Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Selles-Marchart, S.; Casado-Vela, J.; Bru-Martinez, R.
    Isolation of a latent polyphenol oxidase from loquat fruit (Eriobotrya japonica Lindl.): kinetic characterization and comparison with the active form (2006), Arch. Biochem. Biophys., 446, 175-185.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.1 2-mercaptoethanol
-
Rhaphiolepis bibas
1.10.3.1 ascorbate
-
Rhaphiolepis bibas
1.10.3.1 DTT
-
Rhaphiolepis bibas
1.10.3.1 glutathione
-
Rhaphiolepis bibas
1.10.3.1 L-cysteine
-
Rhaphiolepis bibas
1.10.3.1 additional information sensitivity to inhibitors of the soluble and particulate enzyme forms, overview Rhaphiolepis bibas
1.10.3.1 NaCl
-
Rhaphiolepis bibas
1.10.3.1 NaF
-
Rhaphiolepis bibas
1.10.3.1 Sodium diethyl dithiocarbamate
-
Rhaphiolepis bibas
1.10.3.1 sodium disulfite
-
Rhaphiolepis bibas
1.10.3.1 Thiourea
-
Rhaphiolepis bibas
1.10.3.1 tropolone
-
Rhaphiolepis bibas

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.1 additional information
-
additional information temperature and pH dependencis of the two enzyme forms, in absence or presence of SDS Rhaphiolepis bibas
1.10.3.1 1
-
chlorogenic acid pH 4.5, 25°C, soluble, active enzyme form Rhaphiolepis bibas
1.10.3.1 1.2
-
tert-butyl-catechol pH 4.5, 25°C, soluble, active enzyme form Rhaphiolepis bibas
1.10.3.1 1.23
-
tert-butyl-catechol pH 4.5, 25°C, particulate, latent enzyme form Rhaphiolepis bibas
1.10.3.1 5.7
-
chlorogenic acid pH 4.5, 25°C, particulate, latent enzyme form Rhaphiolepis bibas

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.10.3.1 particle-bound 80% of total activity Rhaphiolepis bibas
-
-
1.10.3.1 soluble 20% of total activity Rhaphiolepis bibas
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.1 Cu2+ active site binding Rhaphiolepis bibas

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.1 61200
-
particulate, latent enzyme form, gel filtration Rhaphiolepis bibas

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.1 Rhaphiolepis bibas
-
cv. Algerie
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.1 native soluble, active enzyme form partially 3.3fold by ammonium sulfate fractionation, particulate, latent active enzyme form 40fold to homogeneity by phase partitioning in Triton X-114 followed by anion exchange and hydrophobic interaction chromatography, and gel filtration Rhaphiolepis bibas

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.10.3.1 fruit
-
Rhaphiolepis bibas
-

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 18.7
-
partially purified soluble, active enzyme form, substrate tert-butyl-catechol Rhaphiolepis bibas
1.10.3.1 91.5
-
purified particulate, latent enzyme form, substrate tert-butyl-catechol Rhaphiolepis bibas

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.1 4-methylcatechol + O2
-
Rhaphiolepis bibas 4-methyl-1,2-benzoquinone + H2O
-
?
1.10.3.1 caffeic acid + O2
-
Rhaphiolepis bibas ?
-
?
1.10.3.1 catechol + 1/2 O2
-
Rhaphiolepis bibas 1,2-benzoquinone + H2O
-
?
1.10.3.1 chlorogenic acid + O2 preferred substrate, 50fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme Rhaphiolepis bibas ?
-
?
1.10.3.1 DL-isoproterenol + O2 the L-isomer is preferred Rhaphiolepis bibas ?
-
?
1.10.3.1 dopamine + O2
-
Rhaphiolepis bibas ?
-
?
1.10.3.1 epicatechin + O2
-
Rhaphiolepis bibas ?
-
?
1.10.3.1 L-dopa + 1/2 O2 i.e. L-3,4-dihydroxyphenylalanine Rhaphiolepis bibas L-dopaquinone + H2O
-
?
1.10.3.1 additional information substrate specificity of the soluble and particulate enzyme forms, overview Rhaphiolepis bibas ?
-
?
1.10.3.1 protocatechuic acid + O2
-
Rhaphiolepis bibas ?
-
?
1.10.3.1 pyrocatechol + O2
-
Rhaphiolepis bibas ?
-
?
1.10.3.1 tert-butyl-catechol + O2 2fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme Rhaphiolepis bibas ?
-
?

Subunits

EC Number Subunits Comment Organism
1.10.3.1 monomer 1 x 59200, particulate, latent enzyme form, SDS-PAGE Rhaphiolepis bibas

Synonyms

EC Number Synonyms Comment Organism
1.10.3.1 polyphenol oxidase
-
Rhaphiolepis bibas
1.10.3.1 PPO
-
Rhaphiolepis bibas

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.1 30 35 soluble, active enzyme form Rhaphiolepis bibas
1.10.3.1 70
-
particulate, latent enzyme form Rhaphiolepis bibas

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.10.3.1 30 70 70% of maximal activity within at 30-60°C, particulate, latent enzyme form Rhaphiolepis bibas

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.1 4 6 dependent on conditions, overview Rhaphiolepis bibas

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.10.3.1 additional information
-
pH profile, overview Rhaphiolepis bibas