| Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes. | Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes.
Decembrino D, Girhard M, Urlacher VB., Free PMC Article | 12/4/2021 |
| The cuprous oxidase activity of these mutants was about 20% that of wild-type CueO. These structural features of the G304K mutant provide clues for designing specific substrate-binding mutants in the biotechnological applications. | Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity.
Wang H, Liu X, Zhao J, Yue Q, Yan Y, Gao Z, Dong Y, Zhang Z, Fan Y, Tian J, Wu N, Gong Y., Free PMC Article | 12/14/2019 |
| Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO has been presented. | Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography.
Akter M, Inoue C, Komori H, Matsuda N, Sakurai T, Kataoka K, Higuchi Y, Shibata N., Free PMC Article | 11/26/2017 |
| Exogenous acetate ion reaches the type II copper center in CueO through the water-excretion channel and potentially affects the enzymatic activity. | Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity.
Komori H, Kataoka K, Tanaka S, Matsuda N, Higuchi Y, Sakurai T., Free PMC Article | 11/25/2017 |
| the binding of copper to apo-CueO greatly stabilized the protein, indicating a transformation from an open or flexible domain arrangement with accessible copper sites to a closed structure with deeply buried copper ions. | The Tat Substrate CueO Is Transported in an Incomplete Folding State.
Stolle P, Hou B, Brüser T., Free PMC Article | 12/17/2016 |
| The results provides evidence that CueO possesses high Mn(II) oxidase activity and generates biogenic Mn oxide gamma-Mn3O4. | Catalytic oxidation of manganese(II) by multicopper oxidase CueO and characterization of the biogenic Mn oxide.
Su J, Deng L, Huang L, Guo S, Liu F, He J. | 01/17/2015 |
| At low levels of X-ray exposure, unambiguous electron density for an O atom is observed inside the trinuclear copper center (TNC); binding of oxygen to the TNC after its full reduction is observed in the case of the laccase. | New insights into the catalytic active-site structure of multicopper oxidases.
Komori H, Sugiyama R, Kataoka K, Miyazaki K, Higuchi Y, Sakurai T. | 08/23/2014 |
| Laccase activities of CueO were maximally enhanced 140-fold by virtue of the synergistic effect of mild mutations at and at around the ligand groups to type I copper. | Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center.
Kataoka K, Kogi H, Tsujimura S, Sakurai T. | 08/31/2013 |
| These results exerted on the hydrogen bond network in CueO are discussed in comparison with proton transfers in cytochrome oxidase. | Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities.
Kajikawa T, Kataoka K, Sakurai T. | 08/18/2012 |
| The results revealed that the crude CueO catalyzed the oxidation of anthracene and benzo[a]pyrene in the same way as the fungal laccase from Trametes versicolor, but showed specific characteristics such as thermostability and copper dependence. | Oxidation of polycyclic aromatic hydrocarbons by the bacterial laccase CueO from E. coli.
Zeng J, Lin X, Zhang J, Li X, Wong MH. | 05/28/2011 |
| Data indicate that the methionine-rich alpha-helices of CueO function as a barrier to the access of bulky organic substrates, which provides CueO with specificity as a cuprous oxidase. | Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.
Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T. | 01/21/2010 |
| N-terminus verified by Edman degradation on mature peptide | Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Link AJ, Robison K, Church GM. | 11/5/2007 |
| Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. | The multicopper oxidase (CueO) and cell aggregation in Escherichia coli.
Tree JJ, Ulett GC, Hobman JL, Constantinidou C, Brown NL, Kershaw C, Schembri MA, Jennings MP, McEwan AG. | 01/21/2010 |
| has robust cuprous oxidase activity which is central to the mechanism by which CueO protects E coli against copper toxicity | Cuprous oxidase activity of CueO from Escherichia coli.
Singh SK, Grass G, Rensing C, Montfort WR., Free PMC Article | 01/21/2010 |
| Copper toxicity towards a cueO mutant could be suppressed by addition of the superoxide quencher 1,2-dihydroxybenzene-3,5-disulfonic acid (tiron), suggesting that a primary cause of copper toxicity is the copper-catalyzed production of superoxide anions. | Copper sensitivity of cueO mutants of Escherichia coli K-12 and the biochemical suppression of this phenotype.
Tree JJ, Kidd SP, Jennings MP, McEwan AG. | 01/21/2010 |