Studies on the nonmevalonate pathway to terpenes: The role of the GcpE (IspG) protein
| Autor: | Sabine Amslinger, Stefan Hecht, Petra Adam, Felix Rohdich, Duilio Arigoni, Adelbert Bacher, Wolfgang Eisenreich, Klaus Kis |
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| Rok vydání: | 2001 |
| Předmět: |
Molecular Sequence Data
Cell Mevalonic Acid Mevalonic acid Biology Terpene chemistry.chemical_compound Bacterial Proteins medicine Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Peptide sequence Gene DNA Primers chemistry.chemical_classification Multidisciplinary Base Sequence Sequence Homology Amino Acid Terpenes Nuclear magnetic resonance spectroscopy Biological Sciences Molecular biology Enzymes Enzyme medicine.anatomical_structure chemistry Biochemistry Cysteine |
| Zdroj: | Proceedings of the National Academy of Sciences. 98:14837-14842 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.201399298 |
| Popis: | Recombinant Escherichia coli cells engineered for the expression of the xylB gene in conjunction with genes of the nonmevalonate pathway were supplied with 13 C-labeled 1-deoxy- d -xylulose. Cell extracts were analyzed directly by NMR spectroscopy. 13 C-labeled 2 C -methyl- d -erythritol 2,4-cyclodiphosphate was detected at high levels in cells expressing xylB , ispC , ispD , ispE, and ispF . The additional expression of the gcpE gene afforded 1-hydroxy-2-methyl-2-( E )-butenyl 4-diphosphate as an intermediate of the nonmevalonate pathway. Hypothetical mechanisms involving conserved cysteine residues are proposed for the enzymatic conversion of 2 C -methyl- d -erythritol 2,4-cyclodiphosphate into 1-hydroxy-2-methyl-2-( E )-butenyl 4-diphosphate catalyzed by the GcpE protein. |
| Databáze: | OpenAIRE |
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