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Literature summary for 1.4.3.21 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
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)

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
Aspergillus niger

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
MAO-N
-
Aspergillus niger

Cofactor

Cofactor Comment Organism Structure
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