Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution
about
Ring-cleaving dioxygenases with a cupin foldSite-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sitesChlorocatechols substituted at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase of Pseudomonas chlororaphis RW71Genetic and biochemical characterization of a 2-pyrone-4, 6-dicarboxylic acid hydrolase involved in the protocatechuate 4, 5-cleavage pathway of Sphingomonas paucimobilis SYK-6Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.Structural trees for protein superfamilies.Key aromatic-ring-cleaving enzyme, protocatechuate 3,4-dioxygenase, in the ecologically important marine Roseobacter lineage.Life in a sea of oxygen.Bacterial degradation of chlorophenols: pathways, biochemica, and genetic aspects.Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenaseSubstrate activation for O2 reactions by oxidized metal centers in biologyAll in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.The ins and outs of ring-cleaving dioxygenases.Diversity of the ring-cleaving dioxygenase gene pcaH in a salt marsh bacterial community.Positive selection for mutations affecting bioconversion of aromatic compounds in Agrobacterium tumefaciens: analysis of spontaneous mutations in the protocatechuate 3,4-dioxygenase gene.Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activityCombining localized PCR mutagenesis and natural transformation in direct genetic analysis of a transcriptional regulator gene, pobR.EPR studies of chlorocatechol 1,2-dioxygenase: evidences of iron reduction during catalysis and of the binding of amphipatic moleculesHigh activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production.Cloning, expression, and characterization of catechol 1,2-dioxygenase from a phenol-degrading Candida tropicalis JH8 strain.Iron(III) complexes of tripodal tetradentate 4N ligands as functional models for catechol dioxygenases: the electronic vs. steric effect on extradiol cleavage.Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation.Biomimetic iron(III) complexes of facially and meridionally coordinating tridentate 3N ligands: tuning of regioselective extradiol dioxygenase activity in organized assemblies.Biomimetic iron(III) complexes of N3O and N3O2 donor ligands: protonation of coordinated ethanolate donor enhances dioxygenase activity.Iron(III) complexes of N2O and N3O donor ligands as functional models for catechol dioxygenase enzymes: ether oxygen coordination tunes the regioselectivity and reactivity.In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL: the protocatechuate branch of the β-ketoadipate pathway in Rhodococcus jostii RHA1.XAS characterization of the active sites of novel intradiol ring-cleaving dioxygenases: hydroxyquinol and chlorocatechol dioxygenases
P2860
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P2860
Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution
description
1994 nî lūn-bûn
@nan
1994 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@ast
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@en
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@nl
type
label
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@ast
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@en
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@nl
prefLabel
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@ast
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@en
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@nl
P356
P1476
Structure of protocatechuate 3 ...... eruginosa at 2.15 A resolution
@en
P2093
D H Ohlendorf
J D Lipscomb
P304
P356
10.1006/JMBI.1994.1754
P577
1994-12-01T00:00:00Z