S00925
type: Enzyme
cath: di-copper center containing domain from catechol oxidase
ec: https://purl.uniprot.org/enzyme/1.14.18.1
uniprot: B2ZB02
uniprot: Q83WS2
kegg enzyme: Tyrosinase
kegg pathway: Tyrosine metabolism
kegg pathway: Riboflavin metabolism
kegg pathway: Isoquinoline alkaloid biosynthesis
kegg pathway: Betalain biosynthesis
kegg pathway: Biosynthesis of secondary metabolites
kegg cofactor: Copper
kegg substrate: L-tyrosine
kegg substrate: O2
kegg substrate: L-dopa
kegg product: L-dopa
kegg product: dopaquinone
kegg product: H2O
pdb: 3nm8A
pdb: 3nm8B
pdb: 3npyA
pdb: 3npyB
pdb: 3nq0A
pdb: 3nq0B
pdb: 3nq1A
pdb: 3nq1B
pdb: 3nq5A
pdb: 3nq5B
pdb: 3ntmA
pdb: 3ntmB
pdb: 4d87A
pdb: 4d87B
pdb: 4hd4A
pdb: 4hd4B
pdb: 4hd6A
pdb: 4hd6B
pdb: 4hd7A
pdb: 4hd7B
pdb: 1wx2A
pdb: 1wx4A
pdb: 1wx5A
pdb: 1wx5C
pdb: 1wxcA
pdb: 2ahkA
pdb: 2ahlA
pdb: 2zmxA
pdb: 2zmyA
pdb: 2zmzA
pdb: 2zwdA
pdb: 2zweA
pdb: 2zwfA
pdb: 2zwgA
pdb: 3awsA
pdb: 3awtA
pdb: 3awuA
pdb: 3awvA
pdb: 3awwA
pdb: 3awxA
pdb: 3awyA
pdb: 3awzA
pdb: 3ax0A
active site residues resources: The first crystal structure of tyrosinase: all questions answered?
active site residues resources: Investigation of Streptomyces antibioticus tyrosinase reactivity toward chlorophenols.
active site residues resources: Changes in tyrosinase specificity by ionic liquids and sodium dodecyl sulfate.
references: Protein and active-site structure of tyrosinase.
references: Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase.
references: Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution.
references: Tyrosinase: a comprehensive review of its mechanism.
references: Roles of copper ligands in the activation and secretion of Streptomyces tyrosinase.
references: 1H NMR spectroscopy of the binuclear Cu(II) active site of Streptomyces antibioticus tyrosinase.
references: EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus.
references: Tyrosinase-catalyzed oxidation of fluorophenols.
references: Structural basis and mechanism of the inhibition of the type-3 copper protein tyrosinase from Streptomyces antibioticus by halide ions.
references: Molecular anatomy of tyrosinase and its related proteins: beyond the histidine-bound metal catalytic center.
references: Spectroscopic characterization of the electronic changes in the active site of Streptomyces antibioticus tyrosinase upon binding of transition state analogue inhibitors.
references: Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
references: Paramagnetic properties of the halide-bound derivatives of oxidised tyrosinase investigated by 1H NMR spectroscopy.
references: Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.
references: The first crystal structure of tyrosinase: all questions answered?
references: A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio.

di-copper center containing domain from catechol oxidase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.1280.10
catalytic domain: index.html

Tyrosine metabolism
type: KeggPathway
references: KEGG:MAP00350

Riboflavin metabolism
type: KeggPathway
references: KEGG:MAP00740

Isoquinoline alkaloid biosynthesis
type: KeggPathway
references: KEGG:MAP00950

Betalain biosynthesis
type: KeggPathway
references: KEGG:MAP00965

Biosynthesis of secondary metabolites
type: KeggPathway
references: KEGG:MAP01110

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-tyrosine
type: KeggSubstrate
references: KEGG:C00082
compound type: amino acids
compound type: aromatic ring (only carbon atom)
references: CHEBI:17895
references: CHEBI:58315
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

L-dopa
type: KeggSubstrate
references: KEGG:C00355
compound type: amino acids
compound type: aromatic ring (only carbon atom)
references: CHEBI:15765
references: CHEBI:57504
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
type: KeggProduct

dopaquinone
type: KeggProduct
references: KEGG:C00822
compound type: amino acids
compound type: aromatic ring (only carbon atom)
references: CHEBI:16852
references: CHEBI:57924
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

3nm8A
type: Pdb
references: 3nm8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nm8
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form?

