| 词条 | Methyltransferase/kinase WbdD |
| 释义 |
}}{{Infobox enzyme | Name = methyltransferase/kinase WbdD | EC_number = 2.1.1.294 | CAS_number = | IUBMB_EC_number = 2/7/1/181 | GO_code = | image = 4azs.jpg | width = 270 | caption = Methyltransferase/kinase WbdD homododekamer, E.Coli }} Methyltransferase/kinase WbdD {{EC number|2.1.1.294}} and {{EC number|2.7.1.181}} WbdD is a bifunctional enzyme that regulates the length of the LPS O-antigen polysaccharide chain.[1] Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar. This terminal modification is essential for export of the O-antigen across the inner membrane. WbdD is also required for correct localization of the WbdA mannosyltransferase. This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis. Catalytic activities:S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3))(n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3))(n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol. ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3))(n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3))(n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol. References1. ^{{cite journal | title = Structure of Wbdd; a Bifunctional Kinase and Methyltransferase that Regulates the Chain Length of the O Antigen in Escherichia Coli O9A. |author1 = Hagelueken, G. |author2 = Huang, H. |author3 = Clarke, B.L. |author4 = Lebl, T. |author5 = Whitfield, C. |author6 = Naismith, J.H. |journal = Mol. Microbiol. |year = 2012 |volume = 86 |page = 730 |pmid= 22970759 }} {{One carbon transferases}}{{Kinases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}} 3 : EC 2.1.1|EC 2.7.1|Bacterial proteins |
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