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- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
2-C-Methyl-D-erythritol 2,4-cyclodiphosphate synthase (MEcPP synthase, IspF, EC 4 6 1 12) is a zinc -dependent enzyme and a member of the YgbB N terminal protein domain, which participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis It catalyzes the following reaction: [1]
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- Biosynthesis of terpenoids: YgbB protein converts 4 . . . - PNAS
This paper shows that YgbB protein converts 4-diphos-phocytidyl-2C-methyl-D-erythritol 2-phosphate into the cyclic 2,4-diphosphate of 2C-methyl-D-erythritol Materials Oligonucleotides were custom-synthesized by MWG Biotec, Ebersberg, Germany The preparation of 13C- and 14C-labeled samples of 4-diphosphocytidyl-2C-methyl-D-erythritol,
- YgbB N terminal protein domain - Wikipedia
In molecular biology, YgbB is a protein domain This entry makes reference to a number of proteins from eukaryotes and prokaryotes which share this common N-terminal signature and appear to be involved in terpenoid biosynthesis
- Ygnbb - YouTube
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- Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C . . .
In many microorganisms, the putative orthologs of the Escherichia coli ygbB gene are tightly linked or fused to putative orthologs of ygbP, which has been shown earlier to be involved in terpenoid biosynthesis
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- Cytidine 5′-triphosphate-dependent biosynthesis of isoprenoids: YgbP . . .
We show that an enzyme isolated from cell extract of Escherichia coli converts 2 -C -methylerythritol 4-phosphate into 4-diphosphocytidyl-2 -C -methylerythritol by reaction with CTP The enzyme is specified by the hitherto unannotated ORF ygbP of E coli
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