منابع مشابه
Structure-function correlation in glycine oxidase from Bacillus subtilis.
Structure-function relationships of the flavoprotein glycine oxidase (GO), which was recently proposed as the first enzyme in the biosynthesis of thiamine in Bacillus subtilis, has been investigated by a combination of structural and functional studies. The structure of the GO-glycolate complex was determined at 1.8 A, a resolution at which a sketch of the residues involved in FAD binding and i...
متن کاملGlyphosate resistance by engineering the flavoenzyme glycine oxidase.
Glycine oxidase from Bacillus subtilis is a homotetrameric flavoprotein of great potential biotechnological use because it catalyzes the oxidative deamination of various amines and d-isomer of amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Glyphosate (N-phosphonomethylglycine), a broad spectrum herbicide, is an interesting synthetic amino acid: th...
متن کاملConserved Glycine 232 in the Ligand Channel of ba3 Cytochrome Oxidase from Thermus thermophilus
Knowing how the protein environment modulates ligand pathways and redox centers in the respiratory heme-copper oxidases is fundamental for understanding the relationship between the structure and function of these enzymes. In this study, we investigated the reactions of O2 and NO with the fully reduced G232V mutant of ba3 cytochrome c oxidase from Thermus thermophilus (Tt ba3) in which a conser...
متن کاملImproving Glyphosate Oxidation Activity of Glycine Oxidase from Bacillus cereus by Directed Evolution
Glyphosate, a broad spectrum herbicide widely used in agriculture all over the world, inhibits 5-enolpyruvylshikimate-3-phosphate synthase in the shikimate pathway, and glycine oxidase (GO) has been reported to be able to catalyze the oxidative deamination of various amines and cleave the C-N bond in glyphosate. Here, in an effort to improve the catalytic activity of the glycine oxidase that wa...
متن کاملInhibitory Effect of Cysteine and Glycine Upon Partial Purified Polyphenol Oxidase of Pyrus communis
L-glycine and L-cysteine, exhibit strong inhibition of partial purified PPO of wild pear. The concentration of L-glycine inhibiting PPO activity by 50% (IC ) was 0.8 and 0.5 mM for catechol oxidation and 50 0.75 and 0.5 mM for pyrogallol oxidation at pH 5 and 7, respectively. IC for L-cysteine calculated, 0.6 and 0.35 50 for catechol oxidation and 0.55 and 0.75 mM for pyrogallol oxidation at pH...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1944
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)72097-8