Cofactor specificity switch in Shikimate dehydrogenase by rational design and consensus engineering
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چکیده
منابع مشابه
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design.
Homology modeling was used to identify two particular residues, Glu175 and Ala176, in Pseudomonas stutzeri phosphite dehydrogenase (PTDH) as the principal determinants of nicotinamide cofactor (NAD(+) and NADP(+)) specificity. Replacement of these two residues by site-directed mutagenesis with Ala175 and Arg176 both separately and in combination resulted in PTDH mutants with relaxed cofactor sp...
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Lactate dehydrogenase from Bacillus stearothermophilus is specific for NAD+. There have been several attempts to alter the cofactor specificity of this enzyme, but these have yielded enzymes with relatively low activities that still largely prefer NAD+. A modified consensus approach was used to create a library of phylogenetically preferred amino acids situated near the cofactor binding site, a...
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hydrochlorothiazide (hct) is a diuretic agent which is shown to be effective in the treatment of hypertension. literature reports have demonstrated that urinary excretion data may be used to assess the bioavailability of various formulations containing this thiazide. also hct consumption by the athletes is one of the drugs which should be regulated by world anti-doping agency (wada), because of...
Improvement of the soy formate dehydrogenase properties by rational design.
Previous experiments on substitution of the residue Phe290 to Asp, Asn and Ser in NAD(+)-dependent formate dehydrogenase from soya Glycine max (SoyFDH) showed important role of the residue in enzyme thermal stability and catalytic properties (Alekseeva et al. Prot. Eng. Des. Sel., 2012a; 25: :781-88). In this work, we continued site-directed mutagenesis experiments of the Phe290 and the residue...
متن کاملInhibitors of shikimate dehydrogenase as potential herbicides.
The shikimic acid biosynthetic pathway, which operates in micro-organisms and higher plants but not in mammals, leads to several essential amino acids and also to a variety of other metabolites. It was hoped, therefore, that blockage of the pathway might have a damaging effect on plant metabolism, giving a useful commercial herbicide with selective toxicity. Shikimate dehydrogenase, the enzyme ...
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 2017
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/gzx031