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Literature summary for 1.14.18.1 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
Search for more literature for 1.14.18.1

Cloned(Commentary)

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 [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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Camellia sinensis C0L3S4
-
-

Purification (Commentary)

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

Renatured (Commentary)

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

Source Tissue Comment Organism Textmining
leaf
-
 Camellia sinensis
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
CsPPO
-
 Camellia sinensis
polyphenol oxidase
-
 Camellia sinensis
PPO
-
 Camellia sinensis

pH Optimum

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