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Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway.
Mevalonate (MVA) metabolism provides the isoprenoids used in archaeal lipid biosynthesis. In synthesis of isopentenyl diphosphate, the classical MVA pathway involves decarboxylation of mevalonateExpand
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Expression in Haloferax volcanii of 3-hydroxy-3-methylglutaryl coenzyme A synthase facilitates isolation and characterization of the active form of a key enzyme required for polyisoprenoid cell
Enzymes of the isoprenoid biosynthetic pathway in halophilic archaea remain poorly characterized, and parts of the pathway remain cryptic. This situation may be explained, in part, by the difficultyExpand
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Alterations in ribosomal protein L19 that decrease the fidelity of translation.
Ribosomal protein L19 is an essential ribosomal protein and is a component of bridge B8, one of the protein-RNA bridges linking the large and small ribosomal subunits. Bridge B8 also contributes toExpand
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Identification of H. volcanii Phosphomevalonate Decarboxylase and Isopentenyl Phosphate Kinase as Catalysts of the Terminal Enzymatic Reactions in an Archaeal Alternate Mevalonate Pathway (LB139)
To identify the enzymes responsible for metabolism of mevalonate 5-phosphate to isopentenyl diphosphate in H. volcanii, two open reading frames (HVO_2762; HVO_1412) were selected for expression andExpand
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Discovery of enzymes responsible for an alternate mevalonate pathway in Haloferax volcanii
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