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Literature summary for 3.4.21.50 extracted from

  • Kishimoto, T.; Kondo, J.; Takai-Igarashi, T.; Tanaka, H.
    Accurate mass comparison coupled with two endopeptidases enables identification of protein termini (2011), Proteomics, 11, 485-489.
    View publication on PubMed

Application

Application Comment Organism
analysis method for identification of both the amino and the carboxyl termini of proteins. The method independently uses two proteases, Lys-C and peptidyl-Lys metalloendopeptidase Lys-N, to digest proteins, followed by LC-MS/MS analysis of the two digests. Terminal peptides can be identified as the amino terminal peptide of a protein in Lys-C digest is one lysine residue mass heavier than that in Lys-N digest, the carboxyl terminal peptide in Lys-N digest is one lysine residue mass heavier than that in Lys-C digest, and all internal peptides give exactly the same molecular masses in both the Lys-C and the Lys-N digest, although amino acid sequences of Lys-C and Lys-N peptides are different. Acetylation on N-terminus and protein isoforms, which have different termini, is also determined Achromobacter lyticus

Organism

Organism UniProt Comment Textmining
Achromobacter lyticus
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Achromobacter lyticus
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