title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger.
abstract: Monoamine oxidase from Aspergillus niger (MAO-N) is an FAD-dependent enzyme that catalyses the conversion of terminal amines to their corresponding aldehydes. Variants of MAO-N produced by directed evolution have been shown to possess altered substrate specificity. Crystals of two of these variants (MAO-N-3 and MAO-N-5) have been obtained; the former displays P2(1) symmetry with eight molecules per asymmetric unit and the latter has P4(1)2(1)2 or P4(3)2(1)2 symmetry and two molecules per asymmetric unit. Solution of these structures will help shed light on the molecular determinants of improved activity and high enantioselectivity towards a broad range of substrates.
authors.affiliation: Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England.
authors.forename: Kate E
authors.initials: KE
authors.lastname: Atkin
authors.forename: Renate
authors.initials: R
authors.lastname: Reiss
authors.forename: Nicholas J
authors.initials: NJ
authors.lastname: Turner
authors.forename: Andrzej M
authors.initials: AM
authors.lastname: Brzozowski
authors.forename: Gideon
authors.initials: G
authors.lastname: Grogan
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D015870:Gene Expression / Q000235:genetics*; D008995:Monoamine Oxidase / Q000097:blood* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D008995:Monoamine Oxidase