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

ABSTRACT: Data from ProteomeXchange: PXD ID: PXD001114. Experiment: LysargiNase, silac, file: LR_Ulilysin_PMA_A1_121126.mzml. Published as part of . From the Abstract: {{i}} 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 dimethylated lysine and arginine, facilitating detection of these epigenetic modifications. {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Homo_sapiens_viruses, Human_female

DISEASE(S): Not Available

SUBMITTER: Huesgen PF, et al.  

PROVIDER: GPM32310005457 | GPMDB |

REPOSITORIES: GPMDB