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di-trans,poly-cis-decaprenylcistransferase
di-trans,poly-cis-decaprenylcistransferase
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
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

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

\rightleftharpoons

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. 92 (5). Tokyo: 1527–37. doi:10.1093/oxfordjournals.jbchem.a134077. PMID 6818223.