DB code: T00215

CATH domain 2.60.40.420 : Immunoglobulin-like Catalytic domain
2.60.40.420 : Immunoglobulin-like
2.60.40.420 : Immunoglobulin-like Catalytic domain
E.C. 1.10.3.2
CSA 1a65
M-CSA 1a65
MACiE

CATH domain Related DB codes (homologues)
2.60.40.420 : Immunoglobulin-like T00216 M00115 M00062 M00194

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
Q12718 Laccase-2
EC 1.10.3.2
Benzenediol:oxygen oxidoreductase 2
Urishiol oxidase 2
Diphenol oxidase 2
Laccase I
PF00394 (Cu-oxidase)
PF07731 (Cu-oxidase_2)
PF07732 (Cu-oxidase_3)
[Graphical View]
Q96UT7
Laccase B
EC 1.10.3.2
PF00394 (Cu-oxidase)
PF07731 (Cu-oxidase_2)
PF07732 (Cu-oxidase_3)
[Graphical View]
Q9Y780
Laccase 1
EC 1.10.3.2
PF00394 (Cu-oxidase)
PF07731 (Cu-oxidase_2)
PF07732 (Cu-oxidase_3)
[Graphical View]
Q6H9H7
Laccase
EC 1.10.3.2
PF00394 (Cu-oxidase)
PF07731 (Cu-oxidase_2)
PF07732 (Cu-oxidase_3)
[Graphical View]
Q70KY3 Laccase-1
EC 1.10.3.2
Benzenediol:oxygen oxidoreductase 1
Urishiol oxidase 1
Diphenol oxidase 1
Ligninolytic phenoloxidase
PF00394 (Cu-oxidase)
PF07731 (Cu-oxidase_2)
PF07732 (Cu-oxidase_3)
[Graphical View]

