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Recombinant shewasin D and shewasin A specificity preferences profiled by proteomic identification of protease cleavage sites (PICS)

ABSTRACT: We determined the specificity preferences of both recombinant shewasin D and shewasin A (pepsin-like aspartic proteases from S. denitrificans and S. amazonensis, respectively) using proteome-derived peptide libraries and observed remarkable similarities between both shewasins and eukaryotic pepsins, in particular with BACE-1 thereby confirming their phylogenetic proximity. We further observed subtle differences in sequence preferences at several positions, suggesting variations in their subsite binding pockets.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture, Blood Cell, Monocyte, Blood

DISEASE(S): Acute Leukemia

SUBMITTER: Rui Cruz

LAB HEAD: Isaura Simões

PROVIDER: PXD003078 | Pride | 2016-04-05

REPOSITORIES: Pride

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Enzymatic properties, evidence for in vivo expression, and intracellular localization of shewasin D, the pepsin homolog from Shewanella denitrificans.

Leal Ana Rita AR Cruz Rui R Bur Daniel D Huesgen Pitter F PF Faro Rosário R Manadas Bruno B Wlodawer Alexander A Faro Carlos C Simões Isaura I

Scientific reports 20160331

The widespread presence of pepsin-like enzymes in eukaryotes together with their relevance in the control of multiple biological processes is reflected in the large number of studies published so far for this family of enzymes. By contrast, pepsin homologs from bacteria have only recently started to be characterized. The work with recombinant shewasin A from Shewanella amazonensis provided the first documentation of this activity in prokaryotes. Here we extend our studies to shewasin D, the peps ...[more]

PMID: 27029611

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