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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)
transglycosylase domain-containing protein catalyzes the polymerization of murein glycan chains; such as biosynthetic peptidoglycan transglycosylase and bifunctional penicillin-binding proteins
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