Proteomics

Dataset Information

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LysargiNase cleavage specificity characterization

ABSTRACT: Determination of LysargiNase and tryptic ckeavage efficiency at dimethylated Lys residues

INSTRUMENT(S): QSTAR

ORGANISM(S): Escherichia Coli

SUBMITTER: Pitter Huesgen  

LAB HEAD: Christopher M Overall

PROVIDER: PXD001379 | Pride | 2014-12-16

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
37144dmET.mzXML Mzxml
37144dmET.tandem.interact.pep.xls Xls
37144dmET.tandem.interact.pep.xml Pepxml
37144dmET.tandem.params Other
37144dmET.wiff Wiff
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Publications

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]