Quantum Mechanics/Molecular Mechanics Studies on the Mechanism of Action of Cofactor Pyridoxal 5′-Phosphate in Ornithine 4,5-Aminomutase
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.Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.Application of quantum mechanics/molecular mechanics methods in the study of enzymatic reaction mechanisms
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Quantum Mechanics/Molecular Mechanics Studies on the Mechanism of Action of Cofactor Pyridoxal 5′-Phosphate in Ornithine 4,5-Aminomutase
description
im Juli 2014 veröffentlichter wissenschaftlicher Artikel
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scientific article published on 22 July 2014
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wetenschappelijk artikel
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наукова стаття, опублікована в липні 2014
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name
Quantum Mechanics/Molecular Me ...... e in Ornithine 4,5-Aminomutase
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Quantum Mechanics/Molecular Me ...... e in Ornithine 4,5-Aminomutase
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type
label
Quantum Mechanics/Molecular Me ...... e in Ornithine 4,5-Aminomutase
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Quantum Mechanics/Molecular Me ...... e in Ornithine 4,5-Aminomutase
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prefLabel
Quantum Mechanics/Molecular Me ...... e in Ornithine 4,5-Aminomutase
@en
Quantum Mechanics/Molecular Me ...... e in Ornithine 4,5-Aminomutase
@nl
P2860
P50
P356
P1476
Quantum mechanics/molecular me ...... e in ornithine 4,5-aminomutase
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P2093
Michael J. Sutcliffe
Nigel S. Scrutton
P2860
P304
11390-11401
P356
10.1002/CHEM.201402759
P407
P577
2014-07-22T00:00:00Z