Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17-16 laccase influence enzymatic properties.
axial bond
copper
kinetic analysis
laccase
redox potential
site-directed mutation
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
11
03
2019
revised:
20
03
2019
accepted:
22
03
2019
pubmed:
10
4
2019
medline:
13
11
2019
entrez:
10
4
2019
Statut:
ppublish
Résumé
Laccase is a multi-copper oxidase which oxidizes substrate at the type 1 copper site, simultaneously coupling the reduction of dioxygen to water at the trinuclear copper center. In this study, we used site-directed mutagenesis to study the effect of axial bonds between the metal and amino acid residue side chains in lacTT. Our kinetic and spectral data showed that the replacement of the axial residue with non-coordinating residues resulted in higher efficiency (k
Identifiants
pubmed: 30964606
doi: 10.1002/2211-5463.12633
pmc: PMC6487685
doi:
Substances chimiques
Bacterial Proteins
0
Laccase
EC 1.10.3.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
986-995Informations de copyright
© 2019 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.
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