Dynamic, electrostatic model for the generation and control of high-energy radical intermediates by a coenzyme B₁₂-dependent enzyme.

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http://www.wikidata.org/entity/Q41865658

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

@yue

2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

Dynamic, electrostatic model f ...... coenzyme B₁₂-dependent enzyme.

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type

Item

label

Dynamic, electrostatic model f ...... coenzyme B₁₂-dependent enzyme.

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prefLabel

Dynamic, electrostatic model f ...... coenzyme B₁₂-dependent enzyme.

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P1476

Dynamic, electrostatic model f ...... coenzyme B₁₂-dependent enzyme

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P2093

Henry J Russell

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Zhi-Gang Chen

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P2860

A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase

Crystal structure of substrate complexes of methylmalonyl-CoA mutase

Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase

Large-scale Domain Dynamics and Adenosylcobalamin Reorientation Orchestrate Radical Catalysis in Ornithine 4,5-Aminomutase

Crystal Structures of Ethanolamine Ammonia-lyase Complexed with Coenzyme B12 Analogs and Substrates

Structures of the Human GTPase MMAA and Vitamin B 12 -dependent Methylmalonyl-CoA Mutase and Insight into Their Complex Formation

Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism

Hydrogen bonds guide the short-lived 5'-deoxyadenosyl radical to the place of action

Critical role of arginine 160 of the EutB protein subunit for active site structure and radical catalysis in coenzyme B12-dependent ethanolamine ammonia-lyase.

Characterization of protein contributions to cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase by using photolysis in the ternary complex.

P304

1529-1533

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scholarly article

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10.1002/CBIC.201300420

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2013-08-19T00:00:00Z

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255986643

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23959797

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4155860

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