Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties

DSpace Repository

Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties

Show full item record

Files for download

Find Full text There are no files associated with this item..

Facebook

Simple item record

Publication Article, peer reviewed scientific
Title Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties
Author(s) Osipov, Evgeny ; Polyakov, Konstantin ; Kittl, Roman ; Shleev, Sergey ; Dorovatovsky, Pavel ; Tikhonova, Tamara ; Hann, Stephan ; Ludwig, Roland ; Popov, Vladimir
Date 2014
English abstract
Laccases are members of a large family of multicopper oxidases that catalyze the oxidn. of a wide range of org. and inorg. substrates accompanied by the redn. of dioxygen to water. These enzymes contain four Cu atoms per mol. organized into three sites: T1, T2 and T3. In all laccases, the T1 copper ion is coordinated by two histidines and one cysteine in the equatorial plane and is covered by the side chains of hydrophobic residues in the axial positions. The redox potential of the T1 copper ion influences the enzymic reaction and is detd. by the nature of the axial ligands and the structure of the second coordination sphere. In this work, the laccase from the ascomycete Botrytis aclada was studied, which contains conserved Ile491 and nonconserved Leu499 residues in the axial positions. The three-​dimensional structures of the wild-​type enzyme and the L499M mutant were detd. by X-​ray crystallog. at 1.7 Å resoln. Crystals suitable for X-​ray anal. could only be grown after deglycosylation. Both structures did not contain the T2 copper ion. The catalytic properties of the enzyme were characterized and the redox potentials of both enzyme forms were detd.: E 0 = 720 and 580 mV for the wild-​type enzyme and the mutant, resp. Since the structures of the wild-​type and mutant forms are very similar, the change in the redox potential can be related to the L499M mutation in the T1 site of the enzyme.
DOI http://dx.doi.org/10.1107/S1399004714020380 (link to publisher's fulltext)
Publisher International Union of Crystallography
Host/Issue Acta Crystallographica. Section D, Biological Crystallography;11
Volume 70
ISSN 1399-0047
Pages 2913-2923
Language eng (iso)
Subject(s) Sciences
Research Subject Categories::NATURAL SCIENCES
Handle http://hdl.handle.net/2043/18166 (link to this page)

This item appears in the following Collection(s)

Show full item record

Search


Browse

My Account

Statistics