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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | In prokaryotes, undecaprenyl diphosphate synthase (UPP synthase or di-trans-poly-cis-decaprenylcistransferase ( )), catalyzes the formation of the carrier lipid undecaprenyl pyrophosphate (UPP) in bacterial cell wall peptidoglycan biosynthesis from isopentenyl pyrophosphate (IPP) [, , , , , , , , , , , , , ]. Cis (Z)-Isoprenyl diphosphate synthase (cis-IPPS) catalyzes the successive 1'-4 condensation of the IPP molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+for activity. Homologues are also found in archaebacteria and include a number of uncharacterised proteins including some from yeasts. The structure of diphosphate synthase has three layers (α/β/α) with parallel β-sheet of six strands.This entry also matches related enzymes that transfer alkyl groups, such as dehydrodolichyl diphosphate synthase from eukaryotes, which catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate. | Name | Decaprenyl diphosphate synthase-like superfamily |
| Short Name | UPP_synth-like_sf | Type | Homologous_superfamily |
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