Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo‐β‐lactamase into a Catechol Oxidase | Zendy

Fujieda Nobutaka | Zendy; Hasegawa Atsuhiko | Zendy; Ishihama Kenichi | Zendy; Itoh Shinobu | Zendy

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Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo‐β‐lactamase into a Catechol Oxidase

Author(s) -

Fujieda Nobutaka,

Hasegawa Atsuhiko,

Ishihama Kenichi,

Itoh Shinobu

Publication year - 2012

Publication title -

chemistry – an asian journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.18

H-Index - 106

eISSN - 1861-471X

pISSN - 1861-4728

DOI - 10.1002/asia.201101014

Subject(s) - catechol , oxidase test , reprogramming , catechol oxidase , chemistry , enzyme , mutant , biochemistry , combinatorial chemistry , hydrolysis , artificial enzyme , dioxygenase , pseudomonas , metal , stereochemistry , polyphenol oxidase , bacteria , biology , organic chemistry , cell , gene , genetics , peroxidase

Teaching metalloenzymes new tricks : An artificial type III dicopper oxidase has been developed using a hydrolytic enzyme, metallo‐β‐lactamase, as a metal‐binding platform. The triple mutant D88G/S185H/P224G redesigned by computer‐assisted structural analysis showed spectroscopic features similar to those of type III copper proteins and exhibited a high catalytic activity in the oxidation of catechols under aerobic conditions.

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