Cloned (Comment) | Organism |
---|---|
recombinant expression of codon-optimized CsPPO in Escherichia coli strain BL21(DE3), ectopic expression leads to the formation of inclusion bodies | Camellia sinensis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | enzyme kinetic analysis at different pH values, overview | Camellia sinensis | |
0.314 | - |
epicatechin | pH and temperature not specified in the publication | Camellia sinensis | |
0.479 | - |
catechin | pH and temperature not specified in the publication | Camellia sinensis | |
3.1 | - |
catechol | pH and temperature not specified in the publication | Camellia sinensis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | a copper-containing enzyme, copper content of 0.880 atom/molecule of protein in recombinant refolded enzyme | Camellia sinensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 catechol + O2 | Camellia sinensis | - |
2 1,2-benzoquinone + 2 H2O | - |
? | |
catechin + O2 | Camellia sinensis | - |
? + 2 H2O | - |
? | |
epicatechin + O2 | Camellia sinensis | - |
? + 2 H2O | - |
? | |
additional information | Camellia sinensis | polyphenol oxidases (PPOs) are nuclear-encoded copper-containing metalloproteins involved in either the hydroxylation of monophenols to o-diphenols (EC 1.14.18.1, monophenol monoxinase, tyrosinase, and cresolase) or dehydrogenation of o-diphenols to o-quinones (EC1.10.3.1, diphenol oxygen oxidoreductase and catecholase). The enzyme from Camellia sinensis oxidizes epicatechins to yield theaflavins and thearubigins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Camellia sinensis | C0L3S4 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant refolded enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Camellia sinensis |
Renatured (Comment) | Organism |
---|---|
recombinant enzyme from inclusion bodies, extensive standardization of buffers and methods of refolding such as 1. dialysis, 2. on-column refolding, and 3. rapid dilution yield active PPO from solubilized inclusion bodies with copper content of 0.880 atom/molecule of protein, method development, detailed overview | Camellia sinensis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Camellia sinensis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 catechol + O2 | - |
Camellia sinensis | 2 1,2-benzoquinone + 2 H2O | - |
? | |
catechin + O2 | - |
Camellia sinensis | ? + 2 H2O | - |
? | |
epicatechin + O2 | - |
Camellia sinensis | ? + 2 H2O | - |
? | |
additional information | polyphenol oxidases (PPOs) are nuclear-encoded copper-containing metalloproteins involved in either the hydroxylation of monophenols to o-diphenols (EC 1.14.18.1, monophenol monoxinase, tyrosinase, and cresolase) or dehydrogenation of o-diphenols to o-quinones (EC1.10.3.1, diphenol oxygen oxidoreductase and catecholase). The enzyme from Camellia sinensis oxidizes epicatechins to yield theaflavins and thearubigins | Camellia sinensis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CsPPO | - |
Camellia sinensis |
polyphenol oxidase | - |
Camellia sinensis |
PPO | - |
Camellia sinensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
recombinant refolded enzyme | Camellia sinensis |