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Autoproteolytic and Catalytic Mechanisms for the β-Aminopeptidase BapA-A Member of the Ntn Hydrolase Family


Merz, Tobias; Heck, Tobias; Geueke, Birgit; Mittl, Peer R E; Briand, Christophe; Seebach, Dieter; Kohler, Hans-Peter E; Grütter, Markus G (2012). Autoproteolytic and Catalytic Mechanisms for the β-Aminopeptidase BapA-A Member of the Ntn Hydrolase Family. Structure, 20(11):1850-1860.

Abstract

The β-aminopeptidase BapA from Sphingosinicella xenopeptidilytica belongs to the N-terminal nucleophile (Ntn) hydrolases of the DmpA-like family and has the unprecedented property of cleaving N-terminal β-amino acid residues from peptides. We determined the crystal structures of the native (αβ)(4) heterooctamer and of the 153 kDa precursor homotetramer at a resolution of 1.45 and 1.8 Å, respectively. These structures together with mutational analyses strongly support mechanisms for autoproteolysis and catalysis that involve residues Ser250, Ser288, and Glu290. The autoproteolytic mechanism is different from the one so far described for Ntn hydrolases. The structures together with functional data also provide insight into the discriminating features of the active site cleft that determine substrate specificity.

Abstract

The β-aminopeptidase BapA from Sphingosinicella xenopeptidilytica belongs to the N-terminal nucleophile (Ntn) hydrolases of the DmpA-like family and has the unprecedented property of cleaving N-terminal β-amino acid residues from peptides. We determined the crystal structures of the native (αβ)(4) heterooctamer and of the 153 kDa precursor homotetramer at a resolution of 1.45 and 1.8 Å, respectively. These structures together with mutational analyses strongly support mechanisms for autoproteolysis and catalysis that involve residues Ser250, Ser288, and Glu290. The autoproteolytic mechanism is different from the one so far described for Ntn hydrolases. The structures together with functional data also provide insight into the discriminating features of the active site cleft that determine substrate specificity.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2012
Deposited On:03 Jan 2013 12:29
Last Modified:05 Apr 2016 16:11
Publisher:Cell Press
ISSN:0969-2126
Publisher DOI:https://doi.org/10.1016/j.str.2012.07.017
PubMed ID:22980995

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