Studies on bacterial cell wall inhibitors. X. Properties of phosph-N-acetylmuramoyl-pentapeptide-transferase in peptidoglycan synthesis of Bacillus megaterium and its inhibition by amphomycin.
J Antibiot (Tokyo)
; 35(9): 1216-21, 1982 Sep.
Article
em En
| MEDLINE
| ID: mdl-6292151
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfotransferases
/
Bacillus megaterium
/
Peptidoglicano
/
Antibacterianos
Idioma:
En
Ano de publicação:
1982
Tipo de documento:
Article