M00103
type: Enzyme
cath: Copper Amine Oxidase; Chain A, domain 1
cath: Nuclear Transport Factor 2; Chain
cath: Beta-galactosidase; Chain A, domain 5
ec: https://purl.uniprot.org/enzyme/1.4.3.21
csa: 1oac
uniprot: P46883
kegg enzyme: primary-amine oxidase
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Tyrosine metabolism
kegg pathway: Phenylalanine metabolism
kegg pathway: beta-Alanine metabolism
kegg pathway: Alkaloid biosynthesis II
kegg cofactor: Copper
kegg cofactor: Calcium
kegg cofactor: Topaquinone
kegg substrate: RCH2NH2
kegg substrate: H2O
kegg substrate: Oxygen
kegg product: Aldehyde
kegg product: NH3
kegg product: H2O2
kegg intermediate: Substrate Schiff-base (Iminoquinone=substrate)
kegg intermediate: Product Schiff-base (Aminoquinol=product)
kegg intermediate: Aminoquinol/Semiquinone
kegg intermediate: Iminoquinone
pdb: 1d6uA01
pdb: 1d6uB01
pdb: 1d6yA01
pdb: 1d6yB01
pdb: 1d6zA01
pdb: 1d6zB01
pdb: 1jrqA01
pdb: 1jrqB01
pdb: 1lvnA01
pdb: 1lvnB01
pdb: 1oacA01
pdb: 1oacB01
pdb: 1spuA01
pdb: 1spuB01
pdb: 1dyuA01
pdb: 1dyuB01
pdb: 1qafA01
pdb: 1qafB01
pdb: 1qakA01
pdb: 1qakB01
pdb: 1qalA01
pdb: 1qalB01
pdb: 1d6uA02
pdb: 1d6uB02
pdb: 1d6yA02
pdb: 1d6yB02
pdb: 1d6zA02
pdb: 1d6zB02
pdb: 1jrqA02
pdb: 1jrqB02
pdb: 1lvnA02
pdb: 1lvnB02
pdb: 1oacA02
pdb: 1oacB02
pdb: 1spuA02
pdb: 1spuB02
pdb: 1dyuA02
pdb: 1dyuB02
pdb: 1qafA02
pdb: 1qafB02
pdb: 1qakA02
pdb: 1qakB02
pdb: 1qalA02
pdb: 1qalB02
pdb: 1d6uA03
pdb: 1d6uB03
pdb: 1d6yA03
pdb: 1d6yB03
pdb: 1d6zA03
pdb: 1d6zB03
pdb: 1jrqA03
pdb: 1jrqB03
pdb: 1lvnA03
pdb: 1lvnB03

Copper Amine Oxidase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.457.10

Nuclear Transport Factor 2; Chain
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.10.450.40

Beta-galactosidase; Chain A, domain 5
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.70.98.20
catalytic domain: index.html

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260

Tyrosine metabolism
type: KeggPathway
references: KEGG:MAP00350

Phenylalanine metabolism
type: KeggPathway
references: KEGG:MAP00360

beta-Alanine metabolism
type: KeggPathway
references: KEGG:MAP00410

Alkaloid biosynthesis II
type: KeggPathway
references: KEGG:MAP00960

Copper
type: KeggCofactor
references: KEGG:C00070
compound type: heavy metal
references: CHEBI:28694
references: CHEBI:30052
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Calcium
type: KeggCofactor
references: KEGG:C00076
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:29108
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Topaquinone
type: KeggCofactor
references: KEGG:L00003
compound type: amino acids
compound type: aromatic ring (only carbon atom)
references: CHEBI:36077
references: CHEBI:68431

RCH2NH2
type: KeggSubstrate
references: KEGG:C00375
compound type: amine group

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Oxygen
type: KeggSubstrate
references: KEGG:C00007
compound type: others
references: CHEBI:15379
references: CHEBI:26689
references: CHEBI:27140
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Aldehyde
type: KeggProduct
references: KEGG:C00071
compound type: carbohydrate

