A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO
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Contribution of copper ion resistance to survival of Escherichia coli on metallic copper surfacesThe Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like StructureX-ray analysis of bilirubin oxidase fromMyrothecium verrucariaat 2.3 Å resolution using a twinned crystalCrystal structure of an ascomycete fungal laccase from Thielavia arenaria--common structural features of asco-laccasesCrystal structure of the multicopper oxidase from the pathogenic bacterium Campylobacter jejuni CGUG11284: characterization of a metallo-oxidaseLaccase versus laccase-like multi-copper oxidase: a comparative study of similar enzymes with diverse substrate spectraCopper active sites in biologyCharacterization of SLAC: a small laccase from Streptomyces coelicolor with unprecedented activity.Atmospheric N deposition increases bacterial laccase-like multicopper oxidases: implications for organic matter decay.The multi-copper-ion oxidase CueO of Salmonella enterica serovar Typhimurium is required for systemic virulence.The copper-iron connection in biology: structure of the metallo-oxidase Fet3p.Evidence for lignin oxidation by the giant panda fecal microbiome.Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequenceSurface Mn(II) oxidation actuated by a multicopper oxidase in a soil bacterium leads to the formation of manganese oxide mineralsThe first acidobacterial laccase-like multicopper oxidase revealed by metagenomics shows high salt and thermo-tolerance.Mn(II,III) oxidation and MnO2 mineralization by an expressed bacterial multicopper oxidase.X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.Cuprous oxidase activity of CueO from Escherichia coli.Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.Three-dimensional structures of laccases.Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium Aurantimonas sp. strain SI85-9A1.Bioinformatic analysis reveals high diversity of bacterial genes for laccase-like enzymes.Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production.Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography.Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli.Copper import in Escherichia coli by the yersiniabactin metallophore system.Multireference ab initio calculations of g tensors for trinuclear copper clusters in multicopper oxidasesA Multicopper oxidase (Cj1516) and a CopA homologue (Cj1161) are major components of the copper homeostasis system of Campylobacter jejuni.Differential expression of the three multicopper oxidases from Myxococcus xanthus.The copper-inducible cin operon encodes an unusual methionine-rich azurin-like protein and a pre-Q0 reductase in Pseudomonas putida KT2440The Tat Substrate CueO Is Transported in an Incomplete Folding StateDirect identification of a bacterial manganese(II) oxidase, the multicopper oxidase MnxG, from spores of several different marine Bacillus species.Molecular cloning of a copper-dependent laccase from the dye-decolorizing strain Stenotrophomonas maltophilia AAP56.Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.Substrate specificity and copper loading of the manganese-oxidizing multicopper oxidase Mnx from Bacillus sp. PL-12.Bacterial laccase: recent update on production, properties and industrial applications.A novel quantum dot-laccase hybrid nanobiosensor for low level determination of dopamine.A new ferrous iron-uptake transporter, EfeU (YcdN), from Escherichia coli.Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen.
P2860
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P2860
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@ast
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@en
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@nl
type
label
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@ast
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@en
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@nl
prefLabel
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@ast
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@en
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@nl
P2093
P2860
P356
P1476
A labile regulatory copper ion ...... n the multicopper oxidase CueO
@en
P2093
Andrzej Weichsel
Christopher Rensing
Gregor Grass
Gunter F Wildner
Sue A Roberts
William R Montfort
P2860
P304
P356
10.1074/JBC.M302963200
P407
P577
2003-08-22T00:00:00Z