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Literature summary for 2.7.8.46 extracted from

  • Meredith, T.C.; Swoboda, J.G.; Walker, S.
    Late-stage polyribitol phosphate wall teichoic acid biosynthesis in Staphylococcus aureus (2008), J. Bacteriol., 190, 3046-3056.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.46

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q2G1C2
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Staphylococcus aureus NCTC 8325 Q2G1C2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CDP-ribitol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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 Staphylococcus aureus CMP + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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 ?
CDP-ribitol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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 Staphylococcus aureus NCTC 8325 CMP + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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 ?
additional information TarK is a bifunctional enzyme that catalyzes both ribitol phosphate priming and polymerization, reactions of EC 2.7.18.46 and 2.7.8.47. TarK directs the synthesis of a polyribitol-containing teichoic acid K-WTA Staphylococcus aureus ?
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 ?
additional information TarK is a bifunctional enzyme that catalyzes both ribitol phosphate priming and polymerization, reactions of EC 2.7.18.46 and 2.7.8.47. TarK directs the synthesis of a polyribitol-containing teichoic acid K-WTA Staphylococcus aureus NCTC 8325 ?
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 ?

Synonyms

Synonyms Comment Organism
tarK
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 Staphylococcus aureus

General Information

General Information Comment Organism
physiological function TarK is a bifunctional enzyme that catalyzes both ribitol phosphate priming and polymerization, reactions of EC 2.7.18.46 and 2.7.8.47. TarK can replace polymerase TarL provided that it is sufficiently expressed. TarK directs the synthesis of a polyribitol-containing teichoic acid K-WTA. The biosynthesis of K-WTA is repressed by the accessory gene regulator (agr) system Staphylococcus aureus