KEGG enzyme name
laccase
urishiol oxidase
urushiol oxidase
p-diphenol oxidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q12718 LAC2_TRAVE 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. Secreted. Binds 4 copper ions per monomer.
Q96UT7 Q96UT7_TRAVE
Q9Y780 Q9Y780_COPCI
Q6H9H7 Q6H9H7_9APHY
Q70KY3 LAC1_MELAO 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. Monomer. Binds 4 copper ions per monomer.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00070 C01785 C00007 C02389 C00001
E.C.
Compound Copper Benzenediol O2 Benzosemiquinone H2O
Type heavy metal aromatic ring (only carbon atom) others aromatic ring (only carbon atom) H2O
ChEBI 28694
 30052
 28694
 30052
 		18135
 18135
 		15379
 26689
 27140
 15379
 26689
 27140
 		17977
 17977
 		15377
 15377
PubChem 23978
 23978
 		289
 289
 		977
 977
 		46173720
 46173720
 		22247451
 962
 22247451
 962
1gycA01 Bound:_CU Unbound Unbound Unbound Unbound
1kyaA01 Bound:_CU Unbound Unbound Unbound Unbound
1kyaB01 Bound:_CU Unbound Unbound Unbound Unbound
1kyaC01 Bound:_CU Unbound Unbound Unbound Unbound
1kyaD01 Bound:_CU Unbound Unbound Unbound Unbound
1a65A01 Bound:_CU Unbound Unbound Unbound Unbound
1hfuA01 Bound:_CU Unbound Unbound Unbound Unbound
1v10A01 Bound:_CU Unbound Unbound Unbound Unbound
1gw0A01 Bound:_CU Unbound Unbound Unbound Unbound
1gw0B01 Bound:_CU Unbound Unbound Unbound Unbound
1gycA02 Unbound Unbound Unbound Unbound Unbound
1kyaA02 Unbound Unbound Unbound Unbound Unbound
1kyaB02 Unbound Unbound Unbound Unbound Unbound
1kyaC02 Unbound Unbound Unbound Unbound Unbound
1kyaD02 Unbound Unbound Unbound Unbound Unbound
1a65A02 Unbound Unbound Unbound Unbound Unbound
1hfuA02 Unbound Unbound Unbound Unbound Unbound
1v10A02 Unbound Unbound Unbound Unbound Unbound
1gw0A02 Unbound Unbound Unbound Unbound Unbound
1gw0B02 Unbound Unbound Unbound Unbound Unbound
1gycA03 Bound:3x_CU Unbound Unbound Unbound Unbound
1kyaA03 Bound:3x_CU Analogue:XYD Unbound Unbound Unbound
1kyaB03 Bound:3x_CU Analogue:XYD Unbound Unbound Unbound
1kyaC03 Bound:3x_CU Analogue:XYD Unbound Unbound Unbound
1kyaD03 Bound:3x_CU Analogue:XYD Unbound Unbound Unbound
1a65A03 Bound:2x_CU Unbound Unbound Unbound Intermediate-bound:__O
1hfuA03 Bound:2x_CU Unbound Unbound Unbound Unbound
1v10A03 Bound:3x_CU Unbound Unbound Unbound Unbound
1gw0A03 Bound:3x_CU Unbound Bound:OXY Unbound Unbound
1gw0B03 Bound:3x_CU Unbound Bound:OXY Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2], [6]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1gycA01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1kyaA01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1kyaB01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1kyaC01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1kyaD01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1a65A01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1hfuA01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1v10A01 HIS 111(Copper-3a);HIS 66;HIS 109(Copper-3b);HIS 64(Copper-2)
1gw0A01 HIS 140(Copper-3a);HIS 95;HIS 138(Copper-3b);HIS 93(Copper-2)
1gw0B01 HIS 140(Copper-3a);HIS 95;HIS 138(Copper-3b);HIS 93(Copper-2)
1gycA02
1kyaA02
1kyaB02
1kyaC02
1kyaD02
1a65A02
1hfuA02
1v10A02
1gw0A02
1gw0B02
1gycA03 HIS 452;CYS 453;HIS 454 HIS 395;CYS 453;HIS 458(Copper-1);HIS 400;HIS 452(Copper-3a);HIS 454(Copper-3b);HIS 398(Copper-2)
1kyaA03 HIS 452;CYS 453;HIS 454 HIS 395;CYS 453;HIS 458(Copper-1);HIS 400;HIS 452(Copper-3a);HIS 454(Copper-3b);HIS 398(Copper-2)
1kyaB03 HIS 452;CYS 453;HIS 454 HIS 395;CYS 453;HIS 458(Copper-1);HIS 400;HIS 452(Copper-3a);HIS 454(Copper-3b);HIS 398(Copper-2)
1kyaC03 HIS 452;CYS 453;HIS 454 HIS 395;CYS 453;HIS 458(Copper-1);HIS 400;HIS 452(Copper-3a);HIS 454(Copper-3b);HIS 398(Copper-2)
1kyaD03 HIS 452;CYS 453;HIS 454 HIS 395;CYS 453;HIS 458(Copper-1);HIS 400;HIS 452(Copper-3a);HIS 454(Copper-3b);HIS 398(Copper-2)
1a65A03 HIS 451;CYS 452;HIS 453 HIS 396;CYS 452;HIS 457(Copper-1);HIS 401;HIS 451(Copper-3a);HIS 453(Copper-3b);HIS 399(Copper-2)
1hfuA03 HIS 451;CYS 452;HIS 453 HIS 396;CYS 452;HIS 457(Copper-1);HIS 401;HIS 451(Copper-3a);HIS 453(Copper-3b);HIS 399(Copper-2)
1v10A03 HIS 451;CYS 452;HIS 453 HIS 396;CYS 452;HIS 457(Copper-1);HIS 401;HIS 451(Copper-3a);HIS 453(Copper-3b);HIS 399(Copper-2)
1gw0A03 HIS 502;CYS 503;HIS 504 HIS 431;CYS 503;HIS 508(Copper-1);HIS 436;HIS 502(Copper-3a);HIS 504(Copper-3b);HIS 434(Copper-2)
1gw0B03 HIS 502;CYS 503;HIS 504 HIS 431;CYS 503;HIS 508(Copper-1);HIS 436;HIS 502(Copper-3a);HIS 504(Copper-3b);HIS 434(Copper-2)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.19, p.197-203
[5]
Fig.9, Fig. 10
[6]
p.314
[7]
Fig. 10
[8]
FIG. 7, p.32723-32724
[14]
p.7330-7331
[17]
[18]
p.553-554
[24]
Scheme 2, p.192
[25]
p.1525-1528
[26]
p.94-95

References
[1]
Resource
Comments
Medline ID
PubMed ID 1647440
Journal J Inorg Biochem
Year 1991
Volume 41
Pages 253-60
Authors Meadows KA, Morie-Bebel MM, McMillin DR
Title Copper transfer from Rhus vernicifera laccase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID 92194315
PubMed ID 1548698
Journal J Mol Biol
Year 1992
Volume 224
Pages 179-205
Authors Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A
Title Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7704270
Journal Microbiology
Year 1995
Volume 141
Pages 393-8
Authors Youn HD, Kim KJ, Maeng JS, Han YH, Jeong IB, Jeong G, Kang SO, Hah YC
Title Single electron transfer by an extracellular laccase from the white-rot fungus Pleurotus ostreatus.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9693103
Journal Biochem J
Year 1998
Volume 334
Pages 63-70
Authors Xu F, Berka RM, Wahleithner JA, Nelson BA, Shuster JR, Brown SH, Palmer AE, Solomon EI
Title Site-directed mutations in fungal laccase: effect on redox potential, activity and pH profile.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9602107
Journal Biochim Biophys Acta
Year 1998
Volume 1384
Pages 160-70
Authors Huang HW, Sakurai T, Monjushiro H, Takeda S
Title Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9546223
Journal Nat Struct Biol
Year 1998
Volume 5
Pages 310-6
Authors Ducros V, Brzozowski AM, Wilson KS, Brown SH, Ostergaard P, Schneider P, Yaver DS, Pedersen AH, Davies GJ
Title Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution.
Related PDB 1a65
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10583375
Journal Eur J Biochem
Year 1999
Volume 266
Pages 820-30
Authors Gromov I, Marchesini A, Farver O, Pecht I, Goldfarb D
Title Azide binding to the trinuclear copper center in laccase and ascorbate oxidase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10551829
Journal J Biol Chem
Year 1999
Volume 274
Pages 32718-24
Authors Huang H, Zoppellaro G, Sakurai T
Title Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11173497
Journal Acta Crystallogr D Biol Crystallogr
Year 2001
Volume 57
Pages 333-6
Authors Ducros V, Brzozowski AM, Wilson KS, Ostergaard P, Schneider P, Svendson A, Davies GJ
Title Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.
Related PDB 1hfu
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11703175
Journal Biochemistry (Mosc)
Year 2001
Volume 66
Pages 960-6
Authors Koroleva OV, Stepanova EV, Gavrilova VP, Biniukov VI, Pronin AM
Title Comparative characterization of methods for removal of Cu(II) from the active sites of fungal laccases.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11554598
Journal Bioresour Technol
Year 2001
Volume 80
Pages 29-36
Authors Aktas N, Cicek H, Unal AT, Kibarer G, Kolankaya N, Tanyolac A
Title Reaction kinetics for laccase-catalyzed polymerization of 1-naphthol.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11192701
Journal J Inorg Biochem
Year 2001
Volume 83
Pages 67-75
Authors Bonomo RP, Cennamo G, Purrello R, Santoro AM, Zappala R
Title Comparison of three fungal laccases from Rigidoporus lignosus and Pleurotus ostreatus: correlation between conformation changes and catalytic activity.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11565899
Journal J Protein Chem
Year 2001
Volume 20
Pages 191-201
Authors Garzillo AM, Colao MC, Buonocore V, Oliva R, Falcigno L, Saviano M, Santoro AM, Zappala R, Bonomo RP, Bianco C, Giardina P, Palmieri G, Sannia G
Title Structural and kinetic characterization of native laccases from Pleurotus ostreatus, Rigidoporus lignosus, and Trametes trogii.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12044164
Journal Biochemistry
Year 2002
Volume 41
Pages 7325-33
Authors Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, Mougin C
Title Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics.
Related PDB 1kya
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 12445477
Journal Biochim Biophys Acta
Year 2002
Volume 1601
Pages 155-62
Authors Ragusa S, Cambria MT, Pierfederici F, Scire A, Bertoli E, Tanfani F, Cambria A
Title Structure-activity relationship on fungal laccase from Rigidoporus lignosus: a Fourier-transform infrared spectroscopic study.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11884407
Journal J Biol Chem
Year 2002
Volume 277
Pages 18849-59
Authors Martins LO, Soares CM, Pereira MM, Teixeira M, Costa T, Jones GH, Henriques AO
Title Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 12163489
Journal J Biol Chem
Year 2002
Volume 277
Pages 37663-9
Authors Piontek K, Antorini M, Choinowski T
Title Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers.
Related PDB 1gyc
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 12118243
Journal Nat Struct Biol
Year 2002
Volume 9
Pages 601-5
Authors Hakulinen N, Kiiskinen LL, Kruus K, Saloheimo M, Paananen A, Koivula A, Rouvinen J
Title Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site.
Related PDB 1gw0
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 12126701
Journal Phytochemistry
Year 2002
Volume 60
Pages 551-65
Authors Mayer AM, Staples RC
Title Laccase: new functions for an old enzyme.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 14574106
Journal Antonie Van Leeuwenhoek
Year 2003
Volume 84
Pages 289-99
Authors Valderrama B, Oliver P, Medrano-Soto A, Vazquez-Duhalt R
Title Evolutionary and structural diversity of fungal laccases.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 12800133
Journal Biotechnol Bioeng
Year 2003
Volume 83
Pages 386-94
Authors Kumar SV, Phale PS, Durani S, Wangikar PP
Title Combined sequence and structure analysis of the fungal laccase family.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 12817956
Journal Inorg Chem
Year 2003
Volume 42
Pages 4006-17
Authors Palmer AE, Szilagyi RK, Cherry JR, Jones A, Xu F, Solomon EI
Title Spectroscopic characterization of the Leu513His variant of fungal laccase: effect of increased axial ligand interaction on the geometric and electronic structure of the type 1 Cu site.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 12637519
Journal J Biol Chem
Year 2003
Volume 278
Pages 19416-25
Authors Enguita FJ, Martins LO, Henriques AO, Carrondo MA
Title Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 12929410
Journal Org Biomol Chem
Year 2003
Volume 1
Pages 191-7
Authors Baiocco P, Barreca AM, Fabbrini M, Galli C, Gentili P
Title Promoting laccase activity towards non-phenolic substrates: a mechanistic investigation with some laccase-mediator systems.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 15364578
Journal J Mol Biol
Year 2004
Volume 342
Pages 1519-31
Authors Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M
Title The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair.
Related PDB 1v10
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 15036303
Journal Micron
Year 2004
Volume 35
Pages 93-6
Authors Claus H
Title Laccases: structure, reactions, distribution.
Related PDB
Related UniProtKB

Comments
Coppers can be classified into three types (see [5]):
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 [2] & [6]).
This reaction catalyzes the following reactions (see [2] and [6]):
(A) Oxidation 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:

Created Updated
2005-04-15 2009-10-01