3nm8B
type: Pdb
references: 3nm8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nm8
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form?

3npyA
type: Pdb
references: 3npy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3npy
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form

3npyB
type: Pdb
references: 3npy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3npy
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form

3nq0A
type: Pdb
references: 3nq0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nq0
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)

3nq0B
type: Pdb
references: 3nq0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nq0
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)

3nq1A
type: Pdb
references: 3nq1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nq1
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form

3nq1B
type: Pdb
references: 3nq1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nq1
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form

3nq5A
type: Pdb
references: 3nq5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nq5
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant R209H, Deoxy reduced form

3nq5B
type: Pdb
references: 3nq5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nq5
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant R209H, Deoxy reduced form

3ntmA
type: Pdb
references: 3ntm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ntm
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: Met I form

3ntmB
type: Pdb
references: 3ntm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ntm
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)

4d87A
type: Pdb
references: 4d87
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4d87
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)

4d87B
type: Pdb
references: 4d87
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4d87
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)

4hd4A
type: Pdb
references: 4hd4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4hd4
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant V218F

4hd4B
type: Pdb
references: 4hd4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4hd4
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant V218F

4hd6A
type: Pdb
references: 4hd6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4hd6
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant V218F, Met I form?

4hd6B
type: Pdb
references: 4hd6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4hd6
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant V218F, Met I form

4hd7A
type: Pdb
references: 4hd7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4hd7
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant V218G, Met I form

4hd7B
type: Pdb
references: 4hd7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4hd7
cofactor binding residue: HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
comment: mutant V218G, Met I form?

1wx2A
type: Pdb
references: 1wx2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wx2
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Oxy oxidized form

1wx4A
type: Pdb
references: 1wx4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wx4
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Oxy oxidized form

1wx5A
type: Pdb
references: 1wx5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wx5
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)

1wx5C
type: Pdb
references: 1wx5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wx5
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)

1wxcA
type: Pdb
references: 1wxc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wxc
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)

2ahkA
type: Pdb
references: 2ahk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ahk
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form

2ahlA
type: Pdb
references: 2ahl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ahl
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Deoxy reduced form

2zmxA
type: Pdb
references: 2zmx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zmx
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met I form

2zmyA
type: Pdb
references: 2zmy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zmy
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form

2zmzA
type: Pdb
references: 2zmz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zmz
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Deoxy reduced form

2zwdA
type: Pdb
references: 2zwd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zwd
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Deoxy reduced form?

2zweA
type: Pdb
references: 2zwe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zwe
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met I form

2zwfA
type: Pdb
references: 2zwf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zwf
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met I form

2zwgA
type: Pdb
references: 2zwg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zwg
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form

3awsA
type: Pdb
references: 3aws
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3aws
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)

3awtA
type: Pdb
references: 3awt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3awt
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met I form

3awuA
type: Pdb
references: 3awu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3awu
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met I form

3awvA
type: Pdb
references: 3awv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3awv
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form

3awwA
type: Pdb
references: 3aww
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3aww
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form?

3awxA
type: Pdb
references: 3awx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3awx
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form?

3awyA
type: Pdb
references: 3awy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3awy
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met II form?

3awzA
type: Pdb
references: 3awz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3awz
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)

3ax0A
type: Pdb
references: 3ax0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ax0
cofactor binding residue: HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
comment: Met I form

Protein and active-site structure of tyrosinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3130643
journal: Prog Clin Biol Res
volume: 256
pages: 85-98
published year: 1988
authors:
  item: Lerch K

Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2846043
journal: Biochemistry
volume: 27
pages: 5610-5
published year: 1988
authors:
  item: Huber M
  item: Lerch K

Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1348173
journal: Biochem J
volume: 282
pages: 915-8
published year: 1992
authors:
  item: Jackman MP
  item: Huber M
  item: Hajnal A
  item: Lerch K

Tyrosinase: a comprehensive review of its mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7873577
journal: Biochim Biophys Acta
volume: 1247
pages: 1-11
published year: 1995
authors:
  item: Sanchez-Ferrer A
  item: Rodriguez-Lopez JN
  item: Garcia-Canovas F
  item: Garcia-Carmona F

