Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF. - Wikidata - awgldk - TriplyDB

Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.

Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.

http://www.wikidata.org/entity/Q37705601

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Switch I-dependent allosteric signaling in a G-protein chaperone-B12 enzyme complex.

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P2860

Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.

http://www.wikidata.org/entity/Q37705601

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 27 January 2017

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Cofactor Editing by the G-prot ...... s the Radical B12 Enzyme IcmF.

@en

Cofactor Editing by the G-prot ...... s the Radical B12 Enzyme IcmF.

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type

label

Cofactor Editing by the G-prot ...... s the Radical B12 Enzyme IcmF.

@en

Cofactor Editing by the G-prot ...... s the Radical B12 Enzyme IcmF.

@nl

prefLabel

Cofactor Editing by the G-prot ...... s the Radical B12 Enzyme IcmF.

@en

Cofactor Editing by the G-prot ...... s the Radical B12 Enzyme IcmF.

@nl

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JBC.M117.775957

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Journal of Biological Chemistry

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Cofactor Editing by the G-prot ...... es the Radical B12 Enzyme IcmF

@en

P2093

Derrell Chapman

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Kurt Warncke

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Ruma Banerjee

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Umar T Twahir

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

Zhu Li

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

P2860

Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements.

Structure of ATP-bound human ATP:cobalamin adenosyltransferase

Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP

Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduria

Structural and functional analyses of the human-type corrinoid adenosyltransferase (PduO) from Lactobacillus reuteri

Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate

Residue Phe112 of the Human-Type Corrinoid Adenosyltransferase (PduO) Enzyme of Lactobacillus reuteri Is Critical to the Formation of the Four-Coordinate Co(II) Corrinoid Substrate and to the Activity of the Enzyme † , ‡

A switch III motif relays signaling between a B12 enzyme and its G-protein chaperone

Autoinhibition and Signaling by the Switch II Motif in the G-protein Chaperone of a Radical B12 Enzyme

Novel B(12)-dependent acyl-CoA mutases and their biotechnological potential.

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3977-3987

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scholarly article

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10.1074/JBC.M117.775957

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P433

10

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292

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Valentin Cracan

Kenichi Kitanishi

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2017-01-27T00:00:00Z

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28130442

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5354503

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