Titlebook: Orotidine Monophosphate Decarboxylase; A Mechanistic Dialog J.K. Lee Book 2004 Springer-Verlag Berlin Heidelberg 2004 Biochemistry.Monophos

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,Crystallographic Studies of Native and Mutant Orotidine 5′phosphate Decarboxylases,oduct, and inhibitors as well as on the identification of alternative binding modes. Finally, a dynamic mechanism is proposed in which an increase in the strength of substrate binding and its catalytic conversion to product progress in parallel.

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Catalysis by Enzyme Conformational Change,ctant state than in the transition state. The energy released from conformational relaxation of the protein is the main source of the rate enhancement. The proposed mechanism is consistent with results from site-directed mutagenesis where mutations remote from the reaction center affect.. but not...

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,Developing Active Site Models of ODCase—from Large Quantum Models to a QM/MM Approach,rotonation may be underestimated and the support for the base protonation mechanism is uncertain. An initial QM/MM investigation of a stepwise mechanism, where water molecules seem to play an important role for TS stabilization, gives the most promising results with an estimated barrier of 22 kcal/mol.

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,Insight into the Catalytic Mechanism of Orotidine 5′-phosphate Decarboxylase from Crystallography acal reactions to be described. Orotidine 5′-phosphate decarboxylase (ODCase), the enzyme responsible for catalyzing this difficult transformation, performs its task without the assistance of metals or small molecule cofactors. The crystal structures of ODCase from yeast and three prokaryotes have re

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