1.10.3.1: catechol oxidase

This is an abbreviated version!
For detailed information about catechol oxidase, go to the full flat file.

Reaction

2 catechol +

Synonyms

1,2-benzene: oxygen oxidoreductase, 1,2-benzenediol:oxygen oxidoreductase, AoCO4, catalase-phenol oxidase, catechol oxidase, catecholase, catecholoxidase, CATPO, CO, copper-S100B, cresolase, dihydroxy-L-phenylalanine:oxygen oxidoreductase, Diphenol oxidase, diphenolase, dopa oxidase, germin-like protein, GLP, hemocyanin, ibCO, LsPPO, mettyrosinase, monophenol, o-diphenol: oxygen oxidoreductase, monophenol, o-diphenol:oxygen oxidoreductase, More, MppO, o-diphenol oxidoreductase, o-diphenol: dioxygen oxidoreductase, dehydrogenating, o-diphenol:oxygen oxidoreductase, o-diphenolase, o-diphenoloxidase, oxytyrosinase, phenol oxidase, phenolase, phenoloxidase, polyphenol oxidase, polyphenoloxidase, PPO, PPO 1, PPO 2, PPO II, PPO-6, pyrocatechol oxidase, TYR3, tyrosinase

ECTree

     1 Oxidoreductases

         1.10 Acting on diphenols and related substances as donors

             1.10.3 With oxygen as acceptor

                1.10.3.1 catechol oxidase

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Results	in table
40	Activating Compound
306	AA Sequence
11	Application
1	CAS Registry Number
10	Cloned(Commentary)
9	Cofactor
7	Crystallization (Commentary)
2100	Disease/ Diagnostics
2	Expression
13	General Information
2	General Stability
113	IC50 Value
459	Inhibitors
33	Ki Value [mM]
185	KM Value [mM]
14	Localization
58	Metals/Ions
77	Molecular Weight [Da]
59	Natural Substrates/ Products (Substrates)
123	Organism
5	Pathway
14	PDB ID
86	pH Optimum
25	pH Range
20	pH Stability
2	pI Value
10	Posttranslational Modification
1	Protein Variants
54	Purification (Commentary)
3	Reaction
3	Reaction Type
118	Reference
1	Renatured (Commentary)
93	Source Tissue
120	Specific Activity [micromol/min/mg]
2	Storage Stability
503	Substrates and Products (Substrate)
49	Subunits
251	Synonyms
1	Systematic Name
65	Temperature Optimum [°C]
19	Temperature Range [°C]
55	Temperature Stability [°C]
71	Turnover Number [1/s]

Subunits

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Subunits on EC 1.10.3.1 - catechol oxidase

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

?

12 entries

dimer

3 entries

heterodimer

Amphioctopus fangsiao

-

1 * 75600 + 1 * 73000, proenzyme, estimated from SDS-PAGE

710702

hexamer

Scyllarides latus

-

6 * 78000, SDS-PAGE

675076

homohexamer

Erimacrus isenbeckii

-

6 * 75000, SDS-PAGE

711789

monomer

18 entries

multimer

Vigna unguiculata

-

by partially denaturing SDS-PAGE multiple molecular forms of active PPO are detected: 58 kDa, 73 kDa and 220 kDa

706120

tetramer

4 entries

trimer

2 entries

additional information

8 entries

?

Beta vulgaris

-

x * 36000, latent, nonactivated membrane isozyme, SDS-PAGE, x * 32000, trypsin-activated membrane isozyme, SDS-PAGE

674774

?

Cynara cardunculus var. scolymus

-

x * 57000, SDS-PAGE

658960

?

Malus domestica

-

x * 67300, SDS-PAGE

744954

?

Malus sp.

-

x * 40000, SDS-PAGE

673785

?

Mangifera indica

D2XZ13

x * 144000 + x * 112000 + x * 72000 + x * 23000, SDS-PAGE, differently distributed in fruit pulp and skin, some might by degeneration products

744952

?

Morus alba

-

x * 65000, SDS-PAGE

658788

?

Musa x paradisiaca

-

? * 40000, SDS-PAGE

713387

?

Solanum tuberosum

-

x * 40000, SDS-PAGE

673783

?

Streptomyces griseus

-

x * 100000, SDS-PAGE

440442

?

Streptomyces griseus

-

x * 37000, deduced from amino acid sequence

440442

?

