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Enzyme Nomenclature
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
- 1.14.11.19
-
anthocyanins
- dihydroflavonol
- chalcone
-
4-reductase
- flavanone
- flavonols
-
3-hydroxylase
-
leucoanthocyanidins
-
proanthocyanidins
-
3-o-glucosyltransferase
- dihydroquercetin
- dihydroflavonol-4-reductase
-
2-oxoglutarate-dependent
-
udp-glucose:flavonoid
- leucocyanidins
-
r2r3-myb
-
sarawak
-
3beta-hydroxylase
-
flavonoid-related
- myrtillus
-
anthocyanin-related
-
3',5'-hydroxylase
- agriculture
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.11.19
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RECOMMENDED NAME
GeneOntology No.
anthocyanidin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = a (4S)- 2,3-dehydroflavan-3,4-diol + succinate + CO2 + H2O
(1a)
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a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O
a (4S)- 2,3-dehydroflavan-3,4-diol = an anthocyanidin + H2O
(1b)
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a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O
mechanism
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a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O
mechanism
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a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O
overall reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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CAS REGISTRY NUMBER
COMMENTARY
180984-01-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Lam cultivar A5, A1, Yamakawamurasaki, and A3 and one of white-fleshed sweet potato cultivar Yubeibai
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overexpression in rice mutant Nootripathu, which accumulates proanthocyanidins exclusively in pericarp
UniProt
wild-type and ldox/fls1-2 double mutant, lacking leucoanthocyanidin dioxygenase and functional flavonol synthase 1-2, EC 1.14.11.23
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shoot cultures from TNR 31-35 (hybrid of Malus sieversii var. sieversii f. niedzwetzkyana)
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
lack of enzyme encoding gene BjANS expression blocks biosynthesis of proanthocyanidins in the yellow seed coat, and therefore seeds appear yellow because of transparent testa
malfunction
two inactive alleles are reported: a mutant anthocyanidin synthase allele containing a 4-bp insertion at the end of exon1 is identified from yellow bulbs of the F2 population in which the DFR-A (dihydroflavonol 4-reductase) genotype is homozygous for an active allele. The 4-bp insertion causes a frame-shift mutation and results in creation of a premature stop codon at the start of exon2. This mutant anthocyanidin synthase allele is designated ANSPS allele. RT-PCR results show that transcripts of the ANSPS allele are almost undetectable in yellow F2 bulbs, implying the involvement of nonsense-mediated mRNA decay. Another inactive anthocyanidin synthase allele is identified from the light-red F1 populations showing complementation between DFR-A (dihydroflavonol 4-reductase) and anthocyanidin synthase genes. A critical amino acid change of the strictly conserved serine residue into leucine is found in this mutant allele designated ANSS188L
malfunction
an insertion in the PgLDOX gene (leucoanthocyanidin dioxygenase/anthocyanidin synthase) is responsible for the white anthocyanin-less phenotype. None of the analyzed white pomegranate tissues are able to synthesize mRNA corresponding to the PgLDOX gene
metabolism
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anthocyanidin synthase is one of the key enzymes in the biosynthesis of both anthocyanins and proanthocyanidins in grapevine
metabolism
anthocyanidin synthase, a 2-oxoglutarate iron-dependent oxygenase, converts leucoanthocyanidins into 3-hydroxyanthocyanidin in late flavonoid biosynthesis
metabolism
the enzyme plays a pivotal role in anthocyanin biosynthesis. It is responsible for anthocyanin accumulation during petal coloration in different crabapple cultivars; the enzyme plays a pivotal role in anthocyanin biosynthesis. It is responsible for anthocyanin accumulation during petal coloration in different crabapple cultivars
metabolism
the enzyme catalyzes the conversion of colorless leucoanthocyanins into colored anthocyanins
metabolism
the enzyme catalyzes the penultimate step in anthocyanin biosynthesis, from leucoanthocyanidins to anthocyanidins, the first colored compound in the anthocyanin pathway
metabolism
Reaumuria trigyna leucoanthocyanidin dioxygenase is one of three dioxygenases in the flavonoid pathway that catalyzes the formation of anthocyanidins from leucoanthocyanidins. It is involved in enhancing plant response to NaCl stress
metabolism
the enzyme is involved in the anthocyanin biosynthesis pathway
metabolism
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anthocyanidin synthase is the key enzyme in anthocyanin biosynthesis
metabolism
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anthocyanidin synthase is one of the key enzymes in the biosynthesis of both anthocyanins and proanthocyanidins in grapevine
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physiological function
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flavonol synthase activity, correspondending to EC 1.14.11.23, in case of mutants lacking the active flavonol synthase 1
physiological function
the enzyme is involved in the biosynthesis of proanthocyanidins and in seed coat color formation
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3R)-trans-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + O2
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-
-
-
?
(2R,3S,4R)-trans-leucocyanidin + 2-oxoglutarate + O2
trans-dihydroquercetin + cis-dihydroquercetin + quercetin + succinate + CO2
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-
-
-
?
(2R,3S,4S)-cis-leucocyanidin + 2-oxoglutarate + O2
quercetin + succinate + CO2
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-
-
-
?
2R,3S,4R-trans-leucocyanidin + 2-oxoglutarate + O2
2R,3S-cis-dihydroquercetin + 2R,3R-trans-dihydroquercetin + cyanidin + quercetin
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55% 2R,3S-cis-dihydroquercetin + 11% 2R,3R-trans-dihydroquercetin + 4% cyanidin + 30% quercetin
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?
2R,3S,4S-cis-leucoanthocyanidin + 2-oxoglutarate + O2
cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
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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
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10% 2R,3S-cis-dihydroquercetin + 2% 2R,3R-trans-dihydroquercetin + 3% cyanidin + 85% quercetin
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?
3,4-cis-leucocyanidin + 2-oxoglutarate + O2
cyanidin + succinate + CO2
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-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2
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-
-
?
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + O2
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-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + O2
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-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + O2
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-
-
?
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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using (2R,3S,4R)-leucocyanidin or (2R,3S,4R)-leucopelargonidin as substrates
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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more detail to stereochemistry
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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-
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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more detail to stereochemistry
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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using (2R,3S,4R)-leucocyanidin or (2R,3S,4R)-leucopelargonidin as substrates
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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using (2R,3S,4R)-leucocyanidin or (2R,3S,4R)-leucopelargonidin as substrates
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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using (2R,3S,4R)-leucocyanidin or (2R,3S,4R)-leucopelargonidin as substrates
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ir
leucocyanidin + 2-oxoglutarate + O2
cis-dihydroquercetin + trans-dihydroquercetin + succinate + CO2
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using (2R,3S,4R)-leucocyanidin or (2R,3S,4R)-leucopelargonidin as substrates
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ir
leucocyanidin + 2-oxoglutarate + O2 + H+
cyanidin + succinate + CO2 + 2 H2O
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?
leucocyanidin + 2-oxoglutarate + O2 + H+
cyanidin + succinate + CO2 + 2 H2O
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-
?
additional information
?
-
catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids, from the colorless leucoanthocyanidins to the colored anthocyanidins
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-
additional information
?
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-
catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids, from the colorless leucoanthocyanidins to the colored anthocyanidins
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-
additional information
?
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expression in abiotic stress responses. Up-regulated by all of the six tested abiotic stresses, UV-B, abscisic acid, sucrose, salicylic acid, cold and ethylene, consistent with the promoter region analysis of GbANS
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-
additional information
?
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expression in abiotic stress responses. Up-regulated by all of the six tested abiotic stresses, UV-B, abscisic acid, sucrose, salicylic acid, cold and ethylene, consistent with the promoter region analysis of GbANS
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-
-
additional information
?
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-
catalyzes the penultimate step in the biosynthesis of anthocyanin. This reaction is responsible for the formation of the colored anthocyanidins from the colorless leucoanthocyanidins
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2R,3S,4S-cis-leucoanthocyanidin + 2-oxoglutarate + O2
cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
-
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
?
-
B2M0X8
catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids, from the colorless leucoanthocyanidins to the colored anthocyanidins
-
-
-
additional information
?
-
-
catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids, from the colorless leucoanthocyanidins to the colored anthocyanidins
-
-
-
additional information
?
-
B2M0X8
expression in abiotic stress responses. Up-regulated by all of the six tested abiotic stresses, UV-B, abscisic acid, sucrose, salicylic acid, cold and ethylene, consistent with the promoter region analysis of GbANS
-
-
-
additional information
?
-
-
expression in abiotic stress responses. Up-regulated by all of the six tested abiotic stresses, UV-B, abscisic acid, sucrose, salicylic acid, cold and ethylene, consistent with the promoter region analysis of GbANS
-
-
-
additional information
?
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-
catalyzes the penultimate step in the biosynthesis of anthocyanin. This reaction is responsible for the formation of the colored anthocyanidins from the colorless leucoanthocyanidins
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
all lines and seed coats of the black-seeded lines, not in the yellow-seeded seed coats
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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
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primarily distributed in the growth point and leaf primordium of the leaf buds
levels of transcripts encoding anthocyanidin synthase, dihydroflavonol reductase and anthocyanidin reductase parallel the accumulation of proanthocyanidins in developing seeds
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
additional information
-
primarily distributed in the exocarp, mesocarp, and seed of the fruit, developmentally dependent expression in skin and flesh
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primarily distributed in the exocarp, mesocarp, and seed of the fruit, developmentally dependent expression in skin and flesh
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young and mature. Weakly expressed in young fruits, highest level of GbANS mRNA is observed in mature fruits
genotype SR-305 shows highest activity at 21 days after anthesis
genotype BL-204 shows highest activity in leaves at 7 day after anthesis
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primarily distributed in palisade and spongy tissues of the leaves
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fibrous, thick, and storage roots. IbANS is expressed most abundantly during the formation of storage