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. 1973 Nov;116(2):562–570. doi: 10.1128/jb.116.2.562-570.1973

Participation of Branched-Chain Amino Acid Analogues in Multivalent Repression

John J Wasmuth 1, H E Umbarger 1
PMCID: PMC285418  PMID: 4583240

Abstract

Two isoleucine analogues and two leucine analogues were examined for their ability to replace the natural amino acid preventing the accumulation of threonine deaminase-forming potential. The procedure used to study repression by the analogues distinguishes between true repression and the formation of inactive enzyme by the analogue in question. The leucine analogue 4-azaleucine was found to replace leucine in multivalent repression of threonine deaminase-forming potential in Escherichia coli but not in Salmonella typhimurium. Another leucine analogue, trifluoroleucine, was only partially effective in causing repression in either organism. The isoleucine analogue 4-azaisoleucine was ineffective in replacing isoleucine in repression. In contrast, 4-thiaisoleucine effectively replaced isoleucine in the repression of threonine deaminase-forming potential in S. typhimurium and E. coli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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