Abstract
Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Alanine / chemistry*
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Amino Acid Substitution
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Catalysis
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Catalytic Domain
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Escherichia coli / enzymology
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Isoleucine / chemistry*
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Kinetics
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Molecular Dynamics Simulation
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Mutation
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NADP / chemistry
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NADP / metabolism
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Tetrahydrofolate Dehydrogenase / genetics
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Tetrahydrofolate Dehydrogenase / metabolism*
Substances
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Isoleucine
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NADP
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Tetrahydrofolate Dehydrogenase
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Alanine