Roles of copper ligands in the activation and secretion of Streptomyces tyrosinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9668113
journal: J Biol Chem
volume: 273
pages: 19243-50
published year: 1998
authors:
  item: Tsai TY
  item: Lee YH

1H NMR spectroscopy of the binuclear Cu(II) active site of Streptomyces antibioticus tyrosinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9929004
journal: FEBS Lett
volume: 442
pages: 215-20
published year: 1999
authors:
  item: Bubacco L
  item: Salgado J
  item: Tepper AW
  item: Vijgenboom E
  item: Canters GW

EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10838090
journal: FEBS Lett
volume: 474
pages: 228-32
published year: 2000
authors:
  item: van Gastel M
  item: Bubacco L
  item: Groenen EJ
  item: Vijgenboom E
  item: Canters GW

Tyrosinase-catalyzed oxidation of fluorophenols.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12235154
journal: J Biol Chem
volume: 277
pages: 44606-12
published year: 2002
authors:
  item: Battaini G
  item: Monzani E
  item: Casella L
  item: Lonardi E
  item: Tepper AW
  item: Canters GW
  item: Bubacco L

Structural basis and mechanism of the inhibition of the type-3 copper protein tyrosinase from Streptomyces antibioticus by halide ions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12048185
journal: J Biol Chem
volume: 277
pages: 30436-44
published year: 2002
authors:
  item: Tepper AW
  item: Bubacco L
  item: Canters GW

Molecular anatomy of tyrosinase and its related proteins: beyond the histidine-bound metal catalytic center.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12028580
journal: Pigment Cell Res
volume: 15
pages: 162-73
published year: 2002
authors:
  item: Garcia-Borron JC
  item: Solano F

Spectroscopic characterization of the electronic changes in the active site of Streptomyces antibioticus tyrosinase upon binding of transition state analogue inhibitors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12473668
journal: J Biol Chem
volume: 278
pages: 7381-9
published year: 2003
authors:
  item: Bubacco L
  item: Van Gastel M
  item: Groenen EJ
  item: Vijgenboom E
  item: Canters GW

Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15643881
journal: J Am Chem Soc
volume: 127
pages: 567-75
published year: 2005
authors:
  item: Tepper AW
  item: Bubacco L
  item: Canters GW

Paramagnetic properties of the halide-bound derivatives of oxidised tyrosinase investigated by 1H NMR spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16927257
journal: Chemistry
volume: 12
pages: 7668-75
published year: 2006
authors:
  item: Tepper AW
  item: Bubacco L
  item: Canters GW

Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH COPPER.
references: http://www.ncbi.nlm.nih.gov/pubmed/16436386
journal: J Biol Chem
volume: 281
pages: 8981-90
published year: 2006
authors:
  item: Matoba Y
  item: Kumagai T
  item: Yamamoto A
  item: Yoshitsu H
  item: Sugiyama M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q83WS2

The first crystal structure of tyrosinase: all questions answered?
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16795103
journal: Angew Chem Int Ed Engl
volume: 45
pages: 4546-50
published year: 2006
authors:
  item: Decker H
  item: Schweikardt T
  item: Tuczek F

A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16403014
journal: FEBS J
volume: 273
pages: 257-70
published year: 2006
authors:
  item: Hernandez-Romero D
  item: Sanchez-Amat A
  item: Solano F

X-ray absorption analysis of the active site of Streptomyces antibioticus Tyrosinase upon binding of transition state analogue inhibitors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/17698026
journal: Arch Biochem Biophys
volume: 465
pages: 320-7
published year: 2007
authors:
  item: Bubacco L
  item: Spinazze R
  item: della Longa S
  item: Benfatto M

Modeling tyrosinase activity. Effect of ligand topology on aromatic ring hydroxylation: an overview.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18336914
journal: J Inorg Biochem
volume: 102
pages: 1170-89
published year: 2008
authors:
  item: De A
  item: Mandal S
  item: Mukherjee R

Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium.
type: BibliographicResource
comment: NUCLEOTIDE SEQUENCE.
references: http://www.ncbi.nlm.nih.gov/pubmed/19672047
journal: J Mol Microbiol Biotechnol
volume: 17
pages: 188-200
published year: 2009
authors:
  item: Shuster V
  item: Fishman A
references: B2ZB02

