Article
Sodium ion and proline binding sites in the Na+/proline symport carrier of Escherichia coli.
Biochimica et biophysica acta - 23 Mar 1992
Hanada K, Yoshida T, Yamato I, Anraku Y
Abstract excerpt
Proline binding activity of the Escherichia coli Na+/proline symport carrier is inhibited by a sulfhydryl reagent, N-ethylmaleimide (NEM). Proline and its analogs protected the carrier against the NEM-inactivation in a Na+ (or Li+)-dependent manner. Na+ alone, even in the absence of proline, partially protected it from the NEM-inactivation. Mutant proline carriers, CS281, CS344 and CS349, which have a serine...
Topics
- Amino Acid Sequence
- Amino Acid Transport Systems, Neutral
- Binding Sites
- Carrier Proteins
- Cations
- Cell Membrane
- Escherichia coli
- Escherichia coli Proteins
- Ethylmaleimide
- Molecular Sequence Data
- Mutation