T00216
type: Enzyme
cath: Immunoglobulin-like
ec: https://purl.uniprot.org/enzyme/1.10.3.3
uniprot: P37064
kegg enzyme: L-ascorbate oxidase
kegg enzyme: ascorbase
kegg enzyme: ascorbic acid oxidase
kegg enzyme: ascorbate oxidase
kegg enzyme: ascorbic oxidase
kegg enzyme: ascorbate dehydrogenase
kegg enzyme: L-ascorbic acid oxidase
kegg enzyme: AAO
kegg enzyme: L-ascorbate:O2 oxidoreductase
kegg enzyme: AA oxidase
kegg pathway: Ascorbate and aldarate metabolism
kegg cofactor: Copper
kegg substrate: L-Ascorbate
kegg substrate: O2
kegg product: Dehydroascorbate
kegg product: H2O
pdb: 1aozA01
pdb: 1aozB01
pdb: 1asoA01
pdb: 1asoB01
pdb: 1aspA01
pdb: 1aspB01
pdb: 1asqA01
pdb: 1asqB01
pdb: 1aozA02
pdb: 1aozB02
pdb: 1asoA02
pdb: 1asoB02
pdb: 1aspA02
pdb: 1aspB02
pdb: 1asqA02
pdb: 1asqB02
pdb: 1aozA03
pdb: 1aozB03
pdb: 1asoA03
pdb: 1asoB03
pdb: 1aspA03
pdb: 1aspB03
pdb: 1asqA03
pdb: 1asqB03
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aozA01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aozB01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1asoA01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1asoB01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aspA01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aspB01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1asqA01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1asqB01
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aozA02
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aozB02
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1asoA02
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1asoB02
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aspA02
pdb bound state: Unbound
  compound: L-Ascorbate
  pdb: 1aspB02
active site residues resources: X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.
active site residues resources: EPR spectra of type 3 copper centers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase.
references: Preliminary crystallographic study of ascorbic acid oxidase from green zucchini squash.
references: A new crystalline modification of the copper enzyme ascorbate oxidase.
references: Preliminary X-ray crystal structure and partial cDNA-sequence of ascorbate oxidase from zucchini.
references: X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.
references: The role of copper in the stability of ascorbate oxidase towards denaturing agents.
references: X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini.
references: Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
references: X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.
references: EPR spectra of type 3 copper centers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase.
references: Inhibition of ascorbate oxidase by phenolic compounds. Enzymatic and spectroscopic studies.
references: Role of quaternary structure in the stability of dimeric proteins: the case of ascorbate oxidase.
references: The type 2 copper of ascorbate oxidase.
references: Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements.
references: The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase.
references: Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time.
references: Azide binding to the trinuclear copper center in laccase and ascorbate oxidase.
references: Protein packing: dependence on protein size, secondary structure and amino acid composition.
references: Upward shift of the pH optimum of Acremonium ascorbate oxidase.
references: Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies.
comment: Coppers can be classified into three types (see literature [7], [8] & laccase;T00215 in EzCatDB): Type I copper (blue copper); Copper-1 in this enzyme Type II copper (non-blue copper); Copper-2 Type III copper (EPR-non-detectable copper); Copper-3a & copper-3b in this enzyme. The copper-2, -3a and -3b form a trinuclear copper site, to which an oxygen is bound, whereas the cooper-1 is a monocuclear copper site, to which an organic substrate is bound (see laccase;T00215). This enzyme catalyzes the following reactions: (A) Oxidation (dehydrogenation) of organic substrate at mononuclear coper site: (B) Electron transfer from mononuclear copper site to trinuclear copper site: (C) O2 reduction to produce H2O at trinuclear copper site:

Immunoglobulin-like
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.40.420
catalytic domain: index.html

Ascorbate and aldarate metabolism
type: KeggPathway
references: KEGG:MAP00053

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

L-Ascorbate
type: KeggSubstrate
references: KEGG:C00072
compound type: carbohydrate
compound type: aromatic ring (with hetero atoms other than nitrogen atoms)
references: CHEBI:29073
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

O2
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

Dehydroascorbate
type: KeggProduct
references: KEGG:C05422
compound type: carbohydrate
references: CHEBI:27956
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

1aozA01
type: Pdb
references: 1aoz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aoz
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1aozB01
type: Pdb
references: 1aoz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aoz
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1asoA01
type: Pdb
references: 1aso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aso
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1asoB01
type: Pdb
references: 1aso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aso
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1aspA01
type: Pdb
references: 1asp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asp
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1aspB01
type: Pdb
references: 1asp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asp
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1asqA01
type: Pdb
references: 1asq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asq
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1asqB01
type: Pdb
references: 1asq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asq
cofactor binding residue: HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)

1aozA03
type: Pdb
references: 1aoz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aoz
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1aozB03
type: Pdb
references: 1aoz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aoz
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1asoA03
type: Pdb
references: 1aso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aso
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1asoB03
type: Pdb
references: 1aso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aso
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1aspA03
type: Pdb
references: 1asp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asp
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1aspB03
type: Pdb
references: 1asp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asp
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1asqA03
type: Pdb
references: 1asq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asq
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

1asqB03
type: Pdb
references: 1asq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asq
catalytic residue: HIS 506;CYS 507;HIS 508
cofactor binding residue: HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)

Preliminary crystallographic study of ascorbic acid oxidase from green zucchini squash.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/510553
journal: FEBS Lett
volume: 107
pages: 407-8
published year: 1979
authors:
  item: Ladenstein R
  item: Marchesini A
  item: Palmieri S

