The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase.
نویسندگان
چکیده
Amplification of the mraY gene, previously called open reading frame Y (ORF-Y, 1,080 bp), at 2 min in the chromosome map of Escherichia coli enhanced the activity of UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase (EC 2.7.8.13). This enzyme catalyzes the formation of undecaprenyl-pyrophosphoryl-N-acetylmuramoyl-pentapeptide from UDP-N-acetylmuramoyl-pentapeptide and undecaprenyl-phosphate, the first step in the lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans. The enhanced enzyme activity was sensitive to tunicamycin, and the amino tunicamycin-sensitive N-acetylglucosamine-1-phosphate transferase of Saccharomyces cerevisiae. Very probably mraY is the structural gene for the above enzyme.
منابع مشابه
The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis.
Physiological properties of the murG gene product of Escherichia coli were investigated. The inactivation of the murG gene rapidly inhibits peptidoglycan synthesis in exponentially growing cells. As a result, various alterations of cell shape are observed, and cell lysis finally occurs when the peptidoglycan content is 40% lower than that of normally growing cells. Analysis of the pools of pept...
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Tunicamycins are nucleotide sugar analogs produced by several Streptomyces species. In eukaryotes, tunicamycins inhibit UDP-N-acetylglucosamine: dolichol phosphate GlcNAc-1-P transferase (GPT) that catalyzes the first step in protein glycosylation. In bacteria they inhibit UDP-N-acetylmuramoyl-pentapeptide: undecaprenol phosphate MurNAc-pentapeptide-1-P transtransferase (MraY) that catalyzes an...
متن کاملOn the mechanism of action of vancomycin: inhibition of peptidoglycan synthesis in Gaffkya homari.
Vancomycin inhibits the synthesis of peptidoglycan in membrane preparations from Gaffkya homari with uridine diphosphate-N-acetylmuramyl (UDP-Mur-NAc)-pentapeptide as substrate, but not with either UDP-MurNAc-tetrapeptide or UDP-MurNAc-tripeptide. These results are correlated with the specificity studies described by Perkins and Nieto for complex formation between the antibiotic and the peptide...
متن کاملFluorescence detection-based functional assay for high-throughput screening for MraY.
We have developed a novel assay specific to MraY, which catalyzes the first membrane step in the biosynthesis of bacterial cell wall peptidoglycan. This was accomplished by using UDP-MurNAc-N(epsilon)-dansylpentapeptide, a fluorescent derivative of the MraY nucleotide substrate, and a partially purified preparation of MraY solubilized from membranes of an Escherichia coli overproducing strain. ...
متن کاملComplex lipid requirements for detergent-solubilized phosphoacetylmuramyl-pentapeptide translocase from Micrococcus luteus.
Phospho-MurNAc-pentapeptide translocase activity in the membrane of M. luteus was lost upon addition of the detergent, Triton X-100, but could be restored by addition of lipid fractions to the assay. By assay in the presence of lipid, the activity of the Triton-solubilized enzyme could be measured. The synthesis of C(55)-isoprenyl-P-P-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide required C(...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 173 3 شماره
صفحات -
تاریخ انتشار 1991