Characterization of active site residues of nitroalkane oxidase
نویسندگان
چکیده
منابع مشابه
synthesis and characterization of potentially biological active cyclometallated organoplatinum(ii) complexes
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متن کاملIdentification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide.
The flavoprotein nitroalkane oxidase catalyzes the oxidative denitrification of primary or secondary nitroalkanes to the corresponding aldehydes or ketones with production of hydrogen peroxide and nitrite. The enzyme is irreversibly inactivated by treatment with N-ethylmaleimide at pH 7. The inactivation is time-dependent and shows first-order kinetics for three half-lives. The second-order rat...
متن کاملActive site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues.
Two cysteine residues (C-265 and C-318) in the putative hydrophilic regions of sarcosine oxidase were substituted by using site-directed mutagenesis. Since the mutant with the C-to-S mutation at position 318 (C318S) lost the enzyme activity, C-318 (conserved among sarcosine oxidases) is most likely a part of the active site. C265S, C265A, C265D, and C265R showed nearly the same enzymatic proper...
متن کاملCrystallization and preliminary analysis of active nitroalkane oxidase in three crystal forms.
Nitroalkane oxidase (NAO), a flavoprotein cloned and purified from Fusarium oxysporum, catalyzes the oxidation of neutral nitroalkanes to the corresponding aldehydes or ketones, with the production of H2O2 and nitrite. In this paper, the crystallization and preliminary X-ray data analysis of three crystal forms of active nitroalkane oxidase are described. The first crystal form belongs to a tri...
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ژورنال
عنوان ژورنال: Bioorganic Chemistry
سال: 2010
ISSN: 0045-2068
DOI: 10.1016/j.bioorg.2009.12.004