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.
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Authors | M Ikeda, M Wachi, H K Jung, F Ishino, M Matsuhashi |
Journal | Journal of bacteriology
(J Bacteriol)
Vol. 173
Issue 3
Pg. 1021-6
(Feb 1991)
ISSN: 0021-9193 [Print] United States |
PMID | 1846850
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Uridine Diphosphate N-Acetylmuramic Acid
- Tunicamycin
- UDP-N-acetylmuramic acid pentapeptide
- Uridine Monophosphate
- Phosphotransferases
- Transferases (Other Substituted Phosphate Groups)
- phospho-N-acetylmuramoyl pentapeptide transferase
- UDPacetylglucosamine-dolichyl-phosphate acetylglucosamine-1-phosphate transferase
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Topics |
- Amino Acid Sequence
- Escherichia coli
(enzymology, genetics)
- Genes, Bacterial
- Kinetics
- Molecular Sequence Data
- Phosphotransferases
(chemistry, genetics, metabolism)
- Plasmids
- Restriction Mapping
- Saccharomyces cerevisiae
(enzymology, genetics)
- Sequence Homology, Nucleic Acid
- Transferases (Other Substituted Phosphate Groups)
- Tunicamycin
(pharmacology)
- Uridine Diphosphate N-Acetylmuramic Acid
(analogs & derivatives, metabolism)
- Uridine Monophosphate
(metabolism)
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