Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger.
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.
Atkin
Kate E
KE
Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England.
Reiss
Renate
R
Turner
Nicholas J
NJ
Brzozowski
Andrzej M
AM
Grogan
Gideon
G
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
D008995:Monoamine Oxidase