Multivalent regulation of isoleucine-valine transaminase in an Escherichia coli K-12 ilvA deletion strain.
In a strain of Escherichia coli K-12 lacking threonine deaminase, the enzyme converting alpha-ketoisovalerate and alpha-keto-beta-methylvalerate to valine and isoleucine, respectively, was multivalently repressed by valine, isoleucine, and leucine. This activity was due to transaminase B, specified by the ilvE structural gene.
D002872:Chromosome Deletion; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005796:Genes; D007532:Isoleucine / Q000378:metabolism*; D013913:Threonine Dehydratase / Q000235:genetics / Q000502:physiology; D000637:Transaminases / Q000032:analysis / Q000235:genetics* / Q000378:metabolism*; D014633:Valine / Q000378:metabolism*
D007532:Isoleucine; D000637:Transaminases; C019798:branched-chain-amino-acid transaminase; D013913:Threonine Dehydratase; D014633:Valine