Abstract
The E28D variant of dihydrofolate reductase from Moritella profunda was generated and found to have the same K (i) (within error) for the competitive inhibitor trimethoprim as the wild type enzyme. Contrary to a previous claim in the literature, Glu 28 is therefore not the cause of the reduced affinity for trimethoprim relative to dihydrofolate reductase from Escherichia coli.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Folic Acid Antagonists / pharmacology*
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Glutamic Acid / chemistry
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Glutamic Acid / genetics*
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Glutamic Acid / metabolism
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Kinetics
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Moritella / chemistry
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Moritella / enzymology*
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Moritella / genetics
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Mutation, Missense*
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Tetrahydrofolate Dehydrogenase / chemistry*
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Tetrahydrofolate Dehydrogenase / genetics
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Tetrahydrofolate Dehydrogenase / metabolism
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Trimethoprim / pharmacology*
Substances
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Bacterial Proteins
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Folic Acid Antagonists
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Glutamic Acid
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Trimethoprim
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Tetrahydrofolate Dehydrogenase