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J. Biol. Chem., Vol. 263, Issue 31, 16055-16057, 11, 1988

Site-specific alteration of cysteine 281, cysteine 344, and cysteine 349 in the proline carrier of Escherichia coli

I Yamato and Y Anraku
Department of Biology, Faculty of Science, University of Tokyo, Japan.

Cys-281, Cys-344, or Cys-349 in the proline carrier of Escherichia coli was changed to a serine residue by site-specific mutagenesis. The activities of the resultant mutants for uptake of proline were as great as that of the wild-type strain. These mutant carriers were all as sensitive as the wild-type carrier to the proline analogue azetidine 2- carboxylate. However, the mutant carriers with Ser-281 and Ser-344 were resistant to N-ethylmaleimide, whereas the mutant carrier with Ser-349 was as sensitive as the wild-type carrier to this reagent. These results indicate that these cysteine residues are not essential for proline transport and that Cys-281 and Cys-344 may be close to the substrate-binding site that contains an N-ethylmaleimide-sensitive residue.
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