Trichoderma reesei

-

x * 43200, recombinant enzyme, SDS-PAGE, x * 61151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry

673560

?

Zea mays

-

x * 158000, SDS-PAGE

744661

dimer

Aspergillus oryzae

Q2UNF9

the full-length form and the truncated form of AoCO4 are dimers in solution, the dimerisation does not have a clear functional role

725559

dimer

Portulaca grandiflora

-

1 * 27000 + 1 * 25000, isoenzyme II, SDS-PAGE

440441

dimer

Taraxacum officinale

I7HUF2

2 * 60000, recombinant mutant C197S mutein-tagged isozyme PPO-6, SDS-PAGE

726187

monomer

Beta vulgaris

-

1 * 60000, SDS-PAGE

658955

monomer

Beta vulgaris

-

1 * 40000

673001

monomer

Homo sapiens

-

1 * 66700

673001

monomer

Ipomoea batatas

Q9ZP19

SDS-PAGE

686666

monomer

Ipomoea batatas

-

1 * 39000

440435

monomer

Lonicera japonica

-

1 * 49000, SDS-PAGE

727570

monomer

Lonicera japonica

-

1 * 49277, LC-ESI mass spectrometry

727570

monomer

Musa x paradisiaca

-

1 * 42000, SDS-PAGE

440433

monomer

Neurospora crassa

-

1 * 46000

673001

monomer

Nicotiana tabacum

-

1 * 42000, SDS-PAGE

440438

monomer

Nicotiana tabacum

-

1 * 36500, MALDI-TOF mass spectrometry

440438

monomer

Portulaca grandiflora

-

1 * 65000, isoenzyme Ib, SDS-PAGE

440441

monomer

Portulaca grandiflora

-

1 * 66000, isoenzyme Ia, SDS-PAGE

440441

monomer

Pouteria sapota

-

1 * 18000, SDS-PAGE

713239

monomer

Rhaphiolepis bibas

-

1 x 59200, particulate, latent enzyme form, SDS-PAGE

671593

monomer

Streptomyces glaucescens

-

1 * 30900

673001

monomer

Vitis vinifera

P43311

1 * 40000, mature enzyme, SDS-PAGE

440430

monomer

Vitis vinifera

P43311

1 * 56700, mature enzyme, enzyme is synthesized as a 67300 Da precursor protein, predicted from nucleotide sequence

440430

tetramer

Agaricus bisporus

-

2 * 134000 + 2 * 43000, alpha2beta2 subunit composition

673001

tetramer

Lablab purpureus

-

-

671857

tetramer

Lablab purpureus

-

4 * 30000, SDS-PAGE

440434

tetramer

Taraxacum officinale

I7HUF2

4 * 60000, recombinant wild-type Strep2-tagged isozyme PPO-6, SDS-PAGE

726187

trimer

Panulirus argus

-

1 * 77000 + 1 * 80000 + 1 * 89000

696393

trimer

Streptomyces griseus

-

3 * 34000, boiling for 20 min, SDS-PAGE

440442

additional information

Aspergillus oryzae

Q2UNF9

structure analysis

725559

additional information

Aspergillus oryzae

-

structure analysis

725559

additional information

Coffea arabica

-

enzyme may be synthesized as a 67000 Da precursor that can be hydrolyzed to a 45000 Da form still retaining catalytic activity

440436

additional information

Lablab purpureus

-

the Stokes radius of the native enzyme is found to increase from 49.1 to 75.9 A upon activation of the enzyme, neither SDS nor acid-pH activation brought about any change in the quaternary structure

671857

additional information

Malus domestica

-

the three-dimensional structure of mPPO consists of six alpha-helices, two short beta-strands, and ten random coils, three-dimensional structure modeling based on the Vitis vinifera PPO, PDB ID 2P3X, as template

744954

additional information

Taraxacum officinale

I7HUF2

isozyme PPO-6 is a tetramer, the surface-exposed Cys197 residue stabilizes the tetramer via a disulfide linkage

726187

additional information

Taraxacum officinale

-

isozyme PPO-6 is a tetramer, the surface-exposed Cys197 residue stabilizes the tetramer via a disulfide linkage

726187

additional information

Trichoderma reesei

-

N-terminal and C-terminal structural analyses by fragmentation, chromatography, MS and peptide sequencing of the purified recombinant enzyme, overview

673560