
Time Factors

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Identifiers

PMID: 22384224
DOI: 10.1371/journal.pone.0032343
PMCID: PMC3285688

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