ExplorEnz: EC 2.4.1.70

Your query returned 1 entry. Printable version

2.4.1.70

Accepted name:

poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase

Reaction:

n UDP-N-acetyl-α-D-glucosamine + 4-O-(D-ribitylphospho)_n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-α-D-glucosaminyl-D-ribitylphospho)_n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s):

TarM; UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous); uridine diphosphoacetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous); UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase (ambiguous); UDP-N-acetyl-α-D-glucosamine:poly(ribitol-phosphate) N-acetyl-α-D-glucosaminyltransferase (ambiguous); poly(ribitol-phosphate) N-acetylglucosaminyltransferase (ambiguous)

Systematic name:

UDP-N-acetyl-α-D-glucosamine:4-O-(D-ribitylphospho)_n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)

Comments:

Involved in the biosynthesis of poly(ribitol phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-α-D-glucosamine to the hydroxyl group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.355 [poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-71-7

References:

1.	Nathenson, S.G., Ishimoto, N. and Strominger, J.L. UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases from Staphylococcus aureus. Methods Enzymol. 8 (1966) 426–429.
2.	Xia, G., Maier, L., Sanchez-Carballo, P., Li, M., Otto, M., Holst, O. and Peschel, A. Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM. J. Biol. Chem. 285 (2010) 13405–13415. [DOI] [PMID: 20185825]
3.	Sobhanifar, S., Worrall, L.J., Gruninger, R.J., Wasney, G.A., Blaukopf, M., Baumann, L., Lameignere, E., Solomonson, M., Brown, E.D., Withers, S.G. and Strynadka, N.C. Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase. Proc. Natl. Acad. Sci. USA 112 (2015) E576–E585. [DOI] [PMID: 25624472]
4.	Koc, C., Gerlach, D., Beck, S., Peschel, A., Xia, G. and Stehle, T. Structural and enzymatic analysis of TarM glycosyltransferase from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid. J. Biol. Chem. 290 (2015) 9874–9885. [DOI] [PMID: 25697358]

[EC 2.4.1.70 created 1972, modified 2018]