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Volumn 11, Issue 2, 2007, Pages 195-202

Flavoenzymes

Author keywords

[No Author keywords available]

Indexed keywords

FLAVOPROTEIN; OXIDOREDUCTASE; REBECCAMYCIN; TRYPTOPHAN OXIDASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 34047118271     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2007.01.010     Document Type: Review
Times cited : (237)

References (59)
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    • First insight into the structural properties of single-component Baeyer-Villiger monooxygenases. The structure of phenylacetone monooxygenase exhibits a two-domain architecture resembling that of the disulfide oxidoreductases. An arginine residue oriented near the flavin ring is assumed to stabilize the flavin-peroxide and Criegee intermediates. Domain rotations are proposed to bring about the conformational changes involved in catalysis.
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    • Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action
    • First 3D structure of a flavin reductase that uses FAD both as a substrate and as a prosthetic group.
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