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Characterization of LysargiNase peptide fragmentation

ABSTRACT: Comparison of Lyarginase and tryptic digests with regard to fragmentation behaviour/effect of inclusing a ion in peptide assignment scoring

INSTRUMENT(S): QSTAR

ORGANISM(S): Escherichia Coli

SUBMITTER: Pitter Huesgen

LAB HEAD: Christopher M Overall

PROVIDER: PXD001378 | Pride | 2014-12-16

REPOSITORIES: Pride

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LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification.

Huesgen Pitter F PF Lange Philipp F PF Rogers Lindsay D LD Solis Nestor N Eckhard Ulrich U Kleifeld Oded O Goulas Theodoros T Gomis-Rüth F Xavier FX Overall Christopher M CM

Nature methods 20141124 1

To improve proteome coverage and protein C-terminal identification, we characterized the Methanosarcina acetivorans thermophilic proteinase LysargiNase, which cleaves before lysine and arginine up to 55 °C. Unlike trypsin, LysargiNase-generated peptides had N-terminal lysine or arginine residues and fragmented with b ion-dominated spectra. This improved protein C terminal-peptide identification and several arginine-rich phosphosite assignments. Notably, cleavage also occurred at methylated or di ...[more]

PMID: 25419962

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