Enzymatic basis of thiol-stimulated secretion of porphyrins by Escherichia coli.
1-Thioglycerol (TG) stimulates the synthesis of porphyrin in aerobically growing Escherichia coli. Here the levels of delta-aminolevulinate biosynthetic enzymes in untreated and TG-treated E. coli THU and PUC2 (a mutant of THU which overproduces porphyrins in the presence of thiols) cells were determined. TG treatment elevated the activity of glutamyl-tRNA reductase in both strains. The increased activity was not caused by activation of preexisting enzymes by thiols or by oxidizing agents but was dependent on new protein synthesis.
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Department of Biochemistry and Microbiology, Loma Linda University School of Medicine, California 92350.
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D000622:Aminolevulinic Acid / Q000378:metabolism; D003306:Coproporphyrins / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D005990:Glycerol / Q000031:analogs & derivatives* / Q000494:pharmacology; D006427:Hemin / Q000494:pharmacology; D011166:Porphyrins / Q000378:metabolism*; D011524:Protoporphyrins / Q000494:pharmacology; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012352:RNA, Transfer, Glu / Q000378:metabolism
D003306:Coproporphyrins; D011166:Porphyrins; D011524:Protoporphyrins; D012346:RNA, Transfer, Amino Acyl; D012352:RNA, Transfer, Glu; D006427:Hemin; D000622:Aminolevulinic Acid; C009465:thioglycerol; C028025:protoporphyrin IX; D005990:Glycerol