di-trans,poly-cis-decaprenylcistransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.5.1.31 | ||||||||
CAS no. | 52350-87-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a di-trans,poly-cis-decaprenylcistransferase (EC 2.5.1.31) is an enzyme that catalyzes the chemical reaction
- di-trans,poly-cis-decaprenyl diphosphate + isopentenyl diphosphate diphosphate + di-trans,poly-cis-undecaprenyl diphosphate
Thus, the two substrates of this enzyme are di-trans,poly-cis-decaprenyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and di-trans,poly-cis-undecaprenyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is di-trans,poly-cis-decaprenyl-diphosphate:isopentenyl-diphosphate undecaprenylcistransferase. Other names in common use include di-trans,poly-cis-undecaprenyl-diphosphate synthase, undecaprenyl-diphosphate synthase, bactoprenyl-diphosphate synthase, UPP synthetase, undecaprenyl diphosphate synthetase, and undecaprenyl pyrophosphate synthetase. This enzyme participates in terpenoid biosynthesis.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1F75, 1JP3, 1UEH, 1V7U, 1X06, 1X07, 1X08, 1X09, 2D2R, 2DTN, 2E98, 2E99, 2E9A, 2E9C, and 2E9D.
References
- Muth JD, Allen CM (1984). "Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a dimeric protein". Arch. Biochem. Biophys. 230 (1): 49–60. doi:10.1016/0003-9861(84)90085-7. PMID 6712246.
- Takahashi I, Ogura K (November 1982). "Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase". J. Biochem. Tokyo. 92 (5): 1527–37. doi:10.1093/oxfordjournals.jbchem.a134077. PMID 6818223.