Participation of Branched-chain Amino Acid Analogues in Multivalent Repression

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1973 Nov 1

PMID 4583240

Citations 4

Authors

J J Wasmuth

H E Umbarger

Affiliations

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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.

Citing Articles

Role for free isoleucine of glycyl-leucine in the repression of threonine deaminase in Escherichia coli.

Wasmuth J, Umbarger H J Bacteriol. 1974; 117(1):29-39.

PMID: 4587610 PMC: 246521. DOI: 10.1128/jb.117.1.29-39.1974.

Threonine deaminase: autogenous regulator of the ilv genes in Escherichia coli K-12.

Abrescia P, Guardiola J, Foresti M, Lamberti A, Iaccarino M Mol Gen Genet. 1979; 171(3):261-75.

PMID: 377013 DOI: 10.1007/BF00267581.

Linkage map of Salmonella typhimurium, edition V.

Sanderson K, Hartman P Microbiol Rev. 1978; 42(2):471-519.

PMID: 353483 PMC: 281437. DOI: 10.1128/mr.42.2.471-519.1978.

Transport of L-4-azaleucine in Escherichia coli.

Harrison L, CHRISTENSEN H, Handlogten M, OXENDER D, Quay S J Bacteriol. 1975; 122(3):957-65.

PMID: 238951 PMC: 246147. DOI: 10.1128/jb.122.3.957-965.1975.

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