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malfunction
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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metabolism
the enzyme catalyzes a reaction of the classical mevalonate pathway
metabolism
the enzyme is implicated in latex metabolism. Rubber yields and/or yield characteristics are not significantly correlated with enzyme expression levels
metabolism
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the enzyme catalyzes a reaction of the classical mevalonate pathway
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metabolism
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the enzyme catalyzes a reaction of the classical mevalonate pathway
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physiological function
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investigation of the role of mevalonate diphospho decarboxylase in viral replication
physiological function
gene is able to complement the growth defect of a Saccharomyces cervisiae mevalonete diphosphate decarboxylase mutant on YGPal medium
physiological function
gene is able to functionally complement mevalonate 5-diphosphate decarboxylase deletion mutants in the yeast Saccharomyces cerevisiae
physiological function
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
physiological function
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the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
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physiological function
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gene is able to complement the growth defect of a Saccharomyces cervisiae mevalonete diphosphate decarboxylase mutant on YGPal medium
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physiological function
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the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
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physiological function
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the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
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physiological function
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the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
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additional information
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview
additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview
additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview
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additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview
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additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview
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additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview
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