New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19735457
journal: Pigment Cell Melanoma Res
volume: 22
pages: 750-60
published year: 2009
authors:
  item: Olivares C
  item: Solano F

Crystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/20823537
journal: Acta Crystallogr Sect F Struct Biol Cryst Commun
volume: 66
pages: 1101-3
published year: 2010
authors:
  item: Sendovski M
  item: Kanteev M
  item: Shuster Ben-Yosef V
  item: Adir N
  item: Fishman A

Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19690900
journal: J Biol Inorg Chem
volume: 15
pages: 117-29
published year: 2010
authors:
  item: Deeth RJ
  item: Diedrich C

Investigation of Streptomyces antibioticus tyrosinase reactivity toward chlorophenols.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/20875779
journal: Arch Biochem Biophys
volume: 505
pages: 67-74
published year: 2011
authors:
  item: Marino SM
  item: Fogal S
  item: Bisaglia M
  item: Moro S
  item: Scartabelli G
  item: De Gioia L
  item: Spada A
  item: Monzani E
  item: Casella L
  item: Mammi S
  item: Bubacco L

A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/21730070
journal: J Biol Chem
volume: 286
pages: 30219-31
published year: 2011
authors:
  item: Matoba Y
  item: Bando N
  item: Oda K
  item: Noda M
  item: Higashikawa F
  item: Kumagai T
  item: Sugiyama M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

First structures of an active bacterial tyrosinase reveal copper plasticity.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC.
references: http://www.ncbi.nlm.nih.gov/pubmed/21040728
journal: J Mol Biol
volume: 405
pages: 227-37
published year: 2011
authors:
  item: Sendovski M
  item: Kanteev M
  item: Ben-Yosef VS
  item: Adir N
  item: Fishman A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: B2ZB02

Changes in tyrosinase specificity by ionic liquids and sodium dodecyl sulfate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/22539021
journal: Appl Microbiol Biotechnol
volume: 97
pages: 1953-61
published year: 2013
authors:
  item: Goldfeder M
  item: Egozy M
  item: Shuster Ben-Yosef V
  item: Adir N
  item: Fishman A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Influencing the monophenolase/diphenolase activity ratio in tyrosinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/23305929
journal: Biochim Biophys Acta
volume: 1834
pages: 629-33
published year: 2013
authors:
  item: Goldfeder M
  item: Kanteev M
  item: Adir N
  item: Fishman A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Monophenol monooxygenase
type: KeggEnzyme

Phenolase
type: KeggEnzyme

Monophenol oxidase
type: KeggEnzyme

Cresolase
type: KeggEnzyme

Monophenolase
type: KeggEnzyme

Tyrosine-dopa oxidase
type: KeggEnzyme

Monophenol monooxidase
type: KeggEnzyme

Monophenol dihydroxyphenylalanine:oxygen oxidoreductase
type: KeggEnzyme

N-acetyl-6-hydroxytryptophan oxidase
type: KeggEnzyme

Monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase
type: KeggEnzyme

O-diphenol:O2 oxidoreductase
type: KeggEnzyme

Phenol oxidase
type: KeggEnzyme

Analogue
compound: O2
pdb: 1wx2A
ligand het code: PER

Analogue
compound: O2
pdb: 1wx4A
ligand het code: PER

Analogue
compound: L-dopa
pdb: 2zweA
ligand het code: DAH(chain B)

Analogue
compound: L-dopa
pdb: 2zwfA
ligand het code: DAH(chain B)

Analogue
compound: L-dopa
pdb: 2zwgA
ligand het code: DAH(chain B)

TransitionStateAnalogue
pdb: 3nq1A
ligand het code: KOJ

TransitionStateAnalogue
pdb: 3nq1B
ligand het code: KOJ

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig. 9, p.8989

ReferenceForCatalyticMechanism
reference index: 15
reference section: Scheme 2, p.4550

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig. 2, p.754-756

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig. 17, p.124-127

ReferenceForCatalyticMechanism
reference index: 23
reference section: Scheme 2, p.73-74

ReferenceForCatalyticMechanism
reference index: 25
reference section: p.232-234