Endoproteinase Lys-C is a
protease
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalysis, catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products ...
that cleaves proteins on the
C-terminal
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When t ...
side of
lysine
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. Lysine contains an α-amino group (which is in the protonated form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group ( ...
residues. This enzyme is naturally found in the bacterium ''
Lysobacter enzymogenes
The genus ''Lysobacter'' belongs to the family Xanthomonadaceae within the Gammaproteobacteria and includes at least 46 named species, including: ''Lysobacter enzymogenes, L. antibioticus, L. gummosus, L. brunescens, L. defluvii, L. niabensis, L ...
'' and is commonly used in
protein sequencing
Protein sequencing is the practical process of determining the amino acid sequence of all or part of a protein or peptide. This may serve to identify the protein or characterize its post-translational modifications. Typically, partial sequencing o ...
. Lys-C activity is optimal in the
pH range 7.0 - 9.0.
See also
*
Trypsin
Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the dig ...
*
Lys-N
References
Bacterial enzymes
Proteases
EC 3.4
Post-translational modification
Proteomics
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