| Literature DB >> 6292151 |
H Tanaka, R Oiwa, S Matsukura, J Inokoshi, S Omura.
Abstract
The phospho-N-acetylmuramoyl-pentapeptide-transferase from Bacillus megaterium KM was characterized by the transfer reaction. The particulate enzyme preparation had the activity to transfer phospho-N-acetylmuramoyl-pentapeptide from UDP-N-acetylmuramoyl-pentapeptide to undecaprenoid-1-ol-phosphate. The optimum pH for activity was about 8.5. The reaction required the presence of Mg2+ and an SH-protector. With 25 mm Mg2+ the maximum activity was observed. The reaction was reversible and so the addition of UMP decreased the formation of undecaprenoid-1-ol-diphospho-N-acetylmuramoyl-pentapeptide. Amphomycin inhibited non-competitively the transferase for the substrate UDP-N-acetylmuramoyl-pentapeptide.Entities:
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Year: 1982 PMID: 6292151 DOI: 10.7164/antibiotics.35.1216
Source DB: PubMed Journal: J Antibiot (Tokyo) ISSN: 0021-8820 Impact factor: 2.649