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Mutational analysis of the CitA citrate transporter from Salmonella typhimurium: altered substrate specificity.

Abstract：

:The CitA citrate transporter in Salmonella typhimurium is encoded by the citA gene and consists of 434 amino acid residues that probably include 12 membrane-spanning segments [Shimamoto. T., et al. (1991) J. Biochem. 110, 22-28]. CitA mutants with altered substrate specificities were isolated by in vitro mutagenesis using nitrous acid. The mutants could grow on isocitrate as a sole carbon source which normally cannot be transported well by the CitA transporter of S. typhimurium. The mutation sites in the citA gene of the nine mutants were determined to involve single residues at seven sites (one mutation per mutant). The original amino acid residues at these sites (Arg-19, Ala-38, Glu-51, Gly-132, Ala-169, Pro-262 and Leu-271) were identified to be responsible for the altered substrate specificity. All these amino acid residues were conserved in four other homologous citrate transporters from Escherichia coli, Citrobacter amalonaticus and Klebsiella pneumoniae and are suggested to be involved in substrate recognition by the CitA transporter.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Shimamoto T,Negishi K,Tsuda M,Tsuchiya T

doi

10.1006/bbrc.1996.1381

subject

Has Abstract

pub_date

1996-09-13 00:00:00

pages

481-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91381-9

journal_volume

226

pub_type

杂志文章

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