Proteomics

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Specificity profiling of LysargiNase in comparison to trypsin

ABSTRACT: Protease cleavage site preferences of LysargiNase (former name: ulilysin) and trypsin were tested using proteome-derived peptide libraries (Schilling et al Nature Protocols 2011)

INSTRUMENT(S): QSTAR

ORGANISM(S): Escherichia Coli

TISSUE(S): Cell Culture

SUBMITTER: Pitter Huesgen  

LAB HEAD: Christopher M Overall

PROVIDER: PXD001122 | Pride | 2014-12-16

REPOSITORIES: Pride

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Dataset's files

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95073EcoCT.mzXML Mzxml
95073EcoCT.wiff Wiff
95073EcoCU.mzXML Mzxml
95073EcoCU.wiff Wiff
95081EcoGT.mzXML Mzxml
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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]

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