Structure and activity of Aspergillus nidulans copper amine oxidase

Aaron P McGrath; Suzanne M Mithieux; Charles A Collyer; Janny G Bakhuis; Marco van den Berg; Arjen Sein; Andrea Heinz; Christian Schmelzer; Anthony S Weiss; J Mitchell Guss

doi:10.1021/bi200555c

Structure and activity of Aspergillus nidulans copper amine oxidase

Aaron P McGrath, Suzanne M Mithieux, Charles A Collyer, Janny G Bakhuis, Marco van den Berg, Arjen Sein, Andrea Heinz, Christian Schmelzer, Anthony S Weiss, J Mitchell Guss

21 Citations (Scopus)

Abstract

Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 Å. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.

Original language	English
Journal	Biochemistry
Volume	50
Issue number	25
Pages (from-to)	5718-30
Number of pages	13
ISSN	0006-2960
DOIs	https://doi.org/10.1021/bi200555c
Publication status	Published - 28 Jun 2011

Keywords

Amine Oxidase (Copper-Containing)
Amino Acid Sequence
Aspergillus nidulans
Catalytic Domain
Crystallography, X-Ray
Dimerization
Fungal Proteins
Glycosylation
Humans
Mixed Function Oxygenases
Molecular Sequence Data
Protein Folding
Protein Multimerization
Substrate Specificity
Tropoelastin
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

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title = "Structure and activity of Aspergillus nidulans copper amine oxidase",

abstract = "Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 {\AA}. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.",

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author = "McGrath, {Aaron P} and Mithieux, {Suzanne M} and Collyer, {Charles A} and Bakhuis, {Janny G} and {van den Berg}, Marco and Arjen Sein and Andrea Heinz and Christian Schmelzer and Weiss, {Anthony S} and Guss, {J Mitchell}",

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T1 - Structure and activity of Aspergillus nidulans copper amine oxidase

AU - McGrath, Aaron P

AU - Mithieux, Suzanne M

AU - Collyer, Charles A

AU - Bakhuis, Janny G

AU - van den Berg, Marco

AU - Sein, Arjen

AU - Heinz, Andrea

AU - Schmelzer, Christian

AU - Weiss, Anthony S

AU - Guss, J Mitchell

PY - 2011/6/28

Y1 - 2011/6/28

N2 - Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 Å. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.

AB - Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 Å. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.

KW - Amine Oxidase (Copper-Containing)

KW - Amino Acid Sequence

KW - Aspergillus nidulans

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - Dimerization

KW - Fungal Proteins

KW - Glycosylation

KW - Humans

KW - Mixed Function Oxygenases

KW - Molecular Sequence Data

KW - Protein Folding

KW - Protein Multimerization

KW - Substrate Specificity

KW - Tropoelastin

KW - Comparative Study

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1021/bi200555c

DO - 10.1021/bi200555c

M3 - Journal article

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SN - 0006-2960

VL - 50

SP - 5718

EP - 5730

JO - Biochemistry

JF - Biochemistry

IS - 25

ER -

Structure and activity of Aspergillus nidulans copper amine oxidase

Abstract

Keywords

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