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Literature summary for 1.14.12.22 extracted from

  • Nojiri, H.; Ashikawa, Y.; Noguchi, H.; Nam, J.W.; Urata, M.; Fujimoto, Z.; Uchimura, H.; Terada, T.; Nakamura, S.; Shimizu, K.; Yoshida, T.; Habe, H.; Omori, T.
    Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase (2005), J. Mol. Biol., 351, 355-370.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminal His-tagged form of terminal oxygenase CarAaJ3 in Escherichia coli Janthinobacterium sp. J3

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of oxygenase component CARDO-O at a resolution of 1.95 A, and of selenomethione derivative to 2.3 A resolution. The alpha3 trimeric overall structure of the CARDO-O molecule roughly corresponds to the alpha3 partial structures of other terminal oxygenase components of Rieske non-heme iron oxygenase systems that have the alpha3beta3 configuration and reveals the presence of the specific loops that interact with a neighboring subunit. The shape of the substrate-binding pocket of CARDO-O is markedly different from those of other oxygenase components involved in naphthalene and biphenyl degradation pathways. Docking simulations suggest that carbazole binds to the substrate-binding pocket in a manner suitable for catalysis of angular dioxygenation Janthinobacterium sp. J3

Organism

Organism UniProt Comment Textmining
Janthinobacterium sp. J3
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