Literature DB >> 1732201

Enzymatic basis of thiol-stimulated secretion of porphyrins by Escherichia coli.

G T Javor1, E F Febre.   

Abstract

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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Year:  1992        PMID: 1732201      PMCID: PMC206203          DOI: 10.1128/jb.174.3.1072-1075.1992

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  24 in total

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5.  delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA.

Authors:  G P O'Neill; M W Chen; D Söll
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Authors:  J M Li; C S Russell; S D Cosloy
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9.  5-Aminolevulinic acid synthesis in Escherichia coli.

Authors:  J M Li; O Brathwaite; S D Cosloy; C S Russell
Journal:  J Bacteriol       Date:  1989-05       Impact factor: 3.490

10.  Identification of the enzymatic basis for delta-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli.

Authors:  Y J Avissar; S I Beale
Journal:  J Bacteriol       Date:  1989-06       Impact factor: 3.490

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