Proteomics

Dataset Information

0

Cleavage preference of metalloprotease EA1


ABSTRACT: The cleavage preference of the thermophilic metalloprotease from Geobacillus sp. EA1 was characterised using mass spectrometry, confirming its similarity to thermolysin in preferring P1’ hydrophobic amino acids. While EA1 showed similar efficiencies for cleavage of short peptides with one of six hydrophobic amino acids at the P1’ position, thermolysin showed marked preference for leucine. A single amino acid difference in the S1’ pocket of these similar enzymes provides a rationale for this difference. A variant of EA1 (F133L) had intermediary preference, suggesting that approximately half the difference in preference is attributable to this single amino acid change. Broader preference and higher efficiency make EA1 a superior candidate for quick digestion of varied protein substrates.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli Bacillus Thermoproteolyticus Geobacillus Sp. Eft1

SUBMITTER: Torsten Kleffmann  

LAB HEAD: Sigurd Wilbanks

PROVIDER: PXD064530 | Pride | 2025-11-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
23062_EA1Cleavage_iTRAQ.msf Msf
23062_EA1Cleavage_iTRAQ.mzML Mzml
23062_EA1Cleavage_iTRAQ.pep.xml Pepxml
23062_EA1Cleavage_iTRAQ.wiff Wiff
23062_EA1Cleavage_iTRAQ.wiff.scan Wiff
Items per page:
1 - 5 of 6

Similar Datasets

2019-07-29 | PXD009201 | Pride
2014-10-30 | PXD001217 | Pride
2025-05-06 | PXD048501 | Pride
2018-04-26 | PXD007556 | Pride
2015-10-19 | PXD002474 | Pride
2020-03-19 | PXD010355 | Pride
2024-07-18 | PXD048224 | Pride
2016-07-19 | PXD002532 | Pride
2020-08-11 | PXD017769 | Pride
2018-10-17 | PXD006884 | Pride