The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli
نویسندگان
چکیده
منابع مشابه
5-Aminolevulinic acid synthesis in Escherichia coli.
A hemA mutant of Escherichia coli containing a multicopy plasmid which complemented the mutation excreted 5-aminolevulinic acid (ALA) into the medium. [1-14C]glutamate was substantially incorporated into ALA by this strain, whereas [2-14C]glycine was not. Periodate degradation of labeled ALA showed that C-5 of ALA was derived from C-1 of glutamate. The synthesis of ALA by two sonicate fractions...
متن کاملTransport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium.
In a previous search for mutants of Salmonella typhimurium that are defective in heme synthesis, one class that is apparently defective in 5-aminolevulinic acid (ALA) uptake (alu) was found. Here, I describe the characterization of these mutations. The mutations all map to a single locus near 77.5 min on the genetic map, which is transcribed counterclockwise. Nutritional tests, genetic and phys...
متن کاملOptimization of the heme biosynthesis pathway for the production of 5-aminolevulinic acid in Escherichia coli
5-Aminolevulinic acid (ALA), the committed intermediate of the heme biosynthesis pathway, shows significant promise for cancer treatment. Here, we identified that in addition to hemA and hemL, hemB, hemD, hemF, hemG and hemH are also the major regulatory targets of the heme biosynthesis pathway. Interestingly, up-regulation of hemD and hemF benefited ALA accumulation whereas overexpression of h...
متن کاملEffect of culture conditions on production of 5-aminolevulinic acid by recombinant Escherichia coli.
Aminolevulinic acid (ALA) is formed by the enzyme ALA synthase (hemA gene). Then ALA is converted to Porphobilinogen (PBG) by the ALA dehydratase (hemB gene). For the overproduction of ALA, we used an Escherichia coli BL21(DE3) containing a hemA gene from Bradyrhzobium japonicum, which was created in our previous work. The effects of pH on the ALA synthase and ALA dehydratase were investigated....
متن کاملTopography of lactose permease from Escherichia coli.
The topography of lactose permease, in native membrane vesicles and after reconstitution of the purified protein into proteoliposomes, has been investigated by labeling the membrane-embedded portions of the protein using photoactivatable, hydrophobic reagents and by labeling the exposed portions of the protein with water-soluble, electrophilic reagents. Some sites of modification have been loca...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1993
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.175.5.1452-1456.1993