NDLI: Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1.

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Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mihasan, Marius Stefan, Marius Hritcu, Lucian Artenie, Vlad Brandsch, Roderich
Description	Country affiliation: Romania Author Affiliation: Mihasan M ( Department of Biology, Alexandru Ioan Cuza University, no 20 A, 700505 Iasi, Romania. marius.mihasan@uaic.ro)
Abstract	Due to its high abundance, the D-xylose fraction of lignocellulose provides a promising resource for production of various chemicals. Examples of efficient utilization of d-xylose are nevertheless rare, mainly due to the lack of enzymes with suitable properties for biotechnological applications. The genus Arthrobacter, which occupies an ecological niche rich in lignocellulosic materials and containing species with high resistance and tolerance to environmental factors, is a very suitable candidate for finding D-xylose-degrading enzymes with new properties. In this work, the presence of the pAO1 megaplasmid in cells of Arthrobacter nicotinovorans was directly linked to the ability of this microorganism to ferment D-xylose and to sustain longer log growth. Three pAO1 genes (orf32, orf39, orf40) putatively involved in degradation of xylose were identified and cloned, and the corresponding proteins purified and characterized. ORF40 was shown to be a homotetrameric NADP(+)/NAD(+) sugar dehydrogenase with a strong preference for d-xylose; ORF39 is a monomeric aldehyde dehydrogenase with wide substrate specificity and ORF32 is a constitutive expressed transcription factor putatively involved in control of the entire catabolic pathway. Based on analogies with other pentose degradation pathways, a putative xylose oxidative pathway similar to the Weimberg pathway is postulated.
File Format	HTM / HTML
ISSN	09232508
Issue Number	1
Volume Number	164
e-ISSN	17697123
Journal	Research in Microbiology
Language	English
Publisher	Elsevier
Publisher Date	2013-01-01
Publisher Place	France
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Microbiology Aldehyde Oxidase Genetics Metabolism Arthrobacter Metabolic Networks And Pathways Plasmids Xylose Growth & Development Culture Media Gene Expression Gene Order Open Reading Frames Oxidation-reduction Recombinant Fusion Proteins Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Microbiology

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Sequence of the 165-Kilobase Catabolic Plasmid pAO1 from Arthrobacter nicotinovorans and Identification of a pAO1-Dependent Nicotine Uptake System

Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans.

Arthrobacter nicotinovorans and identification of a pao1-dependent nicotine uptake system (2002).

Plasmid-Encoded Phthalate Catabolic Pathway in Arthrobacter keyseri 12B†

Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans

PAO1 of Arthrobacter nicotinovorans and the Spread of Catabolic Traits by Horizontal Gene Transfer in Gram-Positive Soil Bacteria

References content alerts gene cluster on pao1 of arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of (2001).

A novel gamma-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1.

In-silico evidence of a pAO1 encoded pathway for the catabolism of tagatose derivatives in Arthrobacter nicotinovorans

Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1.

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Sequence of the 165-Kilobase Catabolic Plasmid pAO1 from Arthrobacter nicotinovorans and Identification of a pAO1-Dependent Nicotine Uptake System

Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans.

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