Alteration of Product Specificity of Rhodobacter sphaeroides Phytoene Desaturase by Directed Evolution
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چکیده
منابع مشابه
Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution.
Directed evolution of the C25 farnesylgeranyl diphosphate synthase of Aeropyrum pernix (Fgs) was carried out by error-prone PCR with an in vivo color complementation screen utilizing carotenoid biosynthetic pathway enzymes. Screening yielded 12 evolved clones with C20 geranylgeranyl diphosphate synthase activity which were isolated and characterized in order to understand better the chain elong...
متن کاملPhytoene desaturase from Arabidopsis.
Carotenoids are isoprenyl pigments necessary for protection of the photosynthetic apparatus in a11 green plants. One of the intermediate steps in carotenoid biosynthesis is the conversion of phytoene to {-carotene via two dehydrogenation reactions catalyzed by the enzyme PDS. We have previously cloned cDNAs for this enzyme from soybean (Glycine max; Bartley et al., 1991) and tomato (Lycopersico...
متن کاملComplexes of Rhodobacter sphaeroides and Rhodobacter capsulatus
Photosynthetic bacteria offer excellent experimental opportunities to explore both the structure and function of the ubiquinol-cytochrome c oxidoreductase (bcl complex). In both Rhodobacter sphaeroides and Rhodobaeter capsulatus, the bCl complex functions in both the aerobic respiratory chain and as an essential component of the photosynthetic electron transport chain. Because the bc~ complex i...
متن کاملOsmoregulation in Rhodobacter sphaeroides.
Betaine (N,N,N-trimethylglycine) functioned most effectively as an osmoprotectant in osmotically stressed Rhodobacter sphaeroides cells during aerobic growth in the dark and during anaerobic growth in the light. The presence of the amino acids L-glutamate, L-alanine, or L-proline in the growth medium did not result in a significant increase in the growth rate at increased osmotic strengths. The...
متن کاملSpecific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides.
The effects of multiple changes in hydrogen bond interactions between the electron donor, a bacteriochlorophyll dimer, and histidine residues in the reaction center from Rhodobacter sphaeroides have been investigated. Site-directed mutations were designed to add or remove hydrogen bonds between the 2-acetyl groups of the dimer and histidine residues at the symmetry-related sites His-L168 and Ph...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m105786200