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A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis.
Data clearly show that the yaeM gene encodes an enzyme, designated 1-deoxy-D-xylulose 5-phosphate reductoisomerase, that synthesizes 2-C-methyl- D-erythritol 4-ph phosphate, in a single step by intramolecular rearrangement and reduction and that this gene is responsible for terpenoid biosynthesis in E. coli. Expand
Fosmidomycin, a specific inhibitor of 1-deoxy-d-xylulose 5-phosphate reductoisomerase in the nonmevalonate pathway for terpenoid biosynthesis
Fosmidomycin inhibited 1-deoxy-d-xylulose 5-phosphate reductoisomerase pathway for terpenoid biosynthesis with IC50 of 8.2 nM.
Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products
These crystal structures, coupled with in vitro assays, provide a basis for understanding and potentially manipulating the regio-specific prenylation of aromatic small molecules using this structurally unique family of aromatic PTases. Expand
An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190.
The results indicate that orfD encodes an unusual IPP isomerase showing no sequence similarity to those of IPp isomerases identified to date, considered to be a suitable molecular target for the screening of antibacterial drugs specific to S. aureus. Expand
Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Gibberellins inArabidopsis *
Gas chromatography-mass spectrometry analyses demonstrated that both MVA and MEP pathways can contribute to the biosyntheses of GAs and campesterol, a cytosolic sterol, in Arabidopsisseedlings and provided evidence to suggest that the MVA pathway still contributes to GA biosynthesis when this pathway is limiting. Expand
Mevalonate and Nonmevalonate Pathways for the Biosynthesis of Isoprene Units
  • T. Kuzuyama
  • Biology, Medicine
  • Bioscience, biotechnology, and biochemistry
  • 1 January 2002
This work has identified a recently discovered pathway, the nonmevalonate pathway, which is used by many eubacteria, green algae, and chloroplasts of higher plants, and its corresponding enzymes have been identified. Expand
Terpene synthases are widely distributed in bacteria
A powerful search method based on the use of hidden Markov models (HMMs) and protein families database (Pfam) search that has allowed the discovery of monoterpene synthases of bacterial origin is described. Expand
Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities.
Multiple chemoenzymatic syntheses of various prenylated compounds from aromatic substrates including flavonoids using two prenytransferases NphB and SCO7190, a Nph B homolog from Streptomyces coelicolor A3(2), as biocatalysts are reported. Expand
Diversity of the biosynthesis of the isoprene units.
This review covers the biosynthesis of the starter units of terpenoids via the nonmevalonate pathway together with a new enzyme involved in the conversion of IPP and DMAPP, i.e type 2 IPP isomerase. Expand
Identification of class 2 1-deoxy-D-xylulose 5-phosphate synthase and 1-deoxy-D-xylulose 5-phosphate reductoisomerase genes from Ginkgo biloba and their transcription in embryo culture with respect
Exclusive transcription of ginkgolide biosynthesis-specific LPS and GbDXS2 in roots and the appearance of ginkinggolides in leaves was consistent with translocation of the compounds from roots to leaves. Expand