This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8. The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry
This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8. The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry
the product of chain elongation catalyzed by the Thermotoga maritima enzyme is C40 and the rate of its conversion to C45 is negligible. Under single-turnover condition with 0.01 mM octaprenyl pyrophosphate synthase/farnesyl pyrophosphate complex and 0.001 mM isopentenyl pyrophosphate, only the C20 is formed
octaprenyl pyrophosphate synthase catalyzes the chain elongation of farnesyl pyrophosphate via consecutive condensation reactions with five molecules of isopentenyl pyrophosphate to generate all-trans C40-octaprenyl pyrophosphate. The polymer forms the side chain of ubiquinone that is involved in electron transport system to produce ATP
the enzyme catalyzes consecutive condensation reactions of farnesyl diphosphate with isopentenyl diphosphate to generate octaprenyl diphosphate, which constitutes the side chain of bacterial ubiquinone or menaquinone
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants A76Y, A76Y/S77F, F132A/L128A, F132A/L128A/I123A, and F132A/L128A/I123A/D62A to 3.1, 2.7, 3.3, 3.35 and 3.4 A resolution, respectively. Like wildtype OPPs, all mutant structures contain 12 alpha-helices, nine of them surrounding a large central cavity and an elongated tunnel-shaped active site cavity surrounded by four alpha-helices In the crystal structure of the A76Y/S77F mutant, F77 is pushed away by Y76, thereby creating more space between those two large amino acids to accommodate the C20 product. A large F132 residue at the bottom of the tunnel-shaped active site serves as the floor and determines the final product chain length. The substitution of F132 with a small Ala, thereby removing the blockade, leads to the synthesis of a C50 product larger than that produced by the wild-type enzyme
wild-type and mutants F52A, V73A, S77F, F132A, to 2.28, 2.80, 2.85, 2.45 and 2.40 A resolution, respectively. OPPs is composed entirely of alpha-helices joined by connecting loops and is arranged with nine core helices around a large central cavity. An elongated hydrophobic tunnel between D and F alpha-helices contains two DDXXD motifs on the top for substrate binding and is occupied at the bottom with two large residues Phe-52 and Phe-132
mutant produces only C20 cores instead of the C40 core of octaprenyl diphosphate. The A76Y/S77F mutant synthesizes a larger amount of C20 than the A76Y mutant
A molecular ruler for chain elongation catalyzed by octaprenyl pyrophosphate synthase and its structure-based engineering to produce unprecedented long chain trans-prenyl products
Reaction kinetic pathway of the recombinant octaprenyl pyrophosphate synthase from Thermotoga maritima How is it different from that of the mesophilic enzyme