Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger
Author(s) -
Atkin Kate E.,
Reiss Renate,
Turner Nicholas J.,
Brzozowski Andrzej M.,
Grogan Gideon
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910800345x
Subject(s) - aspergillus niger , monoamine oxidase , molecule , crystallization , enzyme , substrate (aquarium) , oxidase test , cloning (programming) , chemistry , stereochemistry , crystallography , biochemistry , biology , organic chemistry , ecology , computer science , programming language
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 P 2 1 symmetry with eight molecules per asymmetric unit and the latter has P 4 1 2 1 2 or P 4 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.