Literature summary extracted from

Atkin, K.E.; Reiss, R.; Koehler, V.; Bailey, K.R.; Hart, S.; Turkenburg, J.P.; Turner, N.J.; Brzozowski, A.M.; Grogan, G.
The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution (2008), J. Mol. Biol., 384, 1218-1231.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.4.3.21	expression of wild-type and mutant enzymes, expression of selenomethionine-labeled truncated mutant MAO-N-D5 in Escherichia coli strain B834(DE3)	Aspergillus niger

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.4.3.21	purified recombinant mutants MAO-N-D3 and MAO-N-D5, and truncated selenomethionine-labeled mutant MAO-N-D5, X-ray diffraction structure determination and analysis, multiple-wavelength anomalous diffraction and molecular replacement	Aspergillus niger

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.4.3.21	N336S/M348K/I246M	gain-of-function mutant MAO-N-D3, structure analysis, overview. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site	Aspergillus niger
1.4.3.21	N336S/M348K/I246M/T384N/D385S	gain-of-function mutant MAO-N-D5 is able to oxidise tertiary amines, structure analysis, overview. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site. The two additional mutations, Thr384Asn and Asp385Ser, appear to influence the active-site environment remotely through changes in tertiary structure that perturb the side chain of Phe382, again altering the steric and electronic character of the active site near FAD	Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.4.3.21	additional information	Aspergillus niger	MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.4.3.21	Aspergillus niger	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.4.3.21	flavoprotein	-	Aspergillus niger

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.4.3.21	recombinant selenomethionine-labeled truncated mutant MAO-N-D5 from Escherichia coli strain B834(DE3) by nickel affinity chromatography	Aspergillus niger

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.4.3.21	additional information	MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview	Aspergillus niger	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.4.3.21	homotetramer	MAO-N exists as a homotetramer with a large channel at its centre	Aspergillus niger

Synonyms

EC Number	Synonyms	Comment	Organism
1.4.3.21	MAO-N	-	Aspergillus niger

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.4.3.21	FAD	flavoenzyme, a hydrophobic cavity extends from the protein surface to the active site, where a noncovalently bound FAD sits at the base of an aromatic cage, the sides of which are formed by Trp430 and Phe466, binding structure, overview	Aspergillus niger

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Release 2023.1 (January 2023)