Proteomics

Dataset Information

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Proteomic analysis of the papaverine degrading Arthrobacter sp.


ABSTRACT: In previous work in our group, shotgun genome sequencing of Arthrobacter sp. revealed potential new P450 monooxygenases and many other oxidoreductases with putative hydroxylation activity. A targeted approach to identify enzymes involved in the degradation of certain molecules is proteomic analysis. In the case of growth on certain substances, enzymes like P450s, which are responsible for the observed organism’s capabilities, might be overexpressed or initially induced.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Arthrobacter Sp. Hg

SUBMITTER: Jan Klenk  

LAB HEAD: Bernhard Hauer

PROVIDER: PXD009566 | Pride | 2019-02-19

REPOSITORIES: Pride

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Publications

Identification and characterization of cytochrome P450 1232A24 and 1232F1 from Arthrobacter sp. and their role in the metabolic pathway of papaverine.

Klenk Jan M JM   Fischer Max-Philipp MP   Dubiel Paulina P   Sharma Mahima M   Rowlinson Benjamin B   Grogan Gideon G   Hauer Bernhard B  

Journal of biochemistry 20190701 1


Cytochrome P450 monooxygenases (P450s) play crucial roles in the cell metabolism and provide an unsurpassed diversity of catalysed reactions. Here, we report the identification and biochemical characterization of two P450s from Arthrobacter sp., a Gram-positive organism known to degrade the opium alkaloid papaverine. Combining phylogenetic and genomic analysis suggested physiological roles for P450s in metabolism and revealed potential gene clusters with redox partners facilitating the reconstit  ...[more]

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