3we0 | pdb_00003we0

L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813

spinqualitylabelsall models 3we0, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3we0 is a 2 chain structure with sequence from Achromobacter georgiopolitanum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD Gene: laao (Achromobacter georgiopolitanum) Activity: L-amino-acid oxidase, with EC number 1.4.3.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed In this study, it was shown for the first time that l-amino acid oxidase of Pseudomonas sp. AIU813, renamed as l-amino acid oxidase/monooxygenase (l-AAO/MOG), exhibits l-lysine 2-monooxygenase as well as oxidase activity. l-Lysine oxidase activity of l-AAO/MOG was increased in a p-chloromercuribenzoate (p-CMB) concentration-dependent manner to a final level that was five fold higher than that of the non-treated enzyme. In order to explain the effects of modification by the sulfhydryl reagent, saturation mutagenesis studies were carried out on five cysteine residues, and we succeeded in identifying l-AAO/MOG C254I mutant enzyme, which showed five-times higher specific activity of oxidase activity than that of wild type. The monooxygenase activity shown by the C254I variant was decreased significantly. Moreover, we also determined a high-resolution three-dimensional structure of l-AAO/MOG to provide a structural basis for its biochemical characteristics. The key residue for the activity conversion of l-AAO/MOG, Cys-254, is located near the aromatic cage (Trp-418, Phe-473, and Trp-516). Although the location of Cys-254 indicates that it is not directly involved in the substrate binding, the chemical modification by p-CMB or C254I mutation would have a significant impact on the substrate binding via the side chain of Trp-516. It is suggested that a slight difference of the binding position of a substrate can dictate the activity of this type of enzyme as oxidase or monooxygenase. Mutational and crystallographic analysis of l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities.,Matsui D, Im DH, Sugawara A, Fukuta Y, Fushinobu S, Isobe K, Asano Y FEBS Open Bio. 2014 Feb 7;4:220-8. doi: 10.1016/j.fob.2014.02.002. eCollection, 2014. PMID:24693490 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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