Post-translational modifications in aspartate aminotransferase from Sulfolobus solfataricus. Detection of N-e-methyllysines by mass spectrometry
about
Thermal stability and aggregation of sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications.aKMT Catalyzes Extensive Protein Lysine Methylation in the Hyperthermophilic Archaeon Sulfolobus islandicus but is Dispensable for the Growth of the Organism.Exceptional thermal stability and organic solvent tolerance of an esterase expressed from a thermophilic host.
P2860
Post-translational modifications in aspartate aminotransferase from Sulfolobus solfataricus. Detection of N-e-methyllysines by mass spectrometry
description
im Juni 1994 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published on 01 June 1994
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в червні 1994
@uk
name
Post-translational modificatio ...... yllysines by mass spectrometry
@en
Post-translational modificatio ...... yllysines by mass spectrometry
@nl
type
label
Post-translational modificatio ...... yllysines by mass spectrometry
@en
Post-translational modificatio ...... yllysines by mass spectrometry
@nl
prefLabel
Post-translational modificatio ...... yllysines by mass spectrometry
@en
Post-translational modificatio ...... yllysines by mass spectrometry
@nl
P2093
P2860
P1433
P1476
Post-translational modificatio ...... yllysines by mass spectrometry
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1994.TB18922.X
P407
P577
1994-06-01T00:00:00Z