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Gene Cluster of Arthrobacter ilicis Rü61a Involved in the Degradation of Quinaldine to Anthranilate
Qox is the first MCD-containing enzyme to be synthesized in a catalytically fully competent form by a heterologous host, and the catalytic properties and the UV-visible and EPR spectra of Qox purified from P. putida KT2440 pKP1 were essentially like those of wild-type Qox. Expand
Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate.
Arthrobacter nitroguajacolicus Rü61a, which utilizes quinaldine as sole source of carbon and energy, was shown to contain a conjugative linear plasmid of approximately 110 kb, named pAL1. It exhibitsExpand
Dioxygenase-mediated quenching of quinolone-dependent quorum sensing in Pseudomonas aeruginosa.
Data indicate that enzyme-mediated PQS inactivation has potential as an antivirulence strategy against P. aeruginosa. Expand
Complete genome sequence and metabolic potential of the quinaldine-degrading bacterium Arthrobacter sp. Rue61a
The genome provides insight into the molecular basis of the versatility and robustness of this environmental Arthrobacter strain and reflects the saprophytic lifestyle and nutritional versatility of the organism and a strong adaptive potential to environmental stress. Expand
Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation
Sequence analysis of ORFs suggested that pAL1 codes for one or two putative terminal proteins, presumed to be covalently bound to the 5' termini, and a multidomain telomere-associated protein (Tap) comprising 1,707 amino acids. Expand
N-Acetylanthranilate Amidase from Arthrobacter nitroguajacolicus Rü61a, an α/β-Hydrolase-Fold Protein Active towards Aryl-Acylamides and -Esters, and Properties of Its Cysteine-Deficient Variant
Sequence analysis and secondary structure predictions indicated that Amq is related to carboxylesterases and belongs to the alpha/beta-hydrolase-fold superfamily of enzymes; inactivation of (His(6)-tagged) Amq by phenylmethanesulfonyl fluoride and diethyl pyrocarbonate and replacement of conserved residues suggested a catalytic triad consisting of S155, E235, and H266. Expand
Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization.
The EPR features of the redox-active centers of P. putida XDH are very similar to those of eukaryotic XDHs/xanthine oxidases, suggesting that the environment of each center and their functionality are analogous in these enzymes. Expand
A safety evaluation of mixed human milk oligosaccharides in rats
HMO MIX I was not genotoxic and did not induce adverse effects in the repeated dose study, providing strong evidence for the safety of HMO Mix I in infant products and general foods. Expand
Biotechnologically produced fucosylated oligosaccharides inhibit the binding of human noroviruses to their natural receptors.
It is found that the simpler fucosylated HMOs were more effective than complex molecules such as LNFP I when inhibiting the binding of G II.17 and GII.17 virus-like particles, and that a combination of simple and complex fucOSylated structures is more likely to prevent norovirus infections. Expand
Catabolic Linear Plasmids
Catabolic gene clusters localized on invertron-type linear plasmids significantly contribute to the ability of actinobacteria to degrade a wide range of organic compounds. Especially in RhodococcusExpand