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1 larity to the beta/alpha-barrel flavoenzyme, old yellow enzyme.
2 orientation different from that reported for old yellow enzyme.
3 ludes identical copies of a gene encoding an old yellow enzyme, a type of flavin-dependent reductase.
5 hift changes on binding to the apoprotein of Old Yellow Enzyme (apoOYE) and apoflavodoxin, whereas bi
8 demonstrated by supplying reduced flavin to Old Yellow Enzyme "ene-reductases" to support asymmetric
9 ase (ER; i.e., OYE2 or OYE3 belonging to the Old Yellow Enzyme family) with an alcohol dehydrogenase
13 ication studies of modified flavins bound to old yellow enzyme have led to predictions about the flav
15 herein likely shared a common ancestor with old yellow enzyme of yeast, a broad-specificity enzyme w
16 s of oxidized flavin mononucleotide (FMN) in old yellow enzyme (OYE) and OYE complexed with p-chlorop
17 e of flavin-binding similar to that found in Old Yellow Enzyme (OYE) and pentaerythritol tetranitrate
22 lidation and show that overexpression of the old yellow enzyme (OYE) reductase increases ROS resistan
28 vering a long sought biological function for Old Yellow Enzyme, these results establish that cellular
29 ted in the light of the crystal structure of old yellow enzyme to reveal that the spectroscopic and m