Format

Send to

Choose Destination
Appl Microbiol Biotechnol. 2017 May;101(10):4129-4137. doi: 10.1007/s00253-017-8186-8. Epub 2017 Feb 22.

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

Author information

1
Service de Dermatologie, Laboratoire de Mycologie, BT422, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.
2
Laboratoire des Catecholamines et Peptides, Service de Biom├ędecine, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.
3
Centre for Integrative Biology, University of Trento, Trento, Italy.
4
Protein Analysis Facility, Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland.
5
Service de Dermatologie, Laboratoire de Mycologie, BT422, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland. Michel.Monod@chuv.ch.

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:

Angiotensin I; Aspergillus oryzae; Bradykinin; Proline-Xaa carboxypeptidase; Prolyl peptidase

PMID:
28229206
DOI:
10.1007/s00253-017-8186-8
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center