Article
A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change.
European journal of biochemistry - 15 Jul 1992
Ahmad S, Glavas N A, Bragg P D
Abstract excerpt
Escherichia coli RH1 contains a mutation causing complete loss of pyridine nucleotide transhydrogenase activity. A single base change in the chromosomal DNA resulted in the replacement of Gly314 of the beta subunit by a Glu residue. The mutant enzyme was partially purified and its trypsin cleavag...
Topics
- Amino Acid Sequence
- Base Sequence
- Cell Membrane
- Cloning, Molecular
- Escherichia coli
- Genes, Bacterial
- Glutamates
- Glycine
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- NADP
- NADP Transhydrogenases
- Peptide Fragments
- Protein Conformation
- Restriction Mapping
- Solubility
- Structure-Activity Relationship