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 |
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 |
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 | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.10.3.1 | Cu2+ | active site binding | Rhaphiolepis bibas |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.10.3.1 | 61200 | - |
particulate, latent enzyme form, gel filtration | Rhaphiolepis bibas |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.10.3.1 | Rhaphiolepis bibas | - |
cv. Algerie | - |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.10.3.1 | fruit | - |
Rhaphiolepis bibas | - |
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 |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.10.3.1 | monomer | 1 x 59200, particulate, latent enzyme form, SDS-PAGE | Rhaphiolepis bibas |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.10.3.1 | polyphenol oxidase | - |
Rhaphiolepis bibas |
1.10.3.1 | PPO | - |
Rhaphiolepis bibas |
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 |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.10.3.1 | 4 | 6 | dependent on conditions, overview | Rhaphiolepis bibas |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.10.3.1 | additional information | - |
pH profile, overview | Rhaphiolepis bibas |