Structure and activity of Aspergillus nidulans copper amine oxidase

Research output: Contribution to journal › Journal article › Research › peer-review

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Structure and activity of Aspergillus nidulans copper amine oxidase. / McGrath, Aaron P; Mithieux, Suzanne M; Collyer, Charles A; Bakhuis, Janny G; van den Berg, Marco; Sein, Arjen; Heinz, Andrea; Schmelzer, Christian; Weiss, Anthony S; Guss, J Mitchell.

In: Biochemistry, Vol. 50, No. 25, 28.06.2011, p. 5718-30.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

McGrath, AP, Mithieux, SM, Collyer, CA, Bakhuis, JG, van den Berg, M, Sein, A, Heinz, A, Schmelzer, C, Weiss, AS & Guss, JM 2011, 'Structure and activity of Aspergillus nidulans copper amine oxidase', Biochemistry, vol. 50, no. 25, pp. 5718-30. https://doi.org/10.1021/bi200555c

APA

McGrath, A. P., Mithieux, S. M., Collyer, C. A., Bakhuis, J. G., van den Berg, M., Sein, A., Heinz, A., Schmelzer, C., Weiss, A. S., & Guss, J. M. (2011). Structure and activity of Aspergillus nidulans copper amine oxidase. Biochemistry, 50(25), 5718-30. https://doi.org/10.1021/bi200555c

Vancouver

McGrath AP, Mithieux SM, Collyer CA, Bakhuis JG, van den Berg M, Sein A et al. Structure and activity of Aspergillus nidulans copper amine oxidase. Biochemistry. 2011 Jun 28;50(25):5718-30. https://doi.org/10.1021/bi200555c

Author

McGrath, Aaron P ; Mithieux, Suzanne M ; Collyer, Charles A ; Bakhuis, Janny G ; van den Berg, Marco ; Sein, Arjen ; Heinz, Andrea ; Schmelzer, Christian ; Weiss, Anthony S ; Guss, J Mitchell. / Structure and activity of Aspergillus nidulans copper amine oxidase. In: Biochemistry. 2011 ; Vol. 50, No. 25. pp. 5718-30.

Bibtex

@article{9c4b75e34d6e419ab6494fac0b389c71,
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.",
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",
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}",
year = "2011",
month = jun,
day = "28",
doi = "10.1021/bi200555c",
language = "English",
volume = "50",
pages = "5718--30",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "25",

}

RIS

TY - JOUR

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

C2 - 21604787

VL - 50

SP - 5718

EP - 5730

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 25

ER -

ID: 186422319