Probing the catalytic mechanism of prephenate dehydratase by site-directed mutagenesis of the Escherichia coli P-protein dehydratase domain. [electronic resource]
Producer: 20000601Description: 4722-8 p. digitalISSN:- 0006-2960
- Amino Acid Substitution -- genetics
- Bacterial Proteins -- chemistry
- Binding Sites
- Calorimetry
- Catalysis -- drug effects
- Chorismate Mutase -- chemistry
- Chromatography, Gel
- Circular Dichroism
- Conserved Sequence -- genetics
- Cyclohexanecarboxylic Acids -- metabolism
- Cyclohexenes
- Escherichia coli -- enzymology
- Escherichia coli Proteins
- Feedback -- drug effects
- Fluorescence
- Kinetics
- Multienzyme Complexes -- chemistry
- Mutagenesis, Site-Directed -- genetics
- Mutation -- genetics
- Phenylalanine -- metabolism
- Prephenate Dehydratase -- antagonists & inhibitors
- Protein Structure, Tertiary
- Structure-Activity Relationship
- Thermodynamics
- Titrimetry
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Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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