TY - JOUR
T1 - Incorporating Fast Protein Dynamics into Enzyme Design
T2 - A Proposed Mutant Aromatic Amine Dehydrogenase
AU - Zoi, Ioanna
AU - Antoniou, Dimitri
AU - Schwartz, Steven D.
N1 - Publisher Copyright:
© 2017 American Chemical Society.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017/8/3
Y1 - 2017/8/3
N2 - In recent years, there has been encouraging progress in the engineering of enzymes that are designed to catalyze reactions not accelerated by natural enzymes. We tested the possibility of reengineering an existing enzyme by introducing a fast protein motion that couples to the reaction. Aromatic amine dehydrogenase is a system that has been shown to use a fast substrate motion as part of the reaction mechanism. We identified a mutation that preserves this fast motion but also introduces a favorable fast motion near the active site that did not exist in the native enzyme. Transition path sampling was used for the analysis of the atomic details of the mechanism.
AB - In recent years, there has been encouraging progress in the engineering of enzymes that are designed to catalyze reactions not accelerated by natural enzymes. We tested the possibility of reengineering an existing enzyme by introducing a fast protein motion that couples to the reaction. Aromatic amine dehydrogenase is a system that has been shown to use a fast substrate motion as part of the reaction mechanism. We identified a mutation that preserves this fast motion but also introduces a favorable fast motion near the active site that did not exist in the native enzyme. Transition path sampling was used for the analysis of the atomic details of the mechanism.
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U2 - 10.1021/acs.jpcb.7b05319
DO - 10.1021/acs.jpcb.7b05319
M3 - Article
C2 - 28696108
AN - SCOPUS:85026896051
VL - 121
SP - 7290
EP - 7298
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
SN - 1520-6106
IS - 30
ER -