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Literature summary for 1.21.3.6 extracted from

  • Sullivan, M.
    Beyond brown polyphenol oxidases as enzymes of plant specialized metabolism (2015), Front. Plant Sci., 5, 1-7 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene AS1, DNA and amino acid sequence determination and analyis Antirrhinum majus

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuole
-
Antirrhinum majus 5773
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a copper-containing enzyme Neurospora crassa
Cu2+ a copper-containing enzyme Antirrhinum majus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 2',3,4,4',6'-pentahydroxychalcone + O2 Antirrhinum majus
-
bracteatin + 2 H2O
-
?
2',4',6',4-tetrahydroxychalcone + O2 Neurospora crassa
-
aureusidin + H2O
-
?
2',4',6',4-tetrahydroxychalcone + O2 Antirrhinum majus
-
aureusidin + H2O
-
?
additional information Antirrhinum majus substrate specificity allows elucidation of a likely mechanism of aurone formation from 2,4,6,4-tetrahydroxychalcone or PHC involving both tyrosinase and catechol oxidase activities of the Antirrhinum majus PPO, pathway overview. Starting with THC, tyrosinase and catechol oxidase activity, EC 1.14.18.1, result in 3-hydroxylation and formation of the corresponding o-quinone. Whether aureusidine synthase PPO carries out the 3-hydroxylation reaction in vivo, or whether a cytochrome P450 chalcone 3-hydroxylase is also involved is not definitively established. Aureusidine synthase likely forms the same quinone from 2',3,4,4',6'-pentahydroxychalcone without the need for the 3-hydroxylation step. The resulting quinone is predicted to undergo a 2-step non-enzyme mediated rearrangement to form aureusidin ?
-
?

Organism

Organism UniProt Comment Textmining
Antirrhinum majus Q9FRX6
-
-
Neurospora crassa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity from yellow snapdragon flower buds Antirrhinum majus

Source Tissue

Source Tissue Comment Organism Textmining
flower
-
Antirrhinum majus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 2',3,4,4',6'-pentahydroxychalcone + O2
-
Antirrhinum majus bracteatin + 2 H2O
-
?
2',4',6',4-tetrahydroxychalcone + O2
-
Neurospora crassa aureusidin + H2O
-
?
2',4',6',4-tetrahydroxychalcone + O2
-
Antirrhinum majus aureusidin + H2O
-
?
additional information substrate specificity allows elucidation of a likely mechanism of aurone formation from 2,4,6,4-tetrahydroxychalcone or PHC involving both tyrosinase and catechol oxidase activities of the Antirrhinum majus PPO, pathway overview. Starting with THC, tyrosinase and catechol oxidase activity, EC 1.14.18.1, result in 3-hydroxylation and formation of the corresponding o-quinone. Whether aureusidine synthase PPO carries out the 3-hydroxylation reaction in vivo, or whether a cytochrome P450 chalcone 3-hydroxylase is also involved is not definitively established. Aureusidine synthase likely forms the same quinone from 2',3,4,4',6'-pentahydroxychalcone without the need for the 3-hydroxylation step. The resulting quinone is predicted to undergo a 2-step non-enzyme mediated rearrangement to form aureusidin Antirrhinum majus ?
-
?

Synonyms

Synonyms Comment Organism
AS1
-
Antirrhinum majus
aureusidin synthase
-
Neurospora crassa
aureusidin synthase
-
Antirrhinum majus
aurone synthase
-
Antirrhinum majus
More cf. EC 1.14.18.1 Neurospora crassa
More cf. EC 1.14.18.1 Antirrhinum majus

General Information

General Information Comment Organism
metabolism substrate specificity allows elucidation of a likely mechanism of aurone formation from 2,4,6,4-tetrahydroxychalcone or PHC involving both tyrosinase and catechol oxidase activities of the Antirrhinum majus PPO, pathway overview. Starting with THC, tyrosinase and catechol oxidase activity, EC 1.14.18.1, result in 3-hydroxylation and formation of the corresponding o-quinone. Whether aureusidine synthase PPO carries out the 3-hydroxylation reaction in vivo, or whether a cytochrome P450 chalcone 3-hydroxylase is also involved is not definitively established. Aureusidine synthase likely forms the same quinone from 2',3,4,4',6'-pentahydroxychalcone without the need for the 3-hydroxylation step. The resulting quinone is predicted to undergo a 2-step non-enzyme mediated rearrangement to form aureusidine Antirrhinum majus
physiological function PPOs have a role in postharvest browning, secondary reactions of PPO-generated o-quinones with cellular nucleophiles leading to the familiar discoloration of fresh products and plant materials. Aurones (aureusidin and bracteatin) are formed from 2,4,6,4-tetrahydroxychalcone or 2,4,6,3,4-pentahydroxychalcone upon incubation with extracts of yellow snapdragon flowers through activity of aureusidin (or aurone) synthase Antirrhinum majus