PMID:8772200
| Citation |
Di Berardino, M, Dijkstra, A, Stüber, D, Keck, W and Gubler, M (1996) The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes. FEBS Lett. 392:184-8 |
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| Abstract |
Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacteria] species. Here we report the cloning of the homologous Escherichia coli gene and show that the solubilised membrane fraction of E. coli cells overexpressing the mgt gene contain a significantly increased peptidoglycan synthesis activity. In contrast to the high-molecular-weight PBPs, this activity is not inhibited by Flavomycin. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; DNA Primers; Escherichia coli/enzymology; Glycosyltransferases/chemistry; Glycosyltransferases/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Molecular Sequence Data; Peptidoglycan/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Species Specificity |
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