KEGG   ENZYME: 1.10.3.1Help
Entry
EC 1.10.3.1                 Enzyme                                 

Name
catechol oxidase;
diphenol oxidase;
o-diphenolase;
polyphenol oxidase;
pyrocatechol oxidase;
dopa oxidase;
catecholase;
o-diphenol:oxygen oxidoreductase;
o-diphenol oxidoreductase
Class
Oxidoreductases;
Acting on diphenols and related substances as donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
1,2-benzenediol:oxygen oxidoreductase
Reaction(IUBMB)
2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O [RN:R00058]
Reaction(KEGG)
Substrate
catechol [CPD:C00090];
O2 [CPD:C00007]
Product
1,2-benzoquinone [CPD:C02351];
H2O [CPD:C00001]
Comment
A type 3 copper protein that catalyses exclusively the oxidation of catechol (i.e., o-diphenol) to the corresponding o-quinone. The enzyme also acts on a variety of substituted catechols.
It is different from tyrosinase, EC 1.14.18.1, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.
History
EC 1.10.3.1 created 1961, deleted 1972, reinstated 1978
Pathway
ec00350  Tyrosine metabolism
ec00950  Isoquinoline alkaloid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00422  polyphenol oxidase
Genes
CPAP: 110813716 110813822 110817816 110817849 110817859 110820923 110824768
CIT: 102625572
CIC: CICLE_v10014693mg
TCC: 18596894 18596895 18596896 18596897 18596899 18607763
GRA: 105771487 105772626 105772676 105773953 105795312 105798965
GHI: 107886301 107888998 107891789 107901674 107901676 107908785 107923401 107927826 107940403 107941595 107955348 107960202
DZI: 111278202 111278203 111282397 111286844 111308257 111318757
EGR: 104428733 104441046 104442643
GMX: 100037473 100037474 100785410 100789730 100792012 100798184 100798709 100801369 100801754 100802289 100802763 100803171 100803874 100815646 106799311
PVU: PHAVU_002G225600g PHAVU_006G188500g PHAVU_008G073200g
CAM: 101512236
LJA: Lj3g3v0278890.1(Lj3g3v0278890.1) Lj3g3v1729190.1(Lj3g3v1729190.1) Lj6g3v2044610.1(Lj6g3v2044610.1)
RCU: 8278545
JCU: 105649503
OSA: 4337055
DOSA: Os01t0793300-01(Os01g0793300) Os04t0624400-00(Os04g0624400) Os04t0624450-00(Os04g0624450) Os04t0624500-01(Os04g0624500)
ATS: 109735375(LOC109735375) 109747401(LOC109747401) 109762318(LOC109762318) 109762325(LOC109762325)
AOF: 109821572
 » show all
Taxonomy
Reference
1
  Authors
Brown, F.C. and Ward, D.N.
  Title
Preparation of a soluble mammalian tyrosinase.
  Journal
J Am Chem Soc 79:2647-2648 (1957)
Reference
2
  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
3  [PMID:16742427]
  Authors
Gregory RP, Bendall DS
  Title
The purification and some properties of the polyphenol oxidase from tea (Camellia sinensis L.).
  Journal
Biochem J 101:569-81 (1966)
Reference
4  [PMID:13288597]
  Authors
MASON HS.
  Title
Structures and functions of the phenolase complex.
  Journal
Nature 177:79-81 (1956)
Reference
5
  Authors
Mayer, A.M. and Harel, E.
  Title
Polyphenol oxidases in plants.
  Journal
Phytochemistry 18:193-215 (1979)
Reference
6  [PMID:5842066]
  Authors
Patil SS, Zucker M.
  Title
Potato phenolases. Purification and properties.
  Journal
J Biol Chem 240:3938-43 (1965)
Reference
7  [PMID:4965136]
  Authors
Pomerantz SH, Warner MC.
  Title
3,4-dihydroxy-L-phenylalanine as the tyrosinase cofactor. Occurrence in melanoma and binding constant.
  Journal
J Biol Chem 242:5308-14 (1967)
Reference
8
  Authors
Robb, D.A.
  Title
`Tyrosinase.
  Journal
In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, p. 207-240.
Reference
9  [PMID:11900522]
  Authors
Gerdemann C, Eicken C, Krebs B
  Title
The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins.
  Journal
Acc Chem Res 35:183-91 (2002)
DOI:10.1021/ar990019a
Other DBs
ExplorEnz - The Enzyme Database: 1.10.3.1
IUBMB Enzyme Nomenclature: 1.10.3.1
ExPASy - ENZYME nomenclature database: 1.10.3.1
BRENDA, the Enzyme Database: 1.10.3.1
CAS: 9002-10-2

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