NH3
type: KeggProduct
references: KEGG:C00014
compound type: amine group
compound type: organic ion
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H2O2
type: KeggProduct
references: KEGG:C00027
compound type: others
references: CHEBI:16240
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Substrate Schiff-base (Iminoquinone=substrate)
type: KeggIntermediate
references: KEGG:I00021

Product Schiff-base (Aminoquinol=product)
type: KeggIntermediate
references: KEGG:I00022

Aminoquinol/Semiquinone
type: KeggIntermediate
references: KEGG:I00023

Iminoquinone
type: KeggIntermediate
references: KEGG:I00024

1d6uA03
type: Pdb
references: 1d6u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d6u
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYQ 466(aminoquinol)

1d6uB03
type: Pdb
references: 1d6u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d6u
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYQ 466(aminoquinol)

1d6yA03
type: Pdb
references: 1d6y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d6y
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYQ 466(aminoquinol)

1d6yB03
type: Pdb
references: 1d6y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d6y
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYQ 466(aminoquinol)

1d6zA03
type: Pdb
references: 1d6z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d6z
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYY 466(iminoquinone)

1d6zB03
type: Pdb
references: 1d6z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d6z
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYY 466(iminoquinone)

1jrqA03
type: Pdb
references: 1jrq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jrq
catalytic residue: ;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant Y369F

1jrqB03
type: Pdb
references: 1jrq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jrq
catalytic residue: ;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant Y369F

1lvnA03
type: Pdb
references: 1lvn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lvn
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYT 466(iminoquinone-substrate analogue)

1lvnB03
type: Pdb
references: 1lvn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lvn
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYT 466(iminoquinone-substrate analogue)

1oacA03
type: Pdb
references: 1oac
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oac
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)

1oacB03
type: Pdb
references: 1oac
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oac
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)

1spuA03
type: Pdb
references: 1spu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1spu
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: PAQ 466(2-oxy-4-hydroxy-5-(2-hydrazinopyridine)phenylalanine)

1spuB03
type: Pdb
references: 1spu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1spu
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: PAQ 466(2-oxy-4-hydroxy-5-(2-hydrazinopyridine)phenylalanine)

1dyuA03
type: Pdb
references: 1dyu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dyu
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYR 466(topaquinone)

1dyuB03
type: Pdb
references: 1dyu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dyu
catalytic residue: TYR 369;ASP 383
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TYR 466(topaquinone)

1qafA03
type: Pdb
references: 1qaf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qaf
catalytic residue: TYR 369;
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant D383E

1qafB03
type: Pdb
references: 1qaf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qaf
catalytic residue: TYR 369;
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant D383E

1qakA03
type: Pdb
references: 1qak
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qak
catalytic residue: TYR 369;
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant D383A

1qakB03
type: Pdb
references: 1qak
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qak
catalytic residue: TYR 369;
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant D383A

1qalA03
type: Pdb
references: 1qal
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qal
catalytic residue: TYR 369;
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant D383N

1qalB03
type: Pdb
references: 1qal
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qal
catalytic residue: TYR 369;
cofactor binding residue: HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2)
modified residue: TPQ 466(topaquinone)
comment: mutant D383N

