Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Genes, Bacterial
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Kinetics
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Molecular Sequence Data
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Phosphotransferases / chemistry
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Phosphotransferases / genetics*
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Phosphotransferases / metabolism
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Plasmids
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Restriction Mapping
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics
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Sequence Homology, Nucleic Acid
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Transferases (Other Substituted Phosphate Groups)*
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Tunicamycin / pharmacology
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Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives
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Uridine Diphosphate N-Acetylmuramic Acid / metabolism
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Uridine Monophosphate / metabolism
Substances
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Uridine Diphosphate N-Acetylmuramic Acid
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Tunicamycin
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UDP-N-acetylmuramic acid pentapeptide
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Uridine Monophosphate
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Phosphotransferases
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Transferases (Other Substituted Phosphate Groups)
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phospho-N-acetylmuramoyl pentapeptide transferase
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UDPacetylglucosamine-dolichyl-phosphate acetylglucosamine-1-phosphate transferase