N-acetylmuramoyl-l-alanyl-d-glutamyl-l-lysyl-(N6-glycyl)-d-alanyl-d-alaninediphosphoundecaprenyl-Nacetylglucosamine:glycine glycyltransferase 2.3.2.17
Author:
Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/978-3-642-36240-8_43
Reference12 articles.
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2. Tschierske, M.; Ehlert, K.; Stranden, A.M.; Berger-Bachi, B.: Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation. FEMS Microbiol. Lett., 153, 261-264 (1997)
3. Alborn, W.E., Jr.; Hoskins, J.; Unal, S.; Flokowitsch, J.E.; Hayes, C.A.; Dotzlaf, J.E.; Yeh, W.K.; Skatrud, P.L.: Cloning and characterization of femA and femB from Staphylococcus epidermidis. Gene, 180, 177-181 (1996)
4. Maidhof, H.; Reinicke, B.; Blumel, P.; Berger-Bachi, B.; Labischinski, H.: femA, Which encodes a factor essential for expression of methicillin resistance, affects glycine content of peptidoglycan in methicillin-resistant and methicillin-susceptible Staphylococcus aureus strains. J. Bacteriol., 173, 3507-3513 (1991)
5. Ehlert, K.; Schroder, W.; Labischinski, H.: Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol., 179, 7573-7576 (1997)
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