Article
Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study.
Biochemistry - 3 Apr 1990
Peersen O B, Pratt E A, Truong H T, Ho C, Rule G S
Abstract excerpt
The structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli have been investigated by fluorine-19 nuclear magnetic resonance spectroscopy of 5-fluorotryptophan-labeled enzyme in conjunction with oligonucleotide-directed, site-specific mutagenesis. 5-Fluorotryptophan has been substituted for nine phenylalanine, tyrosine, and leucine residues in the enzyme molecule without loss of...
Topics
- Amino Acid Sequence
- Escherichia coli
- Fluorescent Dyes
- Gene Expression
- Kinetics
- L-Lactate Dehydrogenase
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Structure-Activity Relationship