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1 e oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed
5 Criegee rearrangement steps of intradiol and extradiol catechol dioxygenases: a direct 1,2-alkenyl mi
7 ygenases: a direct 1,2-alkenyl migration for extradiol cleavage and an O-O homolytic cleavage mechani
8 s studies of a biomimetic model reaction for extradiol cleavage have highlighted the importance of ac
11 ve site Fe(II) and O(2) to catalyze proximal extradiol cleavage of the aromatic ring of the substrate
13 nane (TACN), and pyridine in methanol is the extradiol cleavage product 2-hydroxymuconic semi-aldehyd
14 mutant enzyme was catalytically inactive for extradiol cleavage, indicating the essential nature of t
15 e for iron(II) rather than iron(III) for the extradiol cleavage, which parallels the selectivity of t
20 the case with the superoxide dismutases, the extradiol-cleaving catechol dioxygenases appear to utili
22 genase family, the transient kinetics of the extradiol dioxygenase catalytic cycle have been difficul
27 e gene product, ArsI, is an Fe(II)-dependent extradiol dioxygenase that cleaves the carbon-arsenic (C
28 mutant enzymes allow the oxygen adduct of an extradiol dioxygenase to be detected for the first time.
29 epimerase), oxidative cleavage of C-C bonds (extradiol dioxygenase), and nucleophilic substitutions (
31 tallographic studies of an Fe(2+)-containing extradiol dioxygenase, no evidence for a superoxo or per
32 meric enzymes belong to the type I family of extradiol dioxygenases (vicinal oxygen chelate superfami
33 site architectures, and Fe(2+) coordination, extradiol dioxygenases can proceed through the same prin
34 ite structures of these enzymes suggest that extradiol dioxygenases cannot differentially compensate
35 y I.2.A, which includes the largest group of extradiol dioxygenases described by culture-dependent st
36 lkylperoxo intermediates from the intra- and extradiol dioxygenases provides a rationale for site spe
37 pha-keto acid-dependent enzymes and with the extradiol dioxygenases show that members of these famili
38 y of metalloenzymes containing glyoxalase I, extradiol dioxygenases, and methylmalonyl-CoA epimerase.
39 entified in the active site of the class III extradiol dioxygenases, positioned within 4-5 A of the i
44 bstituted oxygenase has been observed in the extradiol ring cleavage of the electron-poor substrate 4
47 oli catalyses the hydrolytic cleavage of the extradiol ring fission product on the phenylpropionate c
49 d the first room temperature structure of an extradiol ring-cleaving dioxygenase was solved by utiliz
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