development of an fluorescence assay method for determination by HPLC of vitamin B6 compounds, e.g. pyridoxine and pyridoxal, coupling reaction of recombinant pyridoxine 4-oxidase and recombinant pyridoxal 4-dehydrogenase, overview
2,6-dihydroxypridine, 3-pyridinemethanol, and 4-pyridinemethanol give only about 0.15% of the activity as compared with pyridoxine. The enzyme cannot use pyridoxal 5'-phosphate as a substrate
2,6-dihydroxypridine, 3-pyridinemethanol, and 4-pyridinemethanol give about 0.15% of the activity as compared with pyridoxine. The enzyme cannot use pyridoxal 5'-phosphate as a substrate
2,6-dihydroxypridine, 3-pyridinemethanol, and 4-pyridinemethanol give about 0.15% of the activity as compared with pyridoxine. The enzyme cannot use pyridoxal 5'-phosphate as a substrate
the enzyme belongs to the glucose methanol choline (GMC) oxidoreductase family of enzymes. Active site Pro504 in PNOX corresponds to Asn or His of the conserved His-Asn or His-His pair in other GMC oxidoreductase active sites
in the active site, His460, His462, and Pro504 are located on the re-face of the isoalloxazine ring of FAD, pyridoxamine binds to the active site through several hydrogen bonds, mode, overview. His462 may act as a general base for the abstraction of a proton from the 4'-hydroxyl of pyridoxine. His460 may play a role in the binding and positioning of pyridoxine
in the active site, His460, His462, and Pro504 are located on the re-face of the isoalloxazine ring of FAD, pyridoxamine binds to the active site through several hydrogen bonds, mode, overview. His462 may act as a general base for the abstraction of a proton from the 4'-hydroxyl of pyridoxine. His460 may play a role in the binding and positioning of pyridoxine
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His6-tagged PNOX and PNOX-pyridoxamine complex, sitting drop vapour diffusion mthod and micro-seeding method, mixing of 0.002 ml of 10 mg/ml PNOX with 0.002 ml of a precipitant solution comtaining 0.1 M HEPES-NaOH, pH 7.5, 10% v/v 2-propanol, and 20% w/v PEG 4000, equilibration against 01 ml of precipitant solution, 4°C, primary crystals are crushed and suspended in 0.5 ml of a solution consisting of equal volumes of a crystallization buffer containing 50 mM Tris-HCl, pH 8.0, 10% w/v glycerol, 0.005 mM FAD, 0.1% v/v 2-mercaptoethanol, and 0.01% v/v Tween 20, and precipitant solution as seeding solution, or seeding crystals are prepared by vapor diffusion in a mixture consisting of 0.002 ml of 13 mg/ml PNOX, and 0.002 ml of the precipitant solution comprising 0.1 M HEPES-NaOH, pH 7.5, 25% v/v 2-propanol, 20% w/v PEG 4000, and 10 mM pyridoxamine, 3 weeks, X-ray diffraction structuure determination and analysis at 2.2 A and 2.1 A resolutions, respectively, molecular replacement
overexpression in Escherichia coli strains JM109 and BL21(DE3), co-expression with catalase, chaperonin, and pyridoxal 4-dehydrogenase for construction of a biotransformation system catalyzing the formation of 4-pyridoxolactone from pyridoxine in whole cells, overview
coexpression of enzyme with GroEL/Es genes in Escherichia coli under cold stress at 23°C results in 88fold higher specific activity than that of Microbacterium luteolum
development of a simple and efficient synthesis for 4-pyridoxolactone starting with pyridoxine and using a whole-cell biotransformation by two transformed Escherichia coli cell type expressing the pyridoxine oxidase and the catalase, and chaperonin, while the second set expressed pyridoxal 4-dehydrogenase, overview. Pyridoxine is first oxidized to pyridoxal, which is then dehydrogenated to 4-pyridoxolactone by pyridoxine 4-oxidase and pyridoxal 4-dehydrogenase, respectively
bioconversion of pyridoxine to pyridoxal. Approximately 450 mM pyridoxal is produced from 500 mM pyridoxine using recombinant Rhodococcus erythropolis expressing the pyridoxine 4-oxidase gene. Pyridoxal is converted to pyridoxamine by expression of the pyridoxamine-pyruvate aminotransferase gene derived from Rhizobium loti, and pyridoxine to pyridoxamine through pyridoxal using coexpression of the genes for pyridoxine 4-oxidase and pyridoxamine-pyruvate aminotransferase
Yuan, B.; Yoshikane, Y.; Yokochi, N.; Ohnishi, K.; Yagi, T.
The nitrogen-fixing symbiotic bacterium Mesorhizobium loti has and expresses the gene encoding pyridoxine 4-oxidase involved in the degradation of vitamin B6
Vitamin B6 degradation by pyridoxamine-pyruvate transaminase and pyridoxine 4-oxidase from Ochrobactrum anthropi- and Enterobacter cloacae-like bacteria