Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.

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Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.

P2860

Q46296304-335D9684-9172-499B-B111-7235F39C8A70

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Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.

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http://www.wikidata.org/entity/Q39689651

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@en

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@nl

type

Item

label

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@en

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@nl

prefLabel

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@en

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@nl

P1476

Interaction with the Redox Cof ...... ukaryotic Catalase-Peroxidase.

@en

P2093

Andrea Nicolussi

http://www.w3.org/2001/XMLSchema#string

Bernhard Gasselhuber

http://www.w3.org/2001/XMLSchema#string

Christa Jakopitsch

http://www.w3.org/2001/XMLSchema#string

Marcel Zamocky

http://www.w3.org/2001/XMLSchema#string

Michael M H Graf

http://www.w3.org/2001/XMLSchema#string

Xavi Carpena

http://www.w3.org/2001/XMLSchema#string

P2860

The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui

Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution

High Conformational Stability of Secreted Eukaryotic Catalase-peroxidases: ANSWERS FROM FIRST CRYSTAL STRUCTURE AND UNFOLDING STUDIES

An ionizable active-site tryptophan imparts catalase activity to a peroxidase core

Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation

2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex

Crystal structure of Mycobacterium tuberculosis catalase-peroxidase

Independent evolution of four heme peroxidase superfamilies

Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes.

Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry.

P304

3528-3541

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P31

scholarly article

P356

10.1021/ACS.BIOCHEM.6B00436

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Chris Oostenbrink

Paul G. Furtmüller

Christian Obinger

P577

2016-06-13T00:00:00Z

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P698

27293030

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P932

4928148

http://www.w3.org/2001/XMLSchema#string

Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.

about

P2860

P2860

Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932