Kinetic relationships with processivity in Serratia marcescens family 18 glycoside hydrolases.


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
01 01 2020
Historique:
received: 04 10 2019
accepted: 10 10 2019
pubmed: 21 10 2019
medline: 7 7 2020
entrez: 21 10 2019
Statut: ppublish

Résumé

In nature, recalcitrant polysaccharides such as chitin and cellulose are degraded by glycoside hydrolases (GH) that act synergistically through different modes of action including attack from reducing-end and nonreducing-end (exo-mode) and random (endo-mode) on single polysaccharide chains. Both modes can be combined with a processive mechanism where the GH remain bound to the polysaccharide to perform multiple catalytic steps before dissociation into the solution. In this work, we have determined association rate constants and their activation paramaters for three co-evolved GHs from Serratia marcescens (SmChiA, SmChiB, and SmChiC) with an oligomeric substrate. Interestingly, we observe a positive correlation between the association rate constants and processive ability for the GHs. Previously, a positive correlation has been observed between substrate binding affinity and processive ability. SmChiA with highest processive ability of the three GHs bind with a k

Identifiants

pubmed: 31629467
pii: S0006-291X(19)31982-5
doi: 10.1016/j.bbrc.2019.10.089
pii:
doi:

Substances chimiques

Glycoside Hydrolases EC 3.2.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

120-124

Informations de copyright

Copyright © 2019 Elsevier Inc. All rights reserved.

Auteurs

Anne Grethe Hamre (AG)

Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, N-1432 Ås, Norway.

Morten Sørlie (M)

Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, N-1432 Ås, Norway. Electronic address: morten.sorlie@nmbu.no.

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