KEGG   ENZYME: 1.10.3.2
Entry
EC 1.10.3.2                 Enzyme                                 

Name
laccase;
urishiol oxidase;
urushiol oxidase;
p-diphenol oxidase
Class
Oxidoreductases;
Acting on diphenols and related substances as donors;
With oxygen as acceptor
Sysname
benzenediol:oxygen oxidoreductase
Reaction(IUBMB)
4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O [RN:R00083]
Reaction(KEGG)
R00083
Substrate
benzenediol [CPD:C01785];
O2 [CPD:C00007]
Product
benzosemiquinone [CPD:C05309];
H2O [CPD:C00001]
Comment
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
History
EC 1.10.3.2 created 1961, deleted 1972, reinstated 1978
Orthology
K05909  laccase
Genes
SPU: 576682 584984 763460
SKO: 100376857
BIM: 100749951
MPHA: 105828680
AEC: 105150353
PBAR: 105432747
CFO: 105258597
MDL: 103578067
ATD: 109607983
NVL: 108558327
API: 100161156
DNX: 107162027
AGS: 114122215
RMD: 113552256
ATH: AT1G18140(LAC1) AT2G29130(LAC2) AT2G30210(LAC3) AT2G38080(IRX12) AT2G40370(LAC5) AT2G46570(LAC6) AT3G09220(LAC7) AT5G01040(LAC8) AT5G01050 AT5G01190(LAC10) AT5G03260(LAC11) AT5G05390(LAC12) AT5G07130(LAC13) AT5G09360(LAC14) AT5G48100(TT10) AT5G58910(LAC16) AT5G60020(LAC17)
LJA: Lj0g3v0125739.1(Lj0g3v0125739.1) Lj0g3v0285709.1(Lj0g3v0285709.1) Lj0g3v0316509.1(Lj0g3v0316509.1) Lj0g3v0346879.1(Lj0g3v0346879.1) Lj0g3v0351459.1(Lj0g3v0351459.1) Lj1g3v3438880.1(Lj1g3v3438880.1) Lj1g3v3438880.2(Lj1g3v3438880.2) Lj1g3v3444130.1(Lj1g3v3444130.1) Lj1g3v3458760.1(Lj1g3v3458760.1) Lj1g3v3458800.1(Lj1g3v3458800.1) Lj1g3v3460860.1(Lj1g3v3460860.1) Lj1g3v4139440.1(Lj1g3v4139440.1) Lj2g3v1472930.1(Lj2g3v1472930.1) Lj2g3v1734800.1(Lj2g3v1734800.1) Lj2g3v1734800.2(Lj2g3v1734800.2) Lj2g3v2353640.1(Lj2g3v2353640.1) Lj2g3v2353640.2(Lj2g3v2353640.2) Lj2g3v2833010.1(Lj2g3v2833010.1) Lj3g3v2477620.1(Lj3g3v2477620.1) Lj3g3v2679640.1(Lj3g3v2679640.1) Lj4g3v3114580.1(Lj4g3v3114580.1) Lj5g3v1886260.1(Lj5g3v1886260.1) Lj5g3v1887360.1(Lj5g3v1887360.1) Lj5g3v1887360.2(Lj5g3v1887360.2) Lj6g3v0607060.1(Lj6g3v0607060.1)
DOSA: Os01t0374600-00(Os01g0374600) Os01t0634500-00(Os01g0634500) Os01t0827300-01(Os01g0827300) Os01t0842400-01(Os01g0842400) Os01t0842500-01(Os01g0842500) Os01t0843800-00(Os01g0843800) Os01t0850550-00(Os01g0850550) Os01t0850700-01(Os01g0850700) Os01t0850800-00(Os01g0850800) Os02t0749700-00(Os02g0749700) Os03t0273200-01(Os03g0273200) Os03t0297900-00(Os03g0297900) Os05t0458300-00(Os05g0458300) Os05t0458500-00(Os05g0458500) Os05t0458600-01(Os05g0458600) Os07t0101000-00(Os07g0101000) Os10t0346300-01(Os10g0346300) Os10t0437400-00(Os10g0437400) Os11t0108700-00(Os11g0108700) Os11t0264000-00(Os11g0264000) Os11t0641500-01(Os11g0641500) Os11t0641800-01(Os11g0641800) Os11t0696900-01(Os11g0696900) Os11t0708100-01(Os11g0708100) Os12t0108000-01(Os12g0108000) Os12t0257600-00(Os12g0257600) Os12t0258700-01(Os12g0258700) Os12t0259800-00(Os12g0259800)