A new crystalline modification of the copper enzyme ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6620382
journal: J Mol Biol
volume: 169
pages: 351-2
published year: 1983
authors:
  item: Bolognesi M
  item: Gatti G
  item: Coda A
  item: Avigliano L
  item: Marcozzi G
  item: Finazzi-Agro A

Preliminary X-ray crystal structure and partial cDNA-sequence of ascorbate oxidase from zucchini.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3406029
journal: Prog Clin Biol Res
volume: 274
pages: 285-8
published year: 1988
authors:
  item: Messerschmidt A
  item: Rossi A
  item: Ladenstein R
  item: Huber R
  item: Bolognesi M
  item: Marchesini A
  item: Petruzelli R
  item: Finazzi-Agro A

X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
medline id: 89236417
references: http://www.ncbi.nlm.nih.gov/pubmed/2716059
journal: J Mol Biol
volume: 206
pages: 513-29
published year: 1989
authors:
  item: Messerschmidt A
  item: Rossi A
  item: Ladenstein R
  item: Huber R
  item: Bolognesi M
  item: Gatti G
  item: Marchesini A
  item: Petruzzelli R
  item: Finazzi-Agro A
references: P37064

The role of copper in the stability of ascorbate oxidase towards denaturing agents.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2373076
journal: Eur J Biochem
volume: 190
pages: 491-5
published year: 1990
authors:
  item: Savini I
  item: D'Alessio S
  item: Giartosio A
  item: Morpurgo L
  item: Avigliano L

X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1330552
journal: Eur J Biochem
volume: 209
pages: 597-602
published year: 1992
authors:
  item: Messerschmidt A
  item: Steigemann W
  item: Huber R
  item: Lang G
  item: Kroneck PM

Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
medline id: 92194315
references: http://www.ncbi.nlm.nih.gov/pubmed/1548698
journal: J Mol Biol
volume: 224
pages: 179-205
published year: 1992
authors:
  item: Messerschmidt A
  item: Ladenstein R
  item: Huber R
  item: Bolognesi M
  item: Avigliano L
  item: Petruzzelli R
  item: Rossi A
  item: Finazzi-Agro A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P37064

X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8478945
journal: J Mol Biol
volume: 230
pages: 997-1014
published year: 1993
authors:
  item: Messerschmidt A
  item: Luecke H
  item: Huber R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

EPR spectra of type 3 copper centers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7748896
journal: Biochim Biophys Acta
volume: 1248
pages: 143-8
published year: 1995
authors:
  item: Sakurai T
  item: Takahashi J

Inhibition of ascorbate oxidase by phenolic compounds. Enzymatic and spectroscopic studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9125505
journal: Biochemistry
volume: 36
pages: 4852-9
published year: 1997
authors:
  item: Gaspard S
  item: Monzani E
  item: Casella L
  item: Gullotti M
  item: Maritano S
  item: Marchesini A

Role of quaternary structure in the stability of dimeric proteins: the case of ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9283082
journal: Biochemistry
volume: 36
pages: 10917-22
published year: 1997
authors:
  item: Mei G
  item: Di Venere A
  item: Buganza M
  item: Vecchini P
  item: Rosato N
  item: Finazzi-Agro' A

The type 2 copper of ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9048895
journal: Biochim Biophys Acta
volume: 1337
pages: 191-7
published year: 1997
authors:
  item: Reinhammar B
  item: Aasa R
  item: Vanngard T
  item: Maritano S
  item: Marchesini A

Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9602107
journal: Biochim Biophys Acta
volume: 1384
pages: 160-70
published year: 1998
authors:
  item: Huang HW
  item: Sakurai T
  item: Monjushiro H
  item: Takeda S

The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9781686
journal: FEBS Lett
volume: 436
pages: 239-42
published year: 1998
authors:
  item: Farver O
  item: Eady RR
  item: Abraham ZH
  item: Pecht I

Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10813026
journal: Appl Biochem Biotechnol
volume: 82
pages: 227-41
published year: 1999
authors:
  item: Savini I
  item: Santucci R
  item: Di Venere A
  item: Rosato N
  item: Strukul G
  item: Pinna F
  item: Avigliano L

Azide binding to the trinuclear copper center in laccase and ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10583375
journal: Eur J Biochem
volume: 266
pages: 820-30
published year: 1999
authors:
  item: Gromov I
  item: Marchesini A
  item: Farver O
  item: Pecht I
  item: Goldfarb D

Protein packing: dependence on protein size, secondary structure and amino acid composition.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10860754
journal: J Mol Biol
volume: 299
pages: 487-98
published year: 2000
authors:
  item: Fleming PJ
  item: Richards FM

Upward shift of the pH optimum of Acremonium ascorbate oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11983419
journal: Biochim Biophys Acta
volume: 1596
pages: 36-46
published year: 2002
authors:
  item: Sugino M
  item: Kajita S
  item: Banno K
  item: Shirai T
  item: Yamane T
  item: Kato M
  item: Kobayashi T
  item: Tsukagoshi N

Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15006640
journal: Int J Biochem Cell Biol
volume: 36
pages: 881-92
published year: 2004
authors:
  item: Santagostini L
  item: Gullotti M
  item: De Gioia L
  item: Fantucci P
  item: Franzini E
  item: Marchesini A
  item: Monzani E
  item: Casella L

Analogue
compound: Copper
pdb: 1aozA01
ligand het code: C2O

Analogue
compound: Copper
pdb: 1aozB01
ligand het code: C2O

Analogue
pdb: 1asqA03
ligand het code: AZI_2

Analogue
pdb: 1asqB03
ligand het code: AZI_2

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.19, p.199-203

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.13, p.1012-1013