Analogue
compound: RCH2NH2
pdb: 1qafB03
ligand het code: GOL

Analogue
compound: Oxygen
pdb: 1d6yA03
ligand het code: _NO

Analogue
compound: Oxygen
pdb: 1d6yB03
ligand het code: _NO

Analogue
compound: Topaquinone
pdb: 1d6uA03
ligand het code: TYQ_466

Analogue
compound: Topaquinone
pdb: 1d6uB03
ligand het code: TYQ_466

Analogue
compound: Topaquinone
pdb: 1d6yA03
ligand het code: TYQ_466

Analogue
compound: Topaquinone
pdb: 1d6yB03
ligand het code: TYQ_466

Analogue
compound: Topaquinone
pdb: 1d6zA03
ligand het code: TYY_466

Analogue
compound: Topaquinone
pdb: 1d6zB03
ligand het code: TYY_466

Analogue
compound: Topaquinone
pdb: 1lvnA03
ligand het code: TYT_466

Analogue
compound: Topaquinone
pdb: 1lvnB03
ligand het code: TYT_466

Analogue
compound: Topaquinone
pdb: 1spuA03
ligand het code: PAQ_466

Analogue
compound: Topaquinone
pdb: 1spuB03
ligand het code: PAQ_466

IntermediateAnalogue
compound: Substrate Schiff-base (Iminoquinone=substrate)
pdb: 1lvnA03
ligand het code: TYT_466

IntermediateAnalogue
compound: Substrate Schiff-base (Iminoquinone=substrate)
pdb: 1lvnB03
ligand het code: TYT_466

IntermediateAnalogue
compound: Substrate Schiff-base (Iminoquinone=substrate)
pdb: 1spuA03
ligand het code: PAQ_466

IntermediateAnalogue
compound: Substrate Schiff-base (Iminoquinone=substrate)
pdb: 1spuB03
ligand het code: PAQ_466

IntermediateBound
compound: Aminoquinol/Semiquinone
pdb: 1d6uA03
ligand het code: TYQ_466

IntermediateBound
compound: Aminoquinol/Semiquinone
pdb: 1d6uB03
ligand het code: TYQ_466

IntermediateBound
compound: Aminoquinol/Semiquinone
pdb: 1d6yA03
ligand het code: TYQ_466

IntermediateBound
compound: Aminoquinol/Semiquinone
pdb: 1d6yB03
ligand het code: TYQ_466

IntermediateBound
compound: Iminoquinone
pdb: 1d6zA03
ligand het code: TYY_466

IntermediateBound
compound: Iminoquinone
pdb: 1d6zB03
ligand het code: TYY_466

ReferenceForCatalyticMechanism
reference index: 5
reference section: Scheme II, p.60-62

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig. 1, p.1128-1129

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.1, p.1178-1179

ReferenceForCatalyticMechanism
reference index: 9
reference section: Scheme 1, p.5586-5588

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.2, Fig.10, p.1617-1619

ReferenceForCatalyticMechanism
reference index: 11
reference section: Scheme 23, Scheme 24, p.746-747

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.1, p.8224-8226

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.2, p.1725-1728

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.2, p.12814-12817

ReferenceForCatalyticMechanism
reference index: 17
reference section: Scheme 1, Fig.1, p.4694-4605

ReferenceForCatalyticMechanism
reference index: 18
reference section: Scheme 1, p.814-815

ReferenceForCatalyticMechanism
reference index: 21
reference section: Fig.4, Fig.6, p.313-315

ReferenceForCatalyticMechanism
reference index: 22
reference section: Scheme 1, Fig.1, p.494-496

ReferenceForCatalyticMechanism
reference index: 23
reference section: Scheme 2

Models and molecular orbital semiempirical calculations in the study of the spectroscopic properties of bovine serum amine oxidase quinone cofactor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8155661
journal: Biochemistry
volume: 33
pages: 4425-31
published year: 1994
authors:
  item: Bossa M
  item: Morpurgo GO
  item: Morpurgo L

Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8176752
journal: J Mol Biol
volume: 238
pages: 635-7
published year: 1994
authors:
  item: Roh JH
  item: Suzuki H
  item: Kumagai H
  item: Yamashita M
  item: Azakami H
  item: Murooka Y
  item: Mikami B

Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8585612
journal: Anal Biochem
volume: 230
pages: 159-66
published year: 1995
authors:
  item: Steinebach V
  item: Groen BW
  item: Wijmenga SS
  item: Niessen WM
  item: Jongejan JA
  item: Duine JA

Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7766611
journal: Biochemistry
volume: 34
pages: 7020-6
published year: 1995
authors:
  item: Moenne-Loccoz P
  item: Nakamura N
  item: Steinebach V
  item: Duine JA
  item: Mure M
  item: Klinman JP
  item: Sanders-Loehr J

Catalytic aerobic deamination of activated primary amines by a model for the quinone cofactor of mammalian copper amine oxidases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8524164
journal: Methods Enzymol
volume: 258
pages: 53-69
published year: 1995
authors:
  item: Sayre LM
  item: Lee Y

Copper amine oxidase: a novel use for a tyrosine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8591022
journal: Structure
volume: 3
pages: 1127-9
published year: 1995
authors:
  item: Fontecave M
  item: Eklund H

Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8591028
journal: Structure
volume: 3
pages: 1171-84
published year: 1995
authors:
  item: Parsons MR
  item: Convery MA
  item: Wilmot CM
  item: Yadav KD
  item: Blakeley V
  item: Corner AS
  item: Phillips SE
  item: McPherson MJ
  item: Knowles PF
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The copper-topaquinone-phenylhydrazine-adduct geometry in Escherichia coli amine oxidase derivatized with phenylhydrazines substituted with 19F-NMR relaxation measurements.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8706668
journal: Eur J Biochem
volume: 238
pages: 683-9
published year: 1996
authors:
  item: Steinebach V
  item: De Jong GA
  item: Wijmenga SS
  item: De Vries S
  item: Duine JA

Intermediates in the catalytic cycle of copper-quinoprotein amine oxidase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8621418
journal: J Biol Chem
volume: 271
pages: 5580-8
published year: 1996
authors:
  item: Steinebach V
  item: de Vries S
  item: Duine JA

Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
medline id: 97200715
references: http://www.ncbi.nlm.nih.gov/pubmed/9048544
journal: Biochemistry
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The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
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comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
medline id: 99315198
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Visualization of dioxygen bound to copper during enzyme catalysis.
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comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
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references: http://www.ncbi.nlm.nih.gov/pubmed/10576737
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Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase.
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Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
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Copper amine oxidase: cunning cofactor and controversial copper.
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pages: 666-73
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Irreversible inhibition of pig kidney copper-containing amine oxidase by sodium and lithium ions.
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journal: Eur J Biochem
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pages: 4686-97
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Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.
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journal: Biochem J
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pages: 809-16
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Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases.
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Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases.
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Defining redox state of X-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry.
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Oxygen activation in a copper-containing amine oxidase.
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Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective.
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Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
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Exploring the binding mode of semicarbazide-sensitive amine oxidase/VAP-1: identification of novel substrates with insulin-like activity.
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pages: 4865-74
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amine oxidase (ambiguous)
type: KeggEnzyme

amine oxidase (copper-containing)
type: KeggEnzyme

amine oxidase (pyridoxal containing) (incorrect)
type: KeggEnzyme

benzylamine oxidase (incorrect)
type: KeggEnzyme

CAO (ambiguous)
type: KeggEnzyme

copper amine oxidase (ambiguous)
type: KeggEnzyme

Cu-amine oxidase (ambiguous)
type: KeggEnzyme

Cu-containing amine oxidase (ambiguous)
type: KeggEnzyme

diamine oxidase (incorrect)
type: KeggEnzyme

diamino oxhydrase (incorrect)
type: KeggEnzyme

histamine deaminase (ambiguous)
type: KeggEnzyme

histamine oxidase (ambiguous)
type: KeggEnzyme

monoamine oxidase (ambiguous)
type: KeggEnzyme

plasma monoamine oxidase (ambiguous)
type: KeggEnzyme

polyamine oxidase (ambiguous)
type: KeggEnzyme

semicarbazide-sensitive amine oxidase (ambiguous)
type: KeggEnzyme

SSAO (ambiguous)
type: KeggEnzyme