UNSPECIFIED (2006) Structure-function properties of prolyl oligopeptidase family enzymes. In: 1st Latin-American-Protein-Society Meeting, NOV 08-12, 2004, Angra dos Reis, BRAZIL.

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Abstract

Prolyl oligopeptidase family enzymes regulate the activity of biologically active peptides and peptide hormones, and they are implicated in diseases, including amnesia, depression, diabetes, and trypanosomiasis. Distinctively, these enzymes hydrolyze only relatively short peptide substrates, while large structured peptides and proteins are not usually cleaved. Prolyl oligopeptidase has a C-terminal alpha/beta-hydrolase catalytic domain that is similar to lipases and esterases. An N-terminal beta-propeller domain regulates access to the buried active site, explaining the observed oligopeptidase activity. The catalytic and regulatory mechanisms have been investigated using a combination of X-ray crystallography, site-directed mutagenesis, and enzyme kinetic measurements. Crystal structures have now been determined for representative members of three of the four subfamilies and are facilitating a better understanding of the structure-function properties of these physiologically and pharmaceutically important enzymes.

Item Type:	Conference Item (UNSPECIFIED)
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	CELL BIOCHEMISTRY AND BIOPHYSICS
Publisher:	HUMANA PRESS INC
ISSN:	1085-9195
Date:	2006
Volume:	44
Number:	3
Number of Pages:	17
Page Range:	pp. 349-365
Publication Status:	Published
Title of Event:	1st Latin-American-Protein-Society Meeting
Location of Event:	Angra dos Reis, BRAZIL
Date(s) of Event:	NOV 08-12, 2004
URI:	http://wrap.warwick.ac.uk/id/eprint/33588

Data sourced from Thomson Reuters' Web of Knowledge

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