Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger

被引：29

作者：

Atkin, Kate E. ^{[1
]}

Reiss, Renate ^{[2
]}

Turner, Nicholas J. ^{[2
]}

Brzozowski, Andrzej M. ^{[1
]}

Grogan, Gideon ^{[1
]}

机构：

[1] Univ York, Dept Chem, Struct Biol Lab, York YO10 5YW, N Yorkshire, England

[2] Univ Manchester, Sch Chem, Manchester Interdisciplinary Bioctr, Manchester M1 7DN, Lancs, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1107/S174430910800345X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：182 / 185

页数：4

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