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

Kate E. Atkin; Renate Reiss; Nicholas J. Turner; Andrzej M. Brzozowski; Gideon Grogan

doi:10.1107/S174430910800345X

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

Kate E. Atkin, Renate Reiss, Nicholas J. Turner, Andrzej M. Brzozowski, Gideon Grogan

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	182-185
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	64
Issue number	3
DOIs	https://doi.org/10.1107/S174430910800345X
Publication status	Published - Mar 2008

Keywords

MOLECULAR REPLACEMENT
ENZYME
EVOLUTION
AMINES
ROUTE
MODE

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Atkin, K. E., Reiss, R., Turner, N. J., Brzozowski, A. M., & Grogan, G. (2008). Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(3), 182-185. https://doi.org/10.1107/S174430910800345X

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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.",

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author = "Atkin, {Kate E.} and Renate Reiss and Turner, {Nicholas J.} and Brzozowski, {Andrzej M.} and Gideon Grogan",

year = "2008",

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doi = "10.1107/S174430910800345X",

language = "English",

volume = "64",

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Atkin, KE, Reiss, R, Turner, NJ, Brzozowski, AM & Grogan, G 2008, 'Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 64, no. 3, pp. 182-185. https://doi.org/10.1107/S174430910800345X

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger. / Atkin, Kate E.; Reiss, Renate; Turner, Nicholas J. et al.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 64, No. 3, 03.2008, p. 182-185.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger

AU - Atkin, Kate E.

AU - Reiss, Renate

AU - Turner, Nicholas J.

AU - Brzozowski, Andrzej M.

AU - Grogan, Gideon

PY - 2008/3

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N2 - 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.

AB - 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.

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KW - ENZYME

KW - EVOLUTION

KW - AMINES

KW - ROUTE

KW - MODE

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M3 - Article

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JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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ER -

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

Abstract

Keywords

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