Solid-to-solid peptide synthesis by glycyl endopeptidase

Glycyl endopeptidase catalysed solid-to-solid synthesis can be carried out efficiently for the model peptides Z-Gly-Phe-NH2, Z-Gly-Leu-NH2, Z-Gly-Tyr-NH2and Z-Gly-Tyr-OEt. A small excess of acyl donor Z-Gly improved both the initial rate and final yield, whereas an excess of nucleophile Phe-NH2preve...

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Main Authors:	Phanuphong Chaiwut, Pawinee Kanasawud, Peter J. Halling
Format:	Journal
Published:	2018
Subjects:	Biochemistry, Genetics and Molecular Biology Immunology and Microbiology
Online Access:	https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33847354740&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/60913
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Institution:	Chiang Mai University

id	th-cmuir.6653943832-60913
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spelling	th-cmuir.6653943832-609132018-09-10T04:05:25Z Solid-to-solid peptide synthesis by glycyl endopeptidase Phanuphong Chaiwut Pawinee Kanasawud Peter J. Halling Biochemistry, Genetics and Molecular Biology Immunology and Microbiology Glycyl endopeptidase catalysed solid-to-solid synthesis can be carried out efficiently for the model peptides Z-Gly-Phe-NH2, Z-Gly-Leu-NH2, Z-Gly-Tyr-NH2and Z-Gly-Tyr-OEt. A small excess of acyl donor Z-Gly improved both the initial rate and final yield, whereas an excess of nucleophile Phe-NH2prevented reaction. The highest conversion was achieved when using a substrate molar ratio (Z-Gly:Phe-NH2) of 2:1. Including solid cysteine in the reaction mixture improved both initial rate and final conversion, probably by protecting the enzyme from oxidation. The reasons why conversion to Z-Gly-Phe-NH2stopped at around 83% were investigated. Entrapment of residual solid starting material did not seem significant, while autolysis and inactivation of glycyl endopeptidase in the reaction mixture during catalysis was important. The role of chemical equilibrium position was less clear. © 2006 Elsevier Inc. All rights reserved. 2018-09-10T04:01:15Z 2018-09-10T04:01:15Z 2007-03-05 Journal 01410229 2-s2.0-33847354740 10.1016/j.enzmictec.2006.07.042 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33847354740&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/60913
institution	Chiang Mai University
building	Chiang Mai University Library
country	Thailand
collection	CMU Intellectual Repository
topic	Biochemistry, Genetics and Molecular Biology Immunology and Microbiology
spellingShingle	Biochemistry, Genetics and Molecular Biology Immunology and Microbiology Phanuphong Chaiwut Pawinee Kanasawud Peter J. Halling Solid-to-solid peptide synthesis by glycyl endopeptidase
description	Glycyl endopeptidase catalysed solid-to-solid synthesis can be carried out efficiently for the model peptides Z-Gly-Phe-NH2, Z-Gly-Leu-NH2, Z-Gly-Tyr-NH2and Z-Gly-Tyr-OEt. A small excess of acyl donor Z-Gly improved both the initial rate and final yield, whereas an excess of nucleophile Phe-NH2prevented reaction. The highest conversion was achieved when using a substrate molar ratio (Z-Gly:Phe-NH2) of 2:1. Including solid cysteine in the reaction mixture improved both initial rate and final conversion, probably by protecting the enzyme from oxidation. The reasons why conversion to Z-Gly-Phe-NH2stopped at around 83% were investigated. Entrapment of residual solid starting material did not seem significant, while autolysis and inactivation of glycyl endopeptidase in the reaction mixture during catalysis was important. The role of chemical equilibrium position was less clear. © 2006 Elsevier Inc. All rights reserved.
format	Journal
author	Phanuphong Chaiwut Pawinee Kanasawud Peter J. Halling
author_facet	Phanuphong Chaiwut Pawinee Kanasawud Peter J. Halling
author_sort	Phanuphong Chaiwut
title	Solid-to-solid peptide synthesis by glycyl endopeptidase
title_short	Solid-to-solid peptide synthesis by glycyl endopeptidase
title_full	Solid-to-solid peptide synthesis by glycyl endopeptidase
title_fullStr	Solid-to-solid peptide synthesis by glycyl endopeptidase
title_full_unstemmed	Solid-to-solid peptide synthesis by glycyl endopeptidase
title_sort	solid-to-solid peptide synthesis by glycyl endopeptidase
publishDate	2018
url	https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33847354740&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/60913
_version_	1681425523677331456

Solid-to-solid peptide synthesis by glycyl endopeptidase

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