Protein motions are coupled to the reaction chemistry in coenzyme B12-dependent ethanolamine ammonia lyase.
about
The molecular mechanism of the open-closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase.Temporally overlapped but uncoupled motions in dihydrofolate reductase catalysis.Entropic origin of cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase.Relating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes.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.Engineered control of enzyme structural dynamics and function.Photolytic properties of cobalamins: a theoretical perspective.
P2860
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P2860
Protein motions are coupled to the reaction chemistry in coenzyme B12-dependent ethanolamine ammonia lyase.
description
2012 nî lūn-bûn
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2012年の論文
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name
Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
@en
Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
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type
label
Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
@en
Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
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Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
@en
Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
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P2093
P2860
P50
P356
P1476
Protein motions are coupled to ...... nt ethanolamine ammonia lyase.
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P2093
Gregory M Greetham
Henry J Russell
Nigel S Scrutton
P2860
P304
P356
10.1002/ANIE.201202502
P407
P577
2012-08-15T00:00:00Z