EC - Teichoic acid poly(glycerol phosphate) polymerase

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IntEnz Enzyme Nomenclature


Accepted name:
teichoic acid poly(glycerol phosphate) polymerase
Other names:
CDP-glycerol glycerophosphotransferase [ambiguous]
cytidine diphosphoglycerol glycerophosphotransferase
glycerophosphate synthetase
poly(glycerol phosphate) polymerase
teichoic acid glycerol transferase
teichoic-acid synthase
Tag polymerase
CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase
tagF (gene name)
tarF (gene name) [ambiguous]
Systematic name:
CDP-glycerol:4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase



Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30-50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC, teichoic acid poly(glycerol phosphate) primase. cf. EC, teichoic acid glycerol-phosphate transferase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047355
CAS Registry Number: 9076-71-5


  1. Burger, M.M. and Glaser, L.
    The synthesis of teichoic acids. I. Polyglycerophosphate.
    J. Biol. Chem. 239: 3168-3177 (1964). [PMID: 14245357]
  2. Schertzer, J. W., Brown, E. D.
    Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes the polymerization of glycerol phosphate onto a membrane acceptor in vitro.
    J. Biol. Chem. 278: 18002-18007 (2003). [PMID: 12637499]
  3. Schertzer, J. W., Bhavsar, A. P., Brown, E. D.
    Two conserved histidine residues are critical to the function of the TagF-like family of enzymes.
    J. Biol. Chem. 280: 36683-36690 (2005). [PMID: 16141206]
  4. Pereira, M. P., Schertzer, J. W., D'Elia, M. A., Koteva, K. P., Hughes, D. W., Wright, G. D., Brown, E. D.
    The wall teichoic acid polymerase TagF efficiently synthesizes poly(glycerol phosphate) on the TagB product lipid III.
    Chembiochem 9: 1385-1390 (2008). [PMID: 18465758]
  5. Sewell, E. W., Pereira, M. P., Brown, E. D.
    The wall teichoic acid polymerase TagF is non-processive in vitro and amenable to study using steady state kinetic analysis.
    J. Biol. Chem. 284: 21132-21138 (2009). [PMID: 19520862]
  6. Lovering, A. L., Lin, L. Y., Sewell, E. W., Spreter, T., Brown, E. D., Strynadka, N. C.
    Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis.
    Nat. Struct. Mol. Biol. 17: 582-589 (2010). [PMID: 20400947]
  7. Brown, S., Meredith, T., Swoboda, J., Walker, S.
    Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways.
    Chem. Biol. 17: 1101-1110 (2010). [PMID: 21035733]

[EC created 1972, modified 1982, modified 2017]