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transglycosylase domain-containing protein
The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively [1]. The transglycosylase domain catalyses the polymerisation of murein glycan chains ([4]). [1]. 9244263. Topographical and functional investigation of Escherichia coli. penicillin-binding protein 1b by alanine stretch scanning. mutagenesis.. F. Lefevre, M. H. Remy & J. M. Masson;. J Bacteriol 1997;179:4761-4767.. [2]. 9614972. X-ray studies of enzymes that interact with penicillins.. Kelly JA, Kuzin AP, Charlier P, Fonze E;. Cell Mol Life Sci 1998;54:353-358.. [3]. 8830253. Monofunctional biosynthetic peptidoglycan transglycosylases.. Spratt BG, Zhou J, Taylor M, Merrick MJ;. Mol Microbiol 1996;19:639-640.. [4]. 12867450. The glycosyltransferase domain of penicillin-binding protein 2a. from Streptococcus pneumoniae catalyzes the polymerization of. murein glycan chains.. Di Guilmi AM, Dessen A, Dideberg O, Vernet T;. J Bacteriol 2003;185:4418-4423. (from Pfam)
penicillin-binding transpeptidase domain-containing protein
The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family. [1]. 8605631. X-ray structure of Streptococcus pneumoniae PBP2x, a primary. penicillin target enzyme.. Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. Nat Struct Biol 1996;3:284-289. (from Pfam)
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