EC 2.7.8.12 - Teichoic acid poly(glycerol phosphate) polymerase

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IntEnz Enzyme Nomenclature
EC 2.7.8.12

Names

Accepted name:
teichoic acid poly(glycerol phosphate) polymerase
Other names:
CDP-glycerol glycerophosphotransferase [ambiguous]
CGPTase
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

Reaction

Comments:

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 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, 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
UniProtKB/Swiss-Prot:

References

  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 2.7.8.12 created 1972, modified 1982, modified 2017]