Structure of the monooxygenase component of a two-component flavoprotein monooxygenase
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چکیده
منابع مشابه
Structure of the monooxygenase component of a two-component flavoprotein monooxygenase.
p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase (C2) that uses reduced FMN as substrate. The crystal structures of C2 in the ligand-free and substrate-bound forms reveal a preorganized pocket that binds reduced FMN without large conformational changes. The Phe-266 side chain swings out to ...
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Mycobacterium tuberculosis belongs to a large family of soil bacteria which can degrade a remarkably broad range of organic compounds and utilize them as carbon, nitrogen and energy sources. It has been proposed that a variety of mycobacteria can subsist on alternative carbon sources during latency within an infected human host, with the help of enzymes such as nitrilotriacetate monooxygenase (...
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The spectral changes of the enzyme-hound FAD were investigated in the anaerobic and aerobic reactions of lysine monooxygenase, a flavoprotein. Under anaerobic conditions, the enzyme FAD was fully reduced with lysine via a transient intermediate having a broad absorption band in the long wavelength region. This anaerobic species was presumably involved in the dehydrogenation of lysine leading to...
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A generic approach for flavoenzyme immobilization was developed in which the flavin cofactor is used for anchoring enzymes onto the carrier. It exploits the tight binding of flavin cofactors to their target apo proteins. The method was tested for phenylacetone monooxygenase (PAMO) which is a well-studied and industrially interesting biocatalyst. Also a fusion protein was tested: PAMO fused to p...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2007
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0608381104