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Literature summary for 1.10.3.1 extracted from

  • Fan, T.; Li, M.; Wang, J.; Yang, L.; Cong, R.
    Purification and characterization of phenoloxidase from Octopus ocellatus (2009), Acta Biochim. Biophys. Sin., 41, 865-872.
    View publication on PubMed
Search for more literature for 1.10.3.1

Activating Compound

Activating Compound Comment Organism Structure
Cu2+ phenoloxdiase is a copper-containing metalloenzyme Amphioctopus fangsiao

Inhibitors

Inhibitors Comment Organism Structure
1-Phenyl-2-thiourea complete inhibition at 5 mM Amphioctopus fangsiao
ascorbic acid 70.95% inhibition at 20 mM Amphioctopus fangsiao
benzoic acid 64.86% inhibition at 10 mM Amphioctopus fangsiao
Citric acid 68.92% inhibition at 20 mM Amphioctopus fangsiao
Cu2+ 91.45% inhibition at 20 mM Amphioctopus fangsiao
diethyldithiocarbamate 72.37% inhibition at 20 mM, the diethyldithiocarbamate-inhibited phenoloxidase-like activity can be perfectly restored by 10 mM Cu2+ while Zn2+ has no recovery effect Amphioctopus fangsiao
EDTA 75% inhibition at 10 mM Amphioctopus fangsiao
L-cysteine 43.24% inhibition at 20 mM Amphioctopus fangsiao
additional information no inhibition by Ca2+ and Mg2+ Amphioctopus fangsiao
sodium sulfite complete inhibition at 10 mM Amphioctopus fangsiao
Thiourea 84.46% inhibition at 10 mM Amphioctopus fangsiao
Zn2+ 45.39% inhibition at 20 mM Amphioctopus fangsiao

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1
-
 L-Dopa in 20 mM Tris-HCl buffer at pH 7.1 and 28°C Amphioctopus fangsiao
6.3
-
 catechol in 20 mM Tris-HCl buffer at pH 7.1 and 28°C Amphioctopus fangsiao

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
73000
-
 1 * 75600 + 1 * 73000, proenzyme, estimated from SDS-PAGE Amphioctopus fangsiao
75600
-
 1 * 75600 + 1 * 73000, proenzyme, estimated from SDS-PAGE Amphioctopus fangsiao
153800
-
 gel filtration Amphioctopus fangsiao

Organism

Organism UniProt Comment Textmining
Amphioctopus fangsiao
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sephacryl S-100 gel filtration Amphioctopus fangsiao

Source Tissue

Source Tissue Comment Organism Textmining
ink sac
-
 Amphioctopus fangsiao
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 the specific activity of the crude enzyme is 3.72 units/mg, the specific activity of the 28.24fold purified enzyme is 105 units/mg, one unit is defined as an increase in the rate of absorbance of 0.001 per min, using L-dopa as substrate, at pH 7.1 and 28°C Amphioctopus fangsiao

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 catechol + O2
-
 Amphioctopus fangsiao 2 1,2-benzoquinone + 2 H2O
-
 ?
L-Dopa + O2 specific substrate Amphioctopus fangsiao L-dopaquinone + H2O
-
 ?
additional information the enzyme fails to oxidize hydroquinone, phenol, or tyrosine Amphioctopus fangsiao ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 75600 + 1 * 73000, proenzyme, estimated from SDS-PAGE Amphioctopus fangsiao

Synonyms

Synonyms Comment Organism
phenoloxidase
-
 Amphioctopus fangsiao

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Amphioctopus fangsiao

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 50
-
 Amphioctopus fangsiao

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Amphioctopus fangsiao

pH Range

pH Minimum pH Maximum Comment Organism
6 8
-
 Amphioctopus fangsiao

General Information

General Information Comment Organism
physiological function phenoloxidase functions as a catalytic enzyme in melanin production in ink sacs and also as a humoral factor in host defense via melaninization Amphioctopus fangsiao