1.10.3.1: catechol oxidase
This is an abbreviated version!
For detailed information about catechol oxidase, go to the full flat file.
Word Map on EC 1.10.3.1
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1.10.3.1
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limpet
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keyhole
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brown
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catalase
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lymphocyte
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dismutase
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hemolymph
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igm
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humoral
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larvae
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shrimp
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mushroom
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haptens
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vannamei
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sod
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antigen-specific
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melanization
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arthropod
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haemocyte
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melanin
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crab
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litopenaeus
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idiotype
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o-quinones
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crustacean
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hepatopancreas
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chlorogenic
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delayed-type
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ammonia-lyase
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l-dopa
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postharvest
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laccase
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shelf
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molluscan
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anti-idiotypic
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dinuclear
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gastropod
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crayfish
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nutrition
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pyrogallol
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agriculture
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drug development
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lobster
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alginolyticus
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entomopathogenic
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copper-binding
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antiferromagnetic
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penaeus
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kojic
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copper-containing
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pomatia
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food industry
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toxoid
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limulus
- 1.10.3.1
-
limpet
-
keyhole
- brown
- catalase
- lymphocyte
- dismutase
- hemolymph
- igm
-
humoral
- larvae
- shrimp
- mushroom
-
haptens
- vannamei
- sod
-
antigen-specific
-
melanization
-
arthropod
- haemocyte
- melanin
- crab
- litopenaeus
-
idiotype
- o-quinones
-
crustacean
- hepatopancreas
-
chlorogenic
-
delayed-type
-
ammonia-lyase
- l-dopa
-
postharvest
- laccase
-
shelf
-
molluscan
-
anti-idiotypic
-
dinuclear
-
gastropod
- crayfish
- nutrition
- pyrogallol
- agriculture
- drug development
- lobster
- alginolyticus
-
entomopathogenic
-
copper-binding
-
antiferromagnetic
- penaeus
-
kojic
-
copper-containing
- pomatia
- food industry
- toxoid
- limulus
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
1.10.3.1 catechol oxidaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 1.10.3.1 - catechol oxidase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
hydrogen peroxide
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activating at higher concentrations, however, the concentration of dihydrogen peroxide, formed during the reaction, does not reach this level
catechol
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5 mM catechol results in a 5-8fold acceleration of the rate of oxidation of 2.5 mM L-Dopa
catechol
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5 mM catechol results in a 5-8fold acceleration of the rate of oxidation of 2.5 mM L-Dopa
SDS
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after the addition of SDS, the catecholoxidase activity of Eurypelma hemocyanin develops gradually over a period of 5 min until a constant activity is reached
SDS
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PPO from membrane shows no diphenolase activity unless it is activated by trypsin or sodium dodecyl sulfate
SDS
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when 0.04 mM SDS is added, the phenoloxidase activity starts to increase and peaks at 5 mM SDS (125fold increase)
SDS
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severalfold activation at concentration below the critical micellar concentration of the enzyme, 15-20% activation at concentration below 0.3 mM, maximal activation at 1.25 mM, the activation by SDS and acidic pH results in a localized conformational change that is anchored around the catalytic site of PPO that alters the microenvironment of an essential glutamic residue
SDS
enhances the PPO activity in fruits, with pulp showing a stronger increase than skin
Trypsin
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PPO from membrane shows no diphenolase activity unless it is activated by trypsin or sodium dodecyl sulfate, kinetics of the activation process of latent PPO by trypsin
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Trypsin
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when 0.001 mM trypsin is added, the phenoloxidase activity starts to increase and peaks at 0.04 mM trypsin (40fold increase)
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additional information
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mushroom tyrosinase's catecholase activity is activated by some n-alkyl carboxylic acid derivates whereas mushroom tyrosinase's cresolase activity is inhibited by the same substances
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additional information
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the presence of 5 mM of the following monophenolics has no effect on the rate of oxidation of 2.5 mM L-Dopa: 2-hydroxybenzoic acid (salicylic acid), 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, (2-, 3-, or 4-)coumaric acids (2-, 3-, or 4-hydroxycinnamic acid). Additionally, neither 5 mM vanillin (4-hydroxy-3-methoxybenzaldehyde) nor pyrogallol (1,2,3-trihydroxybenzene) has any effect of the oxidation of 2.5 mM L-DOPA
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additional information
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the presence of 5 mM of the following monophenolics has no effect on the rate of oxidation of 2.5 mM L-Dopa: 2-hydroxybenzoic acid (salicylic acid), 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, (2-, 3-, or 4-)coumaric acids (2-, 3-, or 4-hydroxycinnamic acid). Additionally, neither 5 mM vanillin (4-hydroxy-3-methoxybenzaldehyde) nor pyrogallol (1,2,3-trihydroxybenzene) has any effect of the oxidation of 2.5 mM L-DOPA
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additional information
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beta-1,3-glucan has almost no effect on the phenoloxidase activity
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additional information
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highest activity is measured using the following buffer composition: sodium phosphate + Triton X-100 (1%) + PVP (0.5%) + EDTA (1.0 mM) + sodium thiosulfate (0.25%)
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additional information
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the enzyme is activated on exposure to acid-pH, activation at pH 2.5 and at pH 4.0, reversal of the activation is possible at pH 7.0, the activation by SDS and acidic pH results in a localized conformational change that is anchored around the catalytic site of PPO that alters the microenvironment of an essential glutamic residue, concentration or on exposure to acid-pH, the enzymes possesses a core carboxylate essential to activity, this enhanced catalytic efficiency of PPO, overview
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