TAILIEUCHUNG - Báo cáo khoa học: Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways

An open reading frame (Acc. no. P50740) on theBacillus subtilis chromosome extending from bp 184 997–186 043 with similarity to theidi-2 gene ofStreptomycessp. CL190 specifying type II isopentenyl diphosphate isomerase was expressed in a recombinant Escherichia colistrain. The recombinant protein with a subunit mass of 39 kDa was purified to apparent homogeneity by column chromatog-raphy. The protein was shown to catalyse the conversion of dimethylallyl diphosphate into isopentenyl diphosphate and vice versa at rates of and )1 Æmin )1 , respectively, as diagnosed by 1 H spectroscopy. . | Eur. J. Biochem. 271 2658-2669 2004 FEBS 2004 doi Biochemical characterization of Bacillussubtilis type II isopentenyl diphosphate isomerase and phylogenetic distribution of isoprenoid biosynthesis pathways Ralf Lauoitz1 Stefan Hecht1 Sabine Amslinaer1 Ferdinand Zeoeck1 Johannes Kaiser1 Gerald Richter1 B 4 B B 4 w B B F B B B B w B B F B B B B B BB B B F B B B B BB B B B BB B BB B B B BB B B BB BB BB BB BB B w F B B BB B B B B BB F B BBB B BB B BM BB B BB B BB B B B BB B B BB B Nicholas Schramek1 Stefan Steinbacher2 Robert Huber3 Duilio Arigoni4 Adelbert Bacher1 Wolfgang Eisenreich1 and Felix Rohdich1 1Lehrstuhl fur Organische Chemie und Biochemie Technische Universitdt MUnchen Garching Germany 2Division of Chemistry and Chemical Engineering California Institute of Technology Pasadena CA USA 3Abteilung fur Strukturforschung Max-Planck-Institut fur Biochemie Martinsried Germany 4Laboratorium fur Organische Chemie Eidgenossische Technische Hochschule Zurich Switzerland An open reading frame Acc. no. P50740 on the Bacillus subtilis chromosome extending from bp 184 997-186 043 with similarity to the idi-2 gene of Streptomyces sp. CL190 specifying type II isopentenyl diphosphate isomerase was expressed in a recombinant Escherichia coli strain. The recombinant protein with a subunit mass of 39 kDa was purified to apparent homogeneity by column chromatography. The protein was shown to catalyse the conversion of dimethylallyl diphosphate into isopentenyl diphosphate and vice versa at rates of and pmol-mg_1-min-1 respectively as diagnosed by 1H spectroscopy. FMN and divalent cations are required for catalytic activity the highest rates were found with Ca2 . NADPH is required under aerobic but not under anaerobic assay conditions. The enzyme is related to a widespread family of S -a-hydroxy-acid oxidizing enzymes including flavocytochrome b2 and L-lactate dehydrogenase and was shown to catalyse the formation of 2 3-13C2 lactate from

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• gastric cancer
• hormone medicine
• tumor cells
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• biochemical studies
• environmental medicine