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2 2',3,4,4',6'-pentahydroxychalcone + O2
bracteatin + 2 H2O
Substrates: -
Products: -
?
2',3,4,4',6'-pentahydroxychalcone + 1/2 O2
aureusidin + bracteatin + H2O
-
Substrates: -
Products: -
ir
2',3,4,4',6'-pentahydroxychalcone + O2
aureusidin + bracteatin + H2O
2',3,4,4',6'-pentahydroxychalcone 4'-beta-D-glucopyranoside + O2
aureusidin 6-beta-D-glucopyranoside + bracteatin 6-beta-D-glucopyranoside + H2O
2',4',6',4-tetrahydroxychalcone + O2
aureusidin + H2O
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
2',4,4',6'-tetrahydroxychalcone 4'-beta-D-glucopyranoside + O2
aureusidin 6-beta-D-glucopyranoside + H2O
-
Substrates: -
Products: -
ir
butein + O2
sulfuretin + 3',4',5',6-tetrahydroxyaurone + H2O
-
Substrates: -
Products: products are formed in a 23:1 ratio
ir
isoliquiritigenin + O2
sulfuretin + H2O
-
Substrates: -
Products: -
ir
additional information
?
-
2',3,4,4',6'-pentahydroxychalcone + O2
aureusidin + bracteatin + H2O
-
Substrates: -
Products: products are formed in a 6:1 ratio
ir
2',3,4,4',6'-pentahydroxychalcone + O2
aureusidin + bracteatin + H2O
-
Substrates: best substrate
Products: products are formed in a 6:1 ratio
ir
2',3,4,4',6'-pentahydroxychalcone + O2
aureusidin + bracteatin + H2O
-
Substrates: 2210% activity compared to 2',4,4',6'-tetrahydroxychalcone
Products: products are formed in a 6:1 ratio
ir
2',3,4,4',6'-pentahydroxychalcone + O2
aureusidin + bracteatin + H2O
-
Substrates: 2-6fold higher activity than with 2',4,4',6'-tetrahydroxychalcone
Products: products are formed in a 6:1 ratio
ir
2',3,4,4',6'-pentahydroxychalcone 4'-beta-D-glucopyranoside + O2
aureusidin 6-beta-D-glucopyranoside + bracteatin 6-beta-D-glucopyranoside + H2O
-
Substrates: -
Products: -
ir
2',3,4,4',6'-pentahydroxychalcone 4'-beta-D-glucopyranoside + O2
aureusidin 6-beta-D-glucopyranoside + bracteatin 6-beta-D-glucopyranoside + H2O
-
Substrates: -
Products: products are formed in a 5:1 ratio
ir
2',3,4,4',6'-pentahydroxychalcone 4'-beta-D-glucopyranoside + O2
aureusidin 6-beta-D-glucopyranoside + bracteatin 6-beta-D-glucopyranoside + H2O
-
Substrates: -
Products: products provide the yellow colour of flowers
ir
2',4',6',4-tetrahydroxychalcone + O2
aureusidin + H2O
Substrates: -
Products: -
?
2',4',6',4-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: -
Products: -
?
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: -
Products: -
ir
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: no formation of 2-(alpha-hydroxybenzyl)coumaranone intermediate
Products: -
ir
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: key intermediate in the general flonoid metabolism
Products: -
ir
additional information
?
-
-
Substrates: no activity with L-tyrosine, L-DOPA, 4-coumaric acid, caffeic acid, naringenin, eriodictyol, 4,4',6'-trihydroxyaurone, and aureusidin
Products: -
?
additional information
?
-
-
Substrates: absolutely specific for chalcones
Products: -
?
additional information
?
-
-
Substrates: no activity with 2'-hydroxychalcone, 4-hydroxychalcone, 2',3,4,4',6'-pentahydroxychalcone 3-glucoside, and 2',6'-dihydroxy-4,4'-dimethoxychalcone
Products: -
?
additional information
?
-
-
Substrates: enzyme shows no 3',4'-dehydrogenase activity towards aureusidin
Products: -
?
additional information
?
-
-
Substrates: enzyme shows no 3',4'-dehydrogenase activity towards aureusidin
Products: -
?
additional information
?
-
-
Substrates: pathway, overview
Products: -
?
additional information
?
-
-
Substrates: chalcone-specific polyphenol oxidase specialized for aurone biosynthesis
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a key role in the yellow coloration of flowers, enzyme is a homologue of plant polyphenol oxidase
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a key role in the yellow coloration of flowers, enzyme is a homologue of plant polyphenol oxidase
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a key role in the yellow coloration of flowers, enzyme is a homologue of plant polyphenol oxidase
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
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2 2',3,4,4',6'-pentahydroxychalcone + O2
bracteatin + 2 H2O
Substrates: -
Products: -
?
2',3,4,4',6'-pentahydroxychalcone + 1/2 O2
aureusidin + bracteatin + H2O
-
Substrates: -
Products: -
ir
2',4',6',4-tetrahydroxychalcone + O2
aureusidin + H2O
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
additional information
?
-
2',4',6',4-tetrahydroxychalcone + O2
aureusidin + H2O
Substrates: -
Products: -
?
2',4',6',4-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: -
Products: -
?
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: -
Products: -
ir
2',4,4',6'-tetrahydroxychalcone + O2
aureusidin + H2O
-
Substrates: key intermediate in the general flonoid metabolism
Products: -
ir
additional information
?
-
-
Substrates: pathway, overview
Products: -
?
additional information
?
-
-
Substrates: chalcone-specific polyphenol oxidase specialized for aurone biosynthesis
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a key role in the yellow coloration of flowers, enzyme is a homologue of plant polyphenol oxidase
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a key role in the yellow coloration of flowers, enzyme is a homologue of plant polyphenol oxidase
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a key role in the yellow coloration of flowers, enzyme is a homologue of plant polyphenol oxidase
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
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Nakayama, T.; Yonekura-Sakakibara, K.; Sato, T.; Kikuchi, S.; Fukui, Y.; Fukuchi-Mizutani, M.; Ueda, T.; Nakao, M.; Tanaka, Y.; Kusumi, T.; Nishino, T.
Aureusidin synthase: a polyphenol oxidase homolog responsible for flower coloration
Science
290
1163-1166
2000
Antirrhinum majus
brenda
Nakayama, T.; Sato, T.; Fukui, Y.; Yonekura-Sakakibara, K.; Hayashi, H.; Tanaka, Y.; Kusumi, T.; Nishino, T.
Specificity analysis and mechanism of aurone synthesis catalyzed by aureusidin synthase, a polyphenol oxidase homolog responsible for flower coloration
FEBS Lett.
499
107-111
2001
Antirrhinum majus
brenda
Sato, T.; Nakayama, T.; Kikuchi, S.; Fukui, Y.; Yonekura-Sakakibara, K.; Ueda, T.; Nishino, T.; Tanaka, Y.; Kusumi, T.
Enzymatic formation of aurones in the extracts of yellow snapdragon flowers
Plant Sci.
160
229-236
2001
Antirrhinum majus
brenda
Davies, K.M.; Marshall, G.B.; Bradley, J.M.; Schwinn, K.E.; Bloor, S.J.; Winefield, C.S.; Martin, C.R.
Characterisation of aurone biosynthesis in Antirrhinum majus
Physiol. Plant.
128
593-603
2006
Antirrhinum majus
brenda
Ono, E.; Hatayama, M.; Isono, Y.; Sato, T.; Watanabe, R.; Yonekura-Sakakibara, K.; Fukuchi-Mizutani, M.; Tanaka, Y.; Kusumi, T.; Nishino, T.; Nakayama, T.
Localization of a flavonoid biosynthetic polyphenol oxidase in vacuoles
Plant J.
45
133-143
2006
Antirrhinum majus
brenda
Ono, E.; Fukuchi-Mizutani, M.; Nakamura, N.; Fukui, Y.; Yonekura-Sakakibara, K.; Yamaguchi, M.; Nakayama, T.; Tanaka, T.; Kusumi, T.; Tanaka, Y.
Yellow flowers generated by expression of the aurone biosynthetic pathway
Proc. Natl. Acad. Sci. USA
103
11075-11080
2006
Antirrhinum majus
brenda
Shakya, R.; Ye, J.; Rommens, C.M.
Altered leaf colour is associated with increased superoxide-scavenging activity in aureusidin-producing transgenic plants
Plant Biotechnol. J.
10
1046-1055
2012
Antirrhinum majus (Q9FRX6), Antirrhinum majus
brenda
Elumalai, P.; Liu, H.L.
Homology modeling and dynamics study of aureusidin synthase--an important enzyme in aurone biosynthesis of snapdragon flower
Int. J. Biol. Macromol.
49
134-142
2011
Antirrhinum majus (Q9FRX6), Antirrhinum majus
brenda
Sullivan, M.
Beyond brown polyphenol oxidases as enzymes of plant specialized metabolism
Front. Plant Sci.
5
1-7
2015
Antirrhinum majus (Q9FRX6), Neurospora crassa
brenda