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Stability and kinetic studies on recombinant and variant forms of human pyroglutamyl peptidase I and a single-site variant.

Mtawae, Karima, O'Connor, Brendan orcid logoORCID: 0000-0002-6857-1614 and Ó Fágáin, Ciarán (2007) Stability and kinetic studies on recombinant and variant forms of human pyroglutamyl peptidase I and a single-site variant. In: Biotechnology; Research ,Technology & Applications. Nova Science, pp. 121-142. ISBN 9781604569018

Abstract
Human brain pyroglutamyl peptidase (PAPI; EC 3.4.19.3) is an omega exopeptidase which cleaves pyroglutamic acid from the N-terminus of bioactive peptides and proteins. It plays an important role in the processing and degradation of regulatory peptides such as thyrotropin releasing hormone (TRH) and luteinizing hormone releasing hormone (LHRH). To gain further insights into its performance in vivo and suggest possible applications, such as peptide processing or sequencing, this study focuses on the in vitro stability properties and Michaelis- Menten kinetics of the recombinant wild type enzyme and a single-site mutant, Tyr147→Phe (Y147F).
Metadata
Item Type:Book Section
Refereed:Yes
Additional Information:Your enquiry has been successfully sent to Nova Publishers. 6/3/2013 - No reply
Subjects:Biological Sciences > Biotechnology
Biological Sciences > Biochemistry
Biological Sciences > Molecular biology
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Research Initiatives and Centres > National Centre for Sensor Research (NCSR)
Publisher:Nova Science
Official URL:https://www.novapublishers.com
Copyright Information:© 2007 Nova Science
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 License. View License
Funders:Enterprise Ireland
ID Code:17807
Deposited On:18 Apr 2013 13:46 by Brendan O'connor . Last Modified 18 Oct 2018 13:24
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