Journal of Bacteriology · 1991 · 138 citations · 20 references
Life SciencesBiochemistryMolecular BiologyEnzyme MechanismEnzymologyMicrobial GeneticsEnzyme FunctionLipid BiosynthesisBacterial Cell Wall BiosynthesisBacterial Peptidoglycan SynthesisEnzyme ActivityEscherichia Coli
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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Rapid and Sensitive Protein Similarity Searches
David J. Lipman, William R. Pearson · Science · 1985 · 4.1K citations
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