about
Studies of a ring-cleaving dioxygenase illuminate the role of cholesterol metabolism in the pathogenesis of Mycobacterium tuberculosisStructural and functional analysis of phytotoxin toxoflavin-degrading enzymeThe genome of Tetranychus urticae reveals herbivorous pest adaptationsRing-cleaving dioxygenases with a cupin foldDeciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440Uncovering the protocatechuate 2,3-cleavage pathway genes2-Oxoglutarate: linking TCA cycle function with amino acid, glucosinolate, flavonoid, alkaloid, and gibberellin biosynthesisThe tautomeric half-reaction of BphD, a C-C bond hydrolase. Kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triadSwapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox stateIntermediate in the O−O Bond Cleavage Reaction of an Extradiol Dioxygenase † , ‡Crystal Structure and Functional Analysis of the Extradiol Dioxygenase LapB from a Long-chain Alkylphenol Degradation Pathway in PseudomonasSubstrate Binding Mechanism of a Type I Extradiol DioxygenaseToxoflavin Lyase Requires a Novel 1-His-2-Carboxylate Facial Triad,Structural Basis for the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen ActivationVisualizing the substrate-, superoxo-, alkylperoxo-, and product-bound states at the nonheme Fe(II) site of homogentisate dioxygenaseStructures of aminophenol dioxygenase in complex with intermediate, product and inhibitorLignin valorization through integrated biological funneling and chemical catalysisCharacterizing the promiscuity of LigAB, a lignin catabolite degrading extradiol dioxygenase from Sphingomonas paucimobilis SYK-6Anaerobic catabolism of aromatic compounds: a genetic and genomic view.A polyomic approach to elucidate the fluoranthene-degradative pathway in Mycobacterium vanbaalenii PYR-1The Bark-Beetle-Associated Fungus, Endoconidiophora polonica, Utilizes the Phenolic Defense Compounds of Its Host as a Carbon SourceBacterial degradation of benzoate: cross-regulation between aerobic and anaerobic pathways.High aromatic ring-cleavage diversity in birch rhizosphere: PAH treatment-specific changes of I.E.3 group extradiol dioxygenases and 16S rRNA bacterial communities in soil.OxDBase: a database of oxygenases involved in biodegradation.Role of oxygenases in guiding diverse metabolic pathways in the bacterial degradation of low-molecular-weight polycyclic aromatic hydrocarbons: a review.A C⋅As lyase for degradation of environmental organoarsenical herbicides and animal husbandry growth promoters.Crystallization and preliminary crystallographic analysis of manganese(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from Bacillus sp. JF8.Benzoate metabolism intermediate benzoyl coenzyme A affects gentisate pathway regulation in Comamonas testosteroni.Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris.Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme.Crystal structures of alkylperoxo and anhydride intermediates in an intradiol ring-cleaving dioxygenase.Superoxide dismutases and superoxide reductases.In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase.New dioxygenase from metagenomic library from Brazilian soil: insights into antibiotic resistance and bioremediation.Experimental and computational evidence for the mechanism of intradiol catechol dioxygenation by non-heme iron(III) complexes.A synthetic model of the putative Fe(II)-iminobenzosemiquinonate intermediate in the catalytic cycle of o-aminophenol dioxygenasesStructural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200Horizontal Gene Transfer Contributes to the Evolution of Arthropod Herbivory.Crystal structure of PnpCD, a two-subunit hydroquinone 1,2-dioxygenase, reveals a novel structural class of Fe2+-dependent dioxygenases.A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods.
P2860
Q21131582-16FBAED2-E1FD-4AEE-9C38-5918C178ABD8Q21135296-068A5F69-8A89-4A78-905D-457FB80144FCQ22122161-0FF32C2D-7363-4E69-87B0-A3ECDAC52ECFQ24605922-FFC298C2-0D35-4E47-A0AD-F8DFA66C2B55Q24644289-5EE65B47-F12C-4702-ABBE-E846455F9DF0Q24656257-00F63216-8628-499D-A29B-95966920334AQ27004864-FDA7D971-0526-473D-992B-3179F5E3626DQ27644499-2ED8246F-9931-4D36-8897-C358A063E449Q27650648-37AD6A10-5412-4177-B049-A249730D6F3BQ27652335-F642C0C2-E6B7-497A-B10E-C948267366F4Q27657786-91F4830E-0210-4623-85DD-1B8C1BC35A12Q27664246-C1C5E719-FE1C-4D46-8F4B-4131A376F961Q27666327-254E1515-BDA9-428F-8229-6843EC0D25E7Q27674540-30593845-9D27-4AB6-A60D-28903BF37930Q27679094-742A6095-7082-4D16-9533-F17E06FFA8A0Q27683665-A80213BC-E78A-471A-A8B0-E1F842C145A3Q28654295-42B993C6-43A6-4FF8-A5A7-192594D468DAQ28659011-6F1722A5-B5EA-4A62-9A7F-6A954D56D75DQ28755251-5F5639BE-A6FA-41F8-97B6-72D2639930A6Q28757441-0E405AEE-6BD0-4F78-9F70-6D76E8E9D4E1Q28830653-94FEB10E-7CAA-48C3-9CAD-24785522C60AQ30394031-3D8B1155-A5CA-4AB4-AA12-793F762710A0Q33344760-4A5AAF6B-DF0D-4867-B3B0-15B9177F06D1Q33437226-C5F92FF3-B797-4173-BC54-93B43C7ED05CQ33693798-D0DDCF3F-068E-4E55-AAAA-66D07C963CC7Q33694625-54DE70B0-3D63-49C8-B7C2-DCBBEE77554BQ33707299-ACD8D573-ADA3-4ECA-BEFC-5B492BB29E29Q33743322-4A376B69-C961-413F-8760-F10B86768654Q34033583-A4389271-2365-4221-AD5F-0BC10DCE42C1Q34165579-0C6DA99B-A198-45A6-9A4F-5C0B76CA72A4Q34985604-A5704F39-CC71-4219-B884-36A9A2329D9AQ35049047-181F8B33-3C01-4289-9E77-A9FB34756E56Q35224537-A4D48568-81A6-47F8-B686-EC8F27FA5450Q35637340-474BA46D-A917-4FFF-92C2-E9088EC204F0Q35834921-39DCA2A7-5A73-4BBF-A3B5-53298C60748FQ35882659-4731763E-292E-4D7A-8971-4CA38F861F2FQ36021557-C196DF86-D932-43D6-9738-DB7A406C2BA3Q36053694-831E824C-8C4B-4BBA-960C-D9B1FD32268EQ36115886-A7D3F97F-4D9D-49EB-BE0C-71B56BBB8AE1Q36240394-4EC8B686-B601-4FC1-820D-F937EB7F70DE
P2860
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
The ins and outs of ring-cleaving dioxygenases.
@ast
The ins and outs of ring-cleaving dioxygenases.
@en
type
label
The ins and outs of ring-cleaving dioxygenases.
@ast
The ins and outs of ring-cleaving dioxygenases.
@en
prefLabel
The ins and outs of ring-cleaving dioxygenases.
@ast
The ins and outs of ring-cleaving dioxygenases.
@en
P2860
P1476
The ins and outs of ring-cleaving dioxygenases
@en
P2093
Frédéric H Vaillancourt
Jeffrey T Bolin
P2860
P304
P356
10.1080/10409230600817422
P577
2006-07-01T00:00:00Z