Article
Replacements of histidine 226 of NhaA-Na+/H+ antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values.
The Journal of biological chemistry - 10 Nov 1995
Rimon A, Gerchman Y, Olami Y, Schuldiner S, Padan E
Abstract excerpt
We have previously shown that replacement of His-226 in the NhaA Na+/H+ antiporter of Escherichia coli to Arg (H226R) shifts the pH profile of the antiporter toward acidic pH and as a result of delta nhaA delta nhaB strain bearing this mutation is Na+ sensitive at alkaline pH (Gerchman, Y., Olami...
Topics
- Alanine
- Aspartic Acid
- Codon
- Cysteine
- Escherichia coli
- Histidine
- Hydrogen-Ion Concentration
- Mutagenesis, Site-Directed
- Phenotype
- Point Mutation
- Serine
- Sodium-Hydrogen Exchangers
