A single amino acid substitution within catalytically non-active N-terminal domain of catechol 2,3-dioxygenase (C23O) increases enzyme activity towards 4-chlorocatechol-Reference-Cited by-同舟云学术

A single amino acid substitution within catalytically non-active N-terminal domain of catechol 2,3-dioxygenase (C23O) increases enzyme activity towards 4-chlorocatechol

Published:2015-12 Issue: Volume:122 Page:64-71
ISSN:1381-1177
Container-title:Journal of Molecular Catalysis B: Enzymatic
language:en
Short-container-title:Journal of Molecular Catalysis B: Enzymatic

Author:

Hupert-Kocurek Katarzyna^ORCID,Wojcieszyſska Danuta,Guzik Urszula,Borowski Tomasz

Publisher

Elsevier BV

Subject

Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis

Reference54 articles.

1. Phenol degradation by Rhodococcus opacus strain 1G

2. Non-heme iron-dependent dioxygenases: unravelling catalytic mechanisms for complex enzymatic oxidations

3. An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2

4. Evolutionary relationships among extradiol dioxygenases

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Engineering non-conservative substrate recognition sites of extradiol dioxygenase: Computation guided design to diversify and accelerate degradation of aromatic compounds;International Journal of Biological Macromolecules;2024-04

2. Degradation Mechanism of 2,4-Dichlorophenol by Fungi Isolated from Marine Invertebrates;International Journal of Molecular Sciences;2020-05-07

3. Insights into the Reaction Mechanism of Aromatic Ring Cleavage by Homogentisate Dioxygenase: A Quantum Mechanical/Molecular Mechanical Study;The Journal of Physical Chemistry B;2016-05-12