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1 es (PCADs) has been characterized in several extradiol aromatic compound degradation pathways.
2 e oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed
3                                      For the extradiol aromatic ring-cleaving dioxygenases, we have p
4                                          The extradiol catechol dioxygenases catalyze the non-heme ir
5 tinases but similar to that proposed for the extradiol catechol dioxygenases.
6 Criegee rearrangement steps of intradiol and extradiol catechol dioxygenases: a direct 1,2-alkenyl mi
7                                              Extradiol catecholic dioxygenases catalyze the cleavage
8 ygenases: a direct 1,2-alkenyl migration for extradiol cleavage and an O-O homolytic cleavage mechani
9 s studies of a biomimetic model reaction for extradiol cleavage have highlighted the importance of ac
10                               In particular, extradiol cleavage in the presence of iron(II) shows a r
11                      Under these conditions, extradiol cleavage of a range of 3- and 4-substituted ca
12 ve site Fe(II) and O(2) to catalyze proximal extradiol cleavage of the aromatic ring of the substrate
13 ve site Fe(II) and O(2) to catalyze proximal extradiol cleavage of the substrate aromatic ring.
14 nane (TACN), and pyridine in methanol is the extradiol cleavage product 2-hydroxymuconic semi-aldehyd
15 mutant enzyme was catalytically inactive for extradiol cleavage, indicating the essential nature of t
16 e for iron(II) rather than iron(III) for the extradiol cleavage, which parallels the selectivity of t
17 tent with a direct 1,2-alkenyl migration for extradiol cleavage.
18 tituents, implying a different mechanism for extradiol cleavage.
19 ving insight into the acid/base chemistry of extradiol cleavage.
20             Whereas all other members of the extradiol-cleaving catechol dioxygenase family are iron-
21 the case with the superoxide dismutases, the extradiol-cleaving catechol dioxygenases appear to utili
22 te for ring cleavage that is performed by an extradiol dioxygenase (BbdF) producing 2,4,6-trioxohepta
23 , implying a role for an acidic group in the extradiol dioxygenase active site.
24 genase family, the transient kinetics of the extradiol dioxygenase catalytic cycle have been difficul
25 us to methods used in earlier studies on the extradiol dioxygenase catechol 2,3-dioxygenase.
26 vage, which parallels the selectivity of the extradiol dioxygenase family.
27                   In contrast, incubation of extradiol dioxygenase MhpB from Escherichia coli with 6-
28 volved metapyrocatechase (MPC), a nonheme Fe extradiol dioxygenase not previously studied in new-to-n
29 ransient intermediates to be reported for an extradiol dioxygenase reaction.
30 e gene product, ArsI, is an Fe(II)-dependent extradiol dioxygenase that cleaves the carbon-arsenic (C
31 mutant enzymes allow the oxygen adduct of an extradiol dioxygenase to be detected for the first time.
32 epimerase), oxidative cleavage of C-C bonds (extradiol dioxygenase), and nucleophilic substitutions (
33                                          The extradiol dioxygenase, 2,3-dihydroxybiphenyl 1,2-dioxyge
34 iacols, involves a phylogenetically distinct extradiol dioxygenase, AphC, previously misannotated as
35 tallographic studies of an Fe(2+)-containing extradiol dioxygenase, no evidence for a superoxo or per
36 onally-independent enzyme classes (esterase, extradiol dioxygenase, phosphatase, beta-galactosidase,
37 ged to a newly defined subfamily of type I.2 extradiol dioxygenases (EDOs).
38 meric enzymes belong to the type I family of extradiol dioxygenases (vicinal oxygen chelate superfami
39 site architectures, and Fe(2+) coordination, extradiol dioxygenases can proceed through the same prin
40 ite structures of these enzymes suggest that extradiol dioxygenases cannot differentially compensate
41 y I.2.A, which includes the largest group of extradiol dioxygenases described by culture-dependent st
42 nd stability profiles of 228 esterases and 5 extradiol dioxygenases from sediment and seawater across
43 lkylperoxo intermediates from the intra- and extradiol dioxygenases provides a rationale for site spe
44 pha-keto acid-dependent enzymes and with the extradiol dioxygenases show that members of these famili
45 y of metalloenzymes containing glyoxalase I, extradiol dioxygenases, and methylmalonyl-CoA epimerase.
46 entified in the active site of the class III extradiol dioxygenases, positioned within 4-5 A of the i
47 1 is very similar to that of iron-containing extradiol dioxygenases, which also display a similar str
48 well-characterized Fe(II)-dependent catechol extradiol dioxygenases.
49 t sequence similarity to an unusual class of extradiol dioxygenases.
50 lyoxalase I and the Mn2+- or Fe2+-containing extradiol dioxygenases.
51 gnin, and the determinants of specificity in extradiol dioxygenases.
52 (4NC), which is also cleaved in the proximal extradiol position.
53 bstituted oxygenase has been observed in the extradiol ring cleavage of the electron-poor substrate 4
54  downstream from dntD, the gene encoding the extradiol ring fission enzyme of the pathway.
55 -6-oxo-2,4-hexadienoic acid, consistent with extradiol ring fission of THT.
56 oli catalyses the hydrolytic cleavage of the extradiol ring fission product on the phenylpropionate c
57 te the catechol-substituted substrate for an extradiol ring-cleavage dioxygenase (AtLigB).
58 d the first room temperature structure of an extradiol ring-cleaving dioxygenase was solved by utiliz
59  O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase.