Literature

Abstract

The Baeyer-Villiger monooxygenase MtmOIV from Streptomyces argillaceus is a 56 kDa FAD-dependent and NADPH-dependent enzyme that is responsible for the key frame-modifying step in the biosynthesis of the natural product mithramycin. Crystals of MtmOIV were flash-cooled and diffracted to 2.69 A resolution using synchrotron radiation on beamline SER-CAT 22-ID at the Advanced Photon Source. Crystals of MtmOIV are monoclinic and light-scattering data reveal that the enzyme forms dimers in solution. The rotation function suggests the presence of two dimers in the asymmetric unit. L-Selenomethionine-incorporated MtmOIV has been obtained. Structural solution combining molecular-replacement phases and anomalous phases from selenium is in progress.

DOI： 10.1107/S1744309105033221

Crystallization and X-ray diffraction properties of Baeyer–Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway inStreptomyces argillaceus

Acta Crystallographica Section F Structural Biology and Crystallization Communications 2005.0

Characterization of Kinetics and Products of the Baeyer−Villiger Oxygenase MtmOIV, The Key Enzyme of the Biosynthetic Pathway toward the Natural Product Anticancer Drug Mithramycin from Streptomyces argillaceus

Journal of the American Chemical Society 2005.0

Purification and Characterization of a Monooxygenase Involved in the Biosynthetic Pathway of the Antitumor Drug Mithramycin

Journal of Bacteriology 2003.0

The mtmVUC genes of the mithramycin gene cluster in Streptomycesargillaceus are involved in the biosynthesis of the sugar moieties

Molecular Genetics and Genomics 2001.0

Cloning and insertional inactivation of Streptomyces argillaceus genes involved in the earliest steps of biosynthesis of the sugar moieties of the antitumor polyketide mithramycin

Journal of Bacteriology 1997.0

Analysis of two chromosomal regions adjacent to genes for a type II polyketide synthase involved in the biosynthesis of the antitumor polyketide mithramycin in Streptomyces argillaceus