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Biosynthesis of isoprenoids via the non-mevalonate pathway
The mevalonate pathway is essential in plants, many eubacteria and apicomplexan parasites, but not in archaea and animals, and detailed knowledge about the mechanisms may benefit the development of novel antibiotics, antimalarials and herbicides.
The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: Studies on the mechanisms of the reactions catalyzed by IspG and IspH protein
A recombinant fusion protein comprising maltose binding protein and IspG protein domains was purified from a recombinant Escherichia coli strain and found that auxiliary proteins are required as shuttles for redox equivalents.
Studies on the nonmevalonate terpene biosynthetic pathway: Metabolic role of IspH (LytB) protein
The transformation of exogenous 1-deoxy-d-xylulose into a 5:1 mixture of [U-13C5]isopentenyl diphosphate and dimethylallyl diph phosphate by an E. coli strain engineered for the expression of the ispH (lytB) gene in addition to recombinant xylB and ispCDEFG genes is described.
Studies on the nonmevalonate pathway to terpenes: The role of the GcpE (IspG) protein
Recombinant Escherichia coli cells engineered for the expression of the xylB gene in conjunction with genes of the nonmevalonate pathway were supplied with 13C-labeled 1-deoxy-d-xylulose. Cell
Vitamin B1 biosynthesis in plants requires the essential iron–sulfur cluster protein, THIC
The results suggest that vitamin B1 biosynthesis in plants is in fact more similar to prokaryotic counterparts and that the THIC protein is likely to be the key regulatory protein in the pathway.
Terpenoid biosynthesis from 1-deoxy-D-xylulose in higher plants by intramolecular skeletal rearrangement.
13C Enrichment and 13C13C coupling patterns showed conclusively that 1-deoxy-D-xylulose and not mevalonate is the predominant isoprenoid precursor of phytol, beta-carotene, and lutein.
IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis.
The implementation of a gene cassette directing the overexpression of the isc operon involved in the assembly of iron-sulfur clusters into an Escherichia coli strain engineered for ispH gene expression increased the catalytic activity of IspH protein anaerobically purified from this strain by a factor of at least 200.
Biosynthesis of hyperforin in Hypericum perforatum.
The labeling patterns show that the biosynthesis of hyperforin involves five isoprenoid moieties, which are derived entirely or predominantly via the deoxyxylulose phosphate pathway.
Biosynthesis of terpenes: Studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase
It is demonstrated that cell extract of an Escherichia coli strain engineered for hyperexpression of the ispH (lytB) gene catalyzes the in vitro conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into IPP and DMAPP.