Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein.

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Citation

Rohdich F, Hecht S, Gartner K, Adam P, Krieger C, Amslinger S, Arigoni D, Bacher A, Eisenreich W

Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein.

Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1158-63. Epub 2002 Jan 29.

PubMed ID
11818558 [ View in PubMed
]
Abstract

Isopentenyl diphosphate and dimethylallyl diphosphate serve as the universal precursors for the biosynthesis of terpenes. Although their biosynthesis by means of mevalonate has been studied in detail, a second biosynthetic pathway for their formation by means of 1-deoxy-D-xylulose 5-phosphate has been discovered only recently in plants and certain eubacteria. Earlier in vivo experiments with recombinant Escherichia coli strains showed that exogenous 1-deoxy-D-xylulose can be converted into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate by the consecutive action of enzymes specified by the xylB and ispCDEFG genes. This article describes the transformation of exogenous [U-(13)C(5)]1-deoxy-D-xylulose into a 5:1 mixture of [U-(13)C(5)]isopentenyl diphosphate and [U-(13)C(5)]dimethylallyl diphosphate by an E. coli strain engineered for the expression of the ispH (lytB) gene in addition to recombinant xylB and ispCDEFG genes.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
4-hydroxy-3-methylbut-2-enyl diphosphate reductaseP62623Details