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Literature summary for 1.10.3.1 extracted from
- 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.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | - |
Rhaphiolepis bibas |  |
| ascorbate | - |
Rhaphiolepis bibas | |
| DTT | - |
Rhaphiolepis bibas | |
| glutathione | - |
Rhaphiolepis bibas | |
| L-cysteine | - |
Rhaphiolepis bibas | |
| additional information | sensitivity to inhibitors of the soluble and particulate enzyme forms, overview | Rhaphiolepis bibas | |
| NaCl | - |
Rhaphiolepis bibas | |
| NaF | - |
Rhaphiolepis bibas | |
| Sodium diethyl dithiocarbamate | - |
Rhaphiolepis bibas | |
| sodium disulfite | - |
Rhaphiolepis bibas | |
| Thiourea | - |
Rhaphiolepis bibas | |
| tropolone | - |
Rhaphiolepis bibas | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | temperature and pH dependencis of the two enzyme forms, in absence or presence of SDS | Rhaphiolepis bibas | |
| 1 | - |
chlorogenic acid | pH 4.5, 25°C, soluble, active enzyme form | Rhaphiolepis bibas | |
| 1.2 | - |
tert-butyl-catechol | pH 4.5, 25°C, soluble, active enzyme form | Rhaphiolepis bibas | |
| 1.23 | - |
tert-butyl-catechol | pH 4.5, 25°C, particulate, latent enzyme form | Rhaphiolepis bibas | |
| 5.7 | - |
chlorogenic acid | pH 4.5, 25°C, particulate, latent enzyme form | Rhaphiolepis bibas | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| particle-bound | 80% of total activity | Rhaphiolepis bibas | - |
- |
| soluble | 20% of total activity | Rhaphiolepis bibas | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | active site binding | Rhaphiolepis bibas | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 61200 | - |
particulate, latent enzyme form, gel filtration | Rhaphiolepis bibas |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhaphiolepis bibas | - |
cv. Algerie | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fruit | - |
Rhaphiolepis bibas | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 18.7 | - |
partially purified soluble, active enzyme form, substrate tert-butyl-catechol | Rhaphiolepis bibas |
| 91.5 | - |
purified particulate, latent enzyme form, substrate tert-butyl-catechol | Rhaphiolepis bibas |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-methylcatechol + O2 | - |
Rhaphiolepis bibas | 4-methyl-1,2-benzoquinone + H2O | - |
? | |
| caffeic acid + O2 | - |
Rhaphiolepis bibas | ? | - |
? | |
| catechol + 1/2 O2 | - |
Rhaphiolepis bibas | 1,2-benzoquinone + H2O | - |
? | |
| chlorogenic acid + O2 | preferred substrate, 50fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme | Rhaphiolepis bibas | ? | - |
? | |
| DL-isoproterenol + O2 | the L-isomer is preferred | Rhaphiolepis bibas | ? | - |
? | |
| dopamine + O2 | - |
Rhaphiolepis bibas | ? | - |
? | |
| epicatechin + O2 | - |
Rhaphiolepis bibas | ? | - |
? | |
| L-dopa + 1/2 O2 | i.e. L-3,4-dihydroxyphenylalanine | Rhaphiolepis bibas | L-dopaquinone + H2O | - |
? | |
| additional information | substrate specificity of the soluble and particulate enzyme forms, overview | Rhaphiolepis bibas | ? | - |
? | |
| protocatechuic acid + O2 | - |
Rhaphiolepis bibas | ? | - |
? | |
| pyrocatechol + O2 | - |
Rhaphiolepis bibas | ? | - |
? | |
| tert-butyl-catechol + O2 | 2fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme | Rhaphiolepis bibas | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 x 59200, particulate, latent enzyme form, SDS-PAGE | Rhaphiolepis bibas |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| polyphenol oxidase | - |
Rhaphiolepis bibas |
| PPO | - |
Rhaphiolepis bibas |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 35 | soluble, active enzyme form | Rhaphiolepis bibas |
| 70 | - |
particulate, latent enzyme form | Rhaphiolepis bibas |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 70 | 70% of maximal activity within at 30-60°C, particulate, latent enzyme form | Rhaphiolepis bibas |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 6 | dependent on conditions, overview | Rhaphiolepis bibas |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
pH profile, overview | Rhaphiolepis bibas |
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