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Literature summary extracted from

  • Liu, F.; Zhao, J.H.; Wen, X.; Ni, Y.Y.
    Purification and structural analysis of membrane-bound polyphenol oxidase from Fuji apple (2015), Food Chem., 183, 72-77 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.10.3.1 membrane membrane-bound Malus domestica 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.1 Cu2+ a copper enzyme Malus domestica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.10.3.1 2 4-methylcatechol + O2 Malus domestica
-
 2 4-methyl-1,2-benzoquinone + 2 H2O
-
 ?
1.10.3.1 2 catechol + O2 Malus domestica
-
 2 1,2-benzoquinone + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.1 Malus domestica
-
 cv. Red Fuji
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.1 native enzyme 54.41fold by temperature-induced phase partitioning technique, dialysis, and ion exchange chromatography Malus domestica

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.10.3.1 fruit
-
 Malus domestica
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.10.3.1 additional information
-
 370004 U/mg for the purified native enzyme. One unit of enzyme activity is defined as a 0.001-unit change in absorbance per min per ml Malus domestica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.1 2 4-methylcatechol + O2
-
 Malus domestica 2 4-methyl-1,2-benzoquinone + 2 H2O
-
 ?
1.10.3.1 2 4-methylcatechol + O2 best substrate Malus domestica 2 4-methyl-1,2-benzoquinone + 2 H2O
-
 ?
1.10.3.1 2 catechol + O2
-
 Malus domestica 2 1,2-benzoquinone + 2 H2O
-
 ?
1.10.3.1 additional information the putative substrate-binding pocket contains six polar or charged amino acids, His191, His221, Trp224, Trp228, Phe227, and Val190. Trp224 and Trp228 form hydrogen bonds with 4-methylcatechol. Molecular docking of optimum substrate of mPPO, 4-methylcatechol, overview Malus domestica ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.10.3.1 ? x * 67300, SDS-PAGE Malus domestica
1.10.3.1 More 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 Malus domestica

Synonyms

EC Number Synonyms Comment Organism
1.10.3.1 MppO
-
 Malus domestica
1.10.3.1 polyphenol oxidase
-
 Malus domestica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.1 20
-
 assay at Malus domestica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.1 6.8
-
 assay at Malus domestica

General Information

EC Number General Information Comment Organism
1.10.3.1 additional information three-dimensional structure modeling based on the Vitis vinifera PPO, PDB ID 2P3X, as template Malus domestica