ATS: 109732250(LOC109732250) 109733461(LOC109733461) 109733475(LOC109733475) 109735427(LOC109735427) 109737451(LOC109737451) 109739354(LOC109739354) 109741539(LOC109741539) 109742867(LOC109742867) 109742875(LOC109742875) 109744176(LOC109744176) 109747523(LOC109747523) 109751413(LOC109751413) 109751424(LOC109751424) 109755005(LOC109755005) 109755006(LOC109755006) 109755009(LOC109755009) 109756584(LOC109756584) 109757794(LOC109757794) 109761206(LOC109761206) 109764227(LOC109764227) 109770675(LOC109770675) 109771469(LOC109771469) 109773822(LOC109773822) 109775212(LOC109775212) 109776065(LOC109776065) 109777232(LOC109777232) 109777911(LOC109777911) 109780419(LOC109780419) 109780486(LOC109780486) 109780530(LOC109780530) 109783243(LOC109783243) 109786257(LOC109786257) 109787120(LOC109787120)
 » show all
Reference
1
  Authors
Dawson, C.R. and Tarpley, W.B.
  Title
The copper oxidases.
  Journal
In: Sumner, J.B. and Myrback, K. (Eds.), The Enzymes, 1st ed., vol. 2, Academic Press, New York, 1951, p. 454-498.
Reference
2
  Authors
Keilin, D. and Mann, T.
  Title
Laccase, a blue copper-protein oxidase from the latex of Rhus succedanea.
  Journal
Nature (Lond) 143:23-24 (1939)
Reference
3
  Authors
Malmstrom, B.G., Andreasson, L.-E. and Reinhammar, B.
  Title
Copper-containing oxidases and superoxide dismutase.
  Journal
In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 12, Academic Press, New York, 1975, p. 507-579.
Reference
4
  Authors
Mayer, A.M. and Harel, E.
  Title
Polyphenol oxidases in plants.
  Journal
Phytochemistry 18:193-215 (1979)
Reference
5  [PMID:13584395]
  Authors
NAKAMURA T.
  Title
Purification and physico-chemical properties of laccase.
  Journal
Biochim Biophys Acta 30:44-52 (1958)
DOI:10.1016/0006-3002(58)90239-7
Reference
6  [PMID:13618260]
  Authors
NAKAMURA T.
  Title
Stoichiometric studies on the action of laccase.
  Journal
Biochim Biophys Acta 30:538-42 (1958)
DOI:10.1016/0006-3002(58)90100-8
Reference
7  [PMID:14304827]
  Authors
PEISACH J, LEVINE WG.
  Title
A COMPARISON OF THE ENZYMIC ACTIVITIES OF PIG CERULOPLASMIN AND RHUS VERNICIFERA LACCASE.
  Journal
J Biol Chem 240:2284-9 (1965)
Reference
8
  Authors
Reinhammar, B. and Malmstrom, B.G.
  Title
"Blue" copper-containing oxidases.
  Journal
In: Spiro, T.G. (Ed.), Copper Proteins, Copper Proteins, New York, 1981, p. 109-149.
Other DBs
ExplorEnz - The Enzyme Database: 1.10.3.2
IUBMB Enzyme Nomenclature: 1.10.3.2
ExPASy - ENZYME nomenclature database: 1.10.3.2
UM-BBD (Biocatalysis/Biodegradation Database): 1.10.3.2
BRENDA, the Enzyme Database: 1.10.3.2
CAS: 80498-15-3

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