AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae.

Details

Serval ID
serval:BIB_B070804CB27F
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae.
Journal
Applied microbiology and biotechnology
Author(s)
Salamin K., Eugster P.J., Jousson O., Waridel P., Grouzmann E., Monod M.
ISSN
1432-0614 (Electronic)
ISSN-L
0175-7598
Publication state
Published
Issued date
05/2017
Peer-reviewed
Oui
Volume
101
Number
10
Pages
4129-4137
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
Prolyl peptidases of the MEROPS S28 family are of particular interest because they are key enzymes in the digestion of proline-rich peptides. A BLAST analysis of the Aspergillus oryzae genome revealed sequences coding for four proteases of the S28 family. Three of these proteases, AoS28A, AoS28B, and AoS28C, were previously characterized as acidic prolyl endopeptidases. The fourth protease, AoS28D, showed high sequence divergence with other S28 proteases and belongs to a phylogenetically distinct cluster together with orthologous proteases from other Aspergillus species. The objective of the present paper was to characterize AoS28D protease in terms of substrate specificity and activity. AoS28D produced by gene overexpression in A. oryzae and in Pichia pastoris was a 70-kDa glycoprotein with a 10-kDa sugar moiety. In contrast with other S28 proteases, AoS28D did not hydrolyze internal Pro-Xaa bonds of several tested peptides. Similarly, to human lysosomal Pro-Xaa carboxypeptidase, AoS28D demonstrated selectivity for cleaving C-terminal Pro-Xaa bonds which are resistant to carboxypeptidases of the S10 family concomitantly secreted by A. oryzae. Therefore, AoS28D could act in synergy with these enzymes during sequential degradation of a peptide from its C-terminus.

Keywords
Angiotensins/metabolism, Aspergillus oryzae/enzymology, Aspergillus oryzae/genetics, Aspergillus oryzae/metabolism, Bradykinin/metabolism, Carboxypeptidases/chemistry, Carboxypeptidases/genetics, Carboxypeptidases/metabolism, Genome, Fungal, Humans, Hydrogen-Ion Concentration, Hydrolysis, Peptide Hydrolases/genetics, Peptide Hydrolases/metabolism, Peptides/chemistry, Peptides/metabolism, Pichia/genetics, Proline/metabolism, Substrate Specificity, Angiotensin I, Aspergillus oryzae, Bradykinin, Proline-Xaa carboxypeptidase, Prolyl peptidase
Pubmed
Web of science
Create date
07/03/2017 20:40
Last modification date
20/08/2019 15:19
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