Relating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes. - Wikidata - awgldk - TriplyDB

Relating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes.

Relating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes.

http://www.wikidata.org/entity/Q38086666

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Comparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.A conformational sampling model for radical catalysis in pyridoxal phosphate- and cobalamin-dependent enzymes.The photochemical mechanism of a B12-dependent photoreceptor protein Large-scale domain motions and pyridoxal-5'-phosphate assisted radical catalysis in coenzyme B12-dependent aminomutases.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.Probing reversible chemistry in coenzyme B12 -dependent ethanolamine ammonia lyase with kinetic isotope effects.Dynamic, electrostatic model for the generation and control of high-energy radical intermediates by a coenzyme B₁₂-dependent enzyme.The photochemistry and photobiology of vitamin B12.Photolytic properties of cobalamins: a theoretical perspective.Coenzyme B12 can be produced by engineered Escherichia coli under both anaerobic and aerobic conditions.

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P2860

Relating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes.

http://www.wikidata.org/entity/Q38086666

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Relating localized protein mot ...... oenzyme B₁₂-dependent enzymes.

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Relating localized protein mot ...... oenzyme B₁₂-dependent enzymes.

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Relating localized protein mot ...... oenzyme B₁₂-dependent enzymes.

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Colin Levy

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Nigel S Scrutton

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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

A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase

Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase

The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer

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

B12 cofactors directly stabilize an mRNA regulatory switch

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10.1111/FEBS.12223

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2013-03-21T00:00:00Z

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