Information on EC 1.14.11.19 - anthocyanidin synthase

for references in articles please use BRENDA:EC1.14.11.19
Word Map on EC 1.14.11.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.19
-
RECOMMENDED NAME
GeneOntology No.
anthocyanidin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = a (4S)- 2,3-dehydroflavan-3,4-diol + succinate + CO2 + H2O
show the reaction diagram
(1a)
-
-
-
a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O
show the reaction diagram
a (4S)- 2,3-dehydroflavan-3,4-diol = an anthocyanidin + H2O
show the reaction diagram
(1b)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anthocyanin biosynthesis
-
-
anthocyanin biosynthesis (pelargonidin 3-O-glucoside)
-
-
proanthocyanidins biosynthesis from flavanols
-
-
SYSTEMATIC NAME
IUBMB Comments
(2R,3S,4S)-leucoanthocyanidin,2-oxoglutarate:oxygen oxidoreductase
The enzyme requires Fe(II) and ascorbate. It is involved in the pathway by which many flowering plants make anthocyanin flower pigments (glycosylated anthocyandins). The enzyme hydroxylates the C-3 carbon, followed by a trans diaxial elimination, forming a C-2,C-3 enol. The product loses a second water molecule to form anthocyanidins. When assayed in vitro, non-enzymic epimerization of the product can lead to formation of dihydroflavanols. Thus when the substrate is leucocyanidin, a mixture of (+)-taxifolin and (+)-epitaxifolin are formed. The enzyme can also oxidize the formed (+)-taxifolin to quercetin (cf. EC 1.14.11.23, flavonol synthase) [2,3].
CAS REGISTRY NUMBER
COMMENTARY hide
180984-01-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
snapdragon
-
-
Manually annotated by BRENDA team
yellow- and black-seeded accessions, gene BjANS
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Brown Turkey
-
-
Manually annotated by BRENDA team
1 year old seedlings and 12 year old grafts
UniProt
Manually annotated by BRENDA team
Lam cultivar A5, A1, Yamakawamurasaki, and A3 and one of white-fleshed sweet potato cultivar Yubeibai
-
-
Manually annotated by BRENDA team
Pamp.
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
overexpression in rice mutant Nootripathu, which accumulates proanthocyanidins exclusively in pericarp
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
C7S854
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-trans-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + O2
show the reaction diagram
-
-
-
-
?
(2R,3S,4R)-trans-leucocyanidin + 2-oxoglutarate + O2
trans-dihydroquercetin + cis-dihydroquercetin + quercetin + succinate + CO2
show the reaction diagram
-
-
-
-
?
(2R,3S,4S)-cis-leucocyanidin + 2-oxoglutarate + O2
quercetin + succinate + CO2
show the reaction diagram
-
-
-
-
?
2R,3S,4R-trans-leucocyanidin + 2-oxoglutarate + O2
2R,3S-cis-dihydroquercetin + 2R,3R-trans-dihydroquercetin + cyanidin + quercetin
show the reaction diagram
-
-
55% 2R,3S-cis-dihydroquercetin + 11% 2R,3R-trans-dihydroquercetin + 4% cyanidin + 30% quercetin
-
?
2R,3S,4S-cis-leucoanthocyanidin + 2-oxoglutarate + O2
cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
show the reaction diagram
-
catalyses the penultimate step in anthocyanin biosynthesis by oxidation of the 2R,3S,4S-cis-leucoanthocyanidins
both quercetin and dihydroquercetin are products with the distribution being dependent on the C-4 stereochemistry of the leucocyanidin substrates
-
?
2R,3S,4S-cis-leucocyanidin + 2-oxoglutarate + O2
2R,3S-cis-dihydroquercetin + 2R,3R-trans-dihydroquercetin + cyanidin + quercetin
show the reaction diagram
-
-
10% 2R,3S-cis-dihydroquercetin + 2% 2R,3R-trans-dihydroquercetin + 3% cyanidin + 85% quercetin
-
?
3,4-cis-leucocyanidin + 2-oxoglutarate + O2
cyanidin + succinate + CO2
show the reaction diagram
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2
show the reaction diagram
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + O2
show the reaction diagram
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
show the reaction diagram
leucocyanidin + 2-oxoglutarate + O2 + H+
cyanidin + succinate + CO2 + 2 H2O
show the reaction diagram
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2R,3S,4S-cis-leucoanthocyanidin + 2-oxoglutarate + O2
cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
show the reaction diagram
-
catalyses the penultimate step in anthocyanin biosynthesis by oxidation of the 2R,3S,4S-cis-leucoanthocyanidins
both quercetin and dihydroquercetin are products with the distribution being dependent on the C-4 stereochemistry of the leucocyanidin substrates
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
Fe2+ is required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
ascorbate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038
(2R,3S,4R)-leucocyanidin
-
-
0.059
2-oxoglutarate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.18
sequence calculation
5.27
-
calculated from sequence
6.2
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
all lines and seed coats of the black-seeded lines, not in the yellow-seeded seed coats
Manually annotated by BRENDA team
-
exposure of shaded swollen hypocotyls to artificial light sources. Only UV-A light induces anthocyanin biosynthesis. During 24 h of exposure, expression of anthocyanidin synthase increases together with phenylalanine ammonia lyase EC 4.3.1.5, chalcone synthase EC 2.3.1.74, flavanone 3-hydroxylase EC 1.14.11.9, and dihydroflavonol 4-reductase EC 1.1.1.219
Manually annotated by BRENDA team
-
primarily distributed in the growth point and leaf primordium of the leaf buds
Manually annotated by BRENDA team
moderate expression level
Manually annotated by BRENDA team
levels of transcripts encoding anthocyanidin synthase, dihydroflavonol reductase and anthocyanidin reductase parallel the accumulation of proanthocyanidins in developing seeds
Manually annotated by BRENDA team
BjANS expressed in the seed coats of the black-seeded lines and in embryos of the all lines, but not in the yellow-seeded seed coats, RT-PCR expression analysis
Manually annotated by BRENDA team
-
perilla, red or green
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40300
x * 40300, calculated
40450
-
calculated
40862
x * 40862, sequence calculation
41000
x * 41000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
of recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a full-length, 1427-bp long cDNA named RnANS1 (Ribes nigrum anthocyanidin synthase 1), which is homologous to the anthocyanidin synthase gene, is cloned from blackcurrant using a homologous cloning strategy. RnANS1 is highly homologous to other plant ANS genes at both the nucleotide and amino acid sequence levels. The deduced protein contains domains conserved in the 2-oxoglutarate and Fe(II)-dependent oxygenase, and is phylogenetically closely related to Paeonia suffruticosa and Paeonia lactiflora
analysis of expression in wheat-rye hybrids
C7S854
anthocyanin synthase is cloned from Magnolia sprengeri (MsANS) using rapid amplification of complementary DNA ends technology. The full-length MsANS is 1171-bp long and contains a 1080-bp open reading frame encoding a 360 amino acid polypeptide. In a sequence alignment analysis, the deduced MsANS protein showed high identity to ANS proteins from other plants: Prunus salicina var. cordata (74% identity), Ampelopsis grossedentata (74% identity), Pyrus communis (73% identity), and Prunus avium (73% identity)
expressed in Escherichia coli
expressed in Escherichia coli strain DH5alpha
-
expression in Escherichia coli JM109
expression in Escherichia coli, overexpression in rice mutant Nootripathu, which accumulates proanthocyanidins exclusively in pericarp
gene BjANS, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
overexpression in Escherichia coli
the full-length cDNA of Reaumuria trigyna leucoanthocyanidin dioxygenase (RtLDOX) is cloned into the expression vector pET32a and expressed in Escherichia coli Rosetta (DE3). The RtLDOX recombinant protein is able to replace flavanone-3-hydroxylase (EC 1.14.11.9), another dioxygenase in the flavonoid pathway, to convert naringenin to dihydrokaempferol in vitro. the enzyme can complement the Arabidopsis LDOX mutant transparent testa11 (tt11-11), which has reduced proanthocyanin and anthocyanin levels in seeds, to accumulate these two compounds
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a progressive increase in activity of anthocyanidin synthase is observed in purple fruits from 7 to 21 days after anthesis
activity of anthocyanidin synthase in leaves of all genotypes and fruits of green and white colour progressively decreases from 7 to 21 days after anthesis
decrease at stage of flowering
expression is strongly increased under salt stress
FcANS1 expression is responsive to light, as bagging the syconia reduced FcANS1 expression and anthocyanin content in bothfig skin and female flowers compared to natural light conditions
-
FcANS1 expression is significantly upregulated during syconia maturation. Transcript expression of FcANS1 in the fruit peel and female flowers differs between the bagging treatment and the natural lighting controls. FcANS1 transcripts are more abundant in the control samples
-
the expression of RnANS1 (Ribes nigrum anthocyanidin synthase 1) is upregulated during fruit maturation, and correlated with the accumulation of anthocyanins and soluble carbohydrates in the fruit
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G229R
inactive mutant enzyme
S188L
inactive mutant enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
basis work for molecular directional breeding of sweet potato
additional information