Exemplar Abstract for Arthrobacter globiformis (Conn 1928) Conn and Dimmick 1947 (Approved Lists 1980) emend. Nouioui et al. 2018.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Arthrobacter Globiformis

scholarly journals DEER and RIDME Measurements of the Nitroxide-Spin Labelled Copper-Bound Amine Oxidase Homodimer from Arthrobacter Globiformis

2021 ◽  
Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  
Keyword(s):  
Dipolar Coupling ◽  
Amine Oxidase ◽  
Spin Labels ◽  
Arthrobacter Globiformis ◽  
Copper Amine Oxidase ◽  
Dipole Interactions ◽  
Nitroxide Spin Labels ◽  
Double Electron Electron Resonance ◽  
Dipolar Modulation ◽  
Paramagnetic Centres

AbstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.

Dormant forms of Micrococcus luteus and Arthrobacter globiformis not platable on standard media

Microbiology ◽  
2009 ◽  
Vol 78 (4) ◽  
pp. 407-418 ◽  
Author(s):  
A. L. Mulyukin ◽  
E. V. Demkina ◽  
N. A. Kryazhevskikh ◽  
N. E. Suzina ◽  
L. I. Vorob’eva ◽  
...  
Keyword(s):  
Micrococcus Luteus ◽  
Arthrobacter Globiformis ◽  
Dormant Forms

scholarly journals Genome Sequence of Bacteriophage Adumb2043, Isolated from Arthrobacter globiformis in Southern Colorado

2021 ◽  
Vol 10 (41) ◽  
Author(s):  
Darien Brown ◽  
Shannon Isenhart ◽  
Auremie Kleven ◽  
Adam Gillison ◽  
Lee Anne Martínez ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Trna Genes ◽  
Arthrobacter Globiformis ◽  
Protein Coding ◽  
Content Type ◽  
Colorado Springs ◽  
Protein Coding Genes

We report the discovery and genome sequence of phage Adumb2043, a siphovirus infecting Arthrobacter globiformis , B2979-SEA. Adumb2043 was isolated from soil collected in Colorado Springs, Colorado. The genome has a length of 43,100 bp and contains 68 predicted protein-coding genes and no tRNA genes. Adumb2043 is related to actinobacteriophages Elezi and London.

Degradation of (–)-Ephedrine by Pseudomonas putida Detection of (–)-Ephedrine: NAD+-oxidoreductase from Arthrobacter globiformis

1980 ◽  
Vol 35 (1-2) ◽  
pp. 80-87 ◽  
Author(s):  
E. Klamann ◽  
F. Lingens
Keyword(s):  
Pseudomonas Putida ◽  
Enrichment Culture ◽  
Culture Fluid ◽  
Sole Source ◽  
Culture Technique ◽  
Arthrobacter Globiformis ◽  
Muconic Acid ◽  
Ammonium Sulphate Precipitation ◽  
Wide Range ◽  
Nad Oxidoreductase

Abstract A bacterium utilizing the alkaloid (-)-ephedrine as its sole source of carbon was isolated by an enrichment-culture technique from soil supplemented with 4-benzoyl-1,3-oxazolidinon-(2). The bacterium was identified as Pseudomonasputida by morphological and physiological studies. The following metabolites were isolated from the culture fluid: methylamine, formaldehyde, methyl- benzoylcarbinol (2-hydroxy-1-oxo-1-phenylpropane), benzoid acid, pyrocatechol and cis, cis- muconic acid. A pathway for the degradation of (-)-ephedrine by Pseudomonas putida is proposed and compared with the degradative pathway in Arthrobacter globiformis.The enzyme, which is responsible for the first step in the catabolism of (-)-ephedrine could be demonstrated in extracts from Arthrobacter globiformis. This enzyme catalyses the dehydrogena- tion of (-)-ephedrine yielding phenylacetylcarbinol/methylbenzoylcarbinol and methylamine. It requires NAD+ as cofactor and exhibits optimal activity at pH 11 in 0.1 m glycine/NaOH buffer. The Km value for (-)-ephedrine is 0.02 mM and for NAD+ 0.11 mм, respectively. No remarkable loss of activity is observed following treatment with EDTA. The enzyme has been shown to react with a wide range of ethanolamines. A slight enrichment was obtained by ammonium sulphate precipitation. The name (-)-ephedrine: NAD+-oxidoreductase (deaminating) is proposed.

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