Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.18.1 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
Search for more literature for 1.14.18.1

Cloned(Commentary)

Cloned (Comment) Organism
gene AS1, DNA and amino acid sequence determination and analyis Antirrhinum majus
gene AS1, DNA and amino acid sequence determination and analyis Coreopsis grandiflora
gene PPO, DNA and amino acid sequence determination and analyis Larrea tridentata
single gene Juglans regia

Protein Variants

Protein Variants Comment Organism
additional information generation of several PPO-silenced RNAi transgenic lines that show over 95% reduction in catechol oxidase activity relative to wild-type controls, the plants develop a phenotype with disease-like necrotic lesions. Levels of salicylic acid, H2O2, or malondialdehyde are not significantly different in the PPO-silenced leaves compared to wild-type leaves. Metabolomic analysis of PPO-silenced and wild-type leaves reveal significant differences in many metabolites, particularly phenylpropanoids, and about 10fold increased levels of tyramine. Although L-DOPA is undetectable in both PPO-silenced and wild-type walnut plants, levels of dopamine (derived from either L-DOPA or tyramine) and 5,6 dihydroxyindole (derived from L-DOPA) are reduced approximately 6 and 100fold, respectively, in PPO-silenced plants relative to wild-type controls Juglans regia

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Beta vulgaris 9507
-
chloroplast
-
 Juglans regia 9507
-
chloroplast
-
 Coreopsis grandiflora 9507
-
chloroplast Larrea tridentata PPO contains N-terminal sequences predicting its localization to the chloroplast thylakoid lumen Larrea tridentata 9507
-
thylakoid
-
 Larrea tridentata 9579
-
vacuole
-
 Antirrhinum majus 5773
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a copper-containing enzyme Beta vulgaris
Cu2+ a copper-containing enzyme Juglans regia
Cu2+ a copper-containing enzyme Larrea tridentata
Cu2+ a copper-containing enzyme Antirrhinum majus
Cu2+ a copper-containing enzyme Coreopsis grandiflora

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 Coreopsis grandiflora
-
 bracteatin + 2 H2O
-
 ?
2 L-dopa + O2 Beta vulgaris
-
 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2 Juglans regia
-
 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2 Larrea tridentata
-
 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2 Antirrhinum majus
-
 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2 Coreopsis grandiflora
-
 2 dopaquinone + 2 H2O
-
 ?
2',4',6',4-tetrahydroxychalcone + O2 Coreopsis grandiflora
-
 aureusidin + H2O
-
 ?
L-tyrosine + O2 Beta vulgaris
-
 dopaquinone + H2O
-
 ?
L-tyrosine + O2 Juglans regia
-
 dopaquinone + H2O
-
 ?
L-tyrosine + O2 Larrea tridentata
-
 dopaquinone + H2O
-
 ?
L-tyrosine + O2 Antirrhinum majus
-
 dopaquinone + H2O
-
 ?
L-tyrosine + O2 Coreopsis grandiflora
-
 dopaquinone + H2O
-
 ?
additional information Juglans regia In Juglans regia, PPO is encoded by a single gene and has both catechol oxidase activity (oxidation of o-diphenols to their corresponding o-quinones, EC 1.10.3.1) and tyrosinase activity (hydroxylation of monophenols to o-diphenols, EC 1.14.18.1) ?
-
 ?
additional information Larrea tridentata in Juglans regia, PPO is encoded by a single gene and has both catechol oxidase activity (oxidation of o-diphenols to their corresponding o-quinones, EC 1.10.3.1) and tyrosinase activity (hydroxylation of monophenols to o-diphenols, EC 1.14.18.1). The Larrea tridentate PPO gene product acts as a (+)-larreatricin 3'-hydroxylase in vivo ?
-
 ?
additional information Beta vulgaris most plant polphenol oxidases have catechol oxidase activity (oxidation of o-diphenols to their corresponding o-quinones, EC1.10.3.1) and the ability to hydroxylate monophenols to o-diphenols (tyrosinase, EC 1.14.18.1) ?
-
 ?
additional information Coreopsis grandiflora 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 result in 3-hydroxylation and formation of the corresponding o-quinone. Besides aurone synthase PPO, a cytochrome P450 chalcone 3-hydroxylase is also involved in the 3-hydroxylation step ?
-
 ?
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 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, EC 1.21.3.6, 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
-
-
Beta vulgaris
-
-
-
Coreopsis grandiflora A0A075BX21
-
-
Juglans regia
-
-
-
Larrea tridentata Q6UIL3
-
-
no activity in Arabidopsis thaliana
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
flower
-
 Antirrhinum majus
-
leaf
-
 Juglans regia
-
root
-
 Beta vulgaris
-
tuber
-
 Beta vulgaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 2',3,4,4',6'-pentahydroxychalcone + O2
-
 Coreopsis grandiflora bracteatin + 2 H2O
-
 ?
2 L-dopa + O2
-
 Beta vulgaris 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2
-
 Juglans regia 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2
-
 Larrea tridentata 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2
-
 Antirrhinum majus 2 dopaquinone + 2 H2O
-
 ?
2 L-dopa + O2
-
 Coreopsis grandiflora 2 dopaquinone + 2 H2O
-
 ?
2',4',6',4-tetrahydroxychalcone + O2
-
 Coreopsis grandiflora aureusidin + H2O
-
 ?
3'-hydroxy-larreatricin + O2 3-hydroxylation Larrea tridentata 3,3'-dihydroxylarreatricin
-
 ?
3-hydroxy-larreatricin + O2 3'-hydroxylation Larrea tridentata 3,3'-dihydroxylarreatricin
-
 ?
L-tyrosine + O2
-
 Beta vulgaris dopaquinone + H2O
-
 ?
L-tyrosine + O2
-
 Juglans regia dopaquinone + H2O
-
 ?
L-tyrosine + O2
-
 Larrea tridentata dopaquinone + H2O
-
 ?
L-tyrosine + O2
-
 Antirrhinum majus dopaquinone + H2O
-
 ?
L-tyrosine + O2
-
 Coreopsis grandiflora dopaquinone + H2O
-
 ?
larreatricin + O2 3'-hydroxylation Larrea tridentata 3'-hydroxy-larreatricin
-
 ?
larreatricin + O2 3-hydroxylation Larrea tridentata 3-hydroxy-larreatricin
-
 ?
additional information In Juglans regia, PPO is encoded by a single gene and has both catechol oxidase activity (oxidation of o-diphenols to their corresponding o-quinones, EC 1.10.3.1) and tyrosinase activity (hydroxylation of monophenols to o-diphenols, EC 1.14.18.1) Juglans regia ?
-
 ?
additional information in Juglans regia, PPO is encoded by a single gene and has both catechol oxidase activity (oxidation of o-diphenols to their corresponding o-quinones, EC 1.10.3.1) and tyrosinase activity (hydroxylation of monophenols to o-diphenols, EC 1.14.18.1). The Larrea tridentate PPO gene product acts as a (+)-larreatricin 3'-hydroxylase in vivo Larrea tridentata ?
-
 ?
additional information most plant polphenol oxidases have catechol oxidase activity (oxidation of o-diphenols to their corresponding o-quinones, EC1.10.3.1) and the ability to hydroxylate monophenols to o-diphenols (tyrosinase, EC 1.14.18.1) Beta vulgaris ?
-
 ?
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 result in 3-hydroxylation and formation of the corresponding o-quinone. Besides aurone synthase PPO, a cytochrome P450 chalcone 3-hydroxylase is also involved in the 3-hydroxylation step Coreopsis grandiflora ?
-
 ?
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 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, EC 1.21.3.6, 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 ?
-
 ?
additional information the purified lenzyme also shows highly enantiospecific larreatricin-3'-hydroxylase activity, EC 1.14.99.47 Larrea tridentata ?
-
 ?

Synonyms

Synonyms Comment Organism
aurone synthase
-
 Coreopsis grandiflora
catechol oxidase
-
 Beta vulgaris
catechol oxidase
-
 Juglans regia
catechol oxidase
-
 Larrea tridentata
catechol oxidase
-
 Antirrhinum majus
catechol oxidase
-
 Coreopsis grandiflora
More cf. EC 1.21.3.6 Antirrhinum majus
polyphenol oxidase
-
 Beta vulgaris
polyphenol oxidase
-
 Juglans regia
polyphenol oxidase
-
 Larrea tridentata
polyphenol oxidase
-
 Antirrhinum majus
polyphenol oxidase
-
 Coreopsis grandiflora
tyrosinase
-
 Beta vulgaris
tyrosinase
-
 Juglans regia
tyrosinase
-
 Larrea tridentata
tyrosinase
-
 Antirrhinum majus
tyrosinase
-
 Coreopsis grandiflora

General Information

General Information Comment Organism
malfunction with 95% reduction in catechol oxidase activity relative to wild-type controls, the plants develop a phenotype with disease-like necrotic lesions. Levels of salicylic acid, H2O2, or malondialdehyde are not significantly different in the PPO-silenced leaves compared to wild-type leaves. Metabolomic analysis of PPO-silenced and wild-type leaves reveal significant differences in many metabolites, particularly phenylpropanoids, and about 10fold increased levels of tyramine. Although L-DOPA is undetectable in both PPO-silenced and wild-type walnut plants, levels of dopamine (derived from either L-DOPA or tyramine) and 5,6 dihydroxyindole (derived from L-DOPA) are reduced approximately 6 and 100fold, respectively, in PPO-silenced plants relative to wild-type controls Juglans regia
metabolism PPO-mediated conversion of tyrosine to L-DOPA, tyrosine metabolism in walnut, pathway overview Juglans regia
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 result in 3-hydroxylation and formation of the corresponding o-quinone. Besides aurone synthase PPO, a cytochrome P450 chalcone 3-hydroxylase is also involved in the 3-hydroxylation step Coreopsis grandiflora
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 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, EC 1.21.3.6, 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
metabolism the enzyme is involved in the first step in betalain biosynthesis, the conversion of tyrosine into L-DOP, i.e. L-3,4-dihydroxyphenylalanine. The resulting L-DOPA can be a substrate for DOPA 4,5-dioxygenase (DODA) that cleaves the aromatic ring to form 4,5-seco-DOPA. The cleavage product spontaneously rearranges to form betalamic acid, which can condense with amino acids or other amine groups to form yellow betaxanthins. Condensation of betalamic acid with cyclo-DOPA forms the red betacyanin pigments. The catechol oxidase activity of PPO is involved in the oxidation of DOPA to DOPA quinone that can spontaneously rearrange to form the cyclo-DOPA moiety of the red betacyanin betalains, pathway overview Beta vulgaris
metabolism the tyrosinase activity of PPO is involved in biosynthesis of 8-8'-linked lignans, e.g. nordihydroguaiaretic acid (NDGA), in creosote bush, pathway overview Larrea tridentata
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 Beta vulgaris
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 Juglans regia
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 Larrea tridentata
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, EC 1.21.3.6 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. Coreopsis grandiflora