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Literature summary extracted from

  • Singh, S.; Singh, D.; Kumar, S.
    Expression and biochemical analysis of codon-optimized polyphenol oxidase from Camellia sinensis (L.) O. Kuntze in E. coli (2016), Process Biochem., 59, 180-186 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.18.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.18.1 additional information
-
additional information enzyme kinetic analysis at different pH values, overview Camellia sinensis
1.14.18.1 0.314
-
epicatechin pH and temperature not specified in the publication Camellia sinensis
1.14.18.1 0.479
-
catechin pH and temperature not specified in the publication Camellia sinensis
1.14.18.1 3.1
-
catechol pH and temperature not specified in the publication Camellia sinensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.1 Cu2+ a copper-containing enzyme, copper content of 0.880 atom/molecule of protein in recombinant refolded enzyme Camellia sinensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.18.1 2 catechol + O2 Camellia sinensis
-
2 1,2-benzoquinone + 2 H2O
-
?
1.14.18.1 catechin + O2 Camellia sinensis
-
? + 2 H2O
-
?
1.14.18.1 epicatechin + O2 Camellia sinensis
-
? + 2 H2O
-
?
1.14.18.1 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

EC Number Organism UniProt Comment Textmining
1.14.18.1 Camellia sinensis C0L3S4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.18.1 recombinant refolded enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Camellia sinensis

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.14.18.1 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

EC Number Source Tissue Comment Organism Textmining
1.14.18.1 leaf
-
Camellia sinensis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.1 2 catechol + O2
-
Camellia sinensis 2 1,2-benzoquinone + 2 H2O
-
?
1.14.18.1 catechin + O2
-
Camellia sinensis ? + 2 H2O
-
?
1.14.18.1 epicatechin + O2
-
Camellia sinensis ? + 2 H2O
-
?
1.14.18.1 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

EC Number Synonyms Comment Organism
1.14.18.1 CsPPO
-
Camellia sinensis
1.14.18.1 polyphenol oxidase
-
Camellia sinensis
1.14.18.1 PPO
-
Camellia sinensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.18.1 5
-
recombinant refolded enzyme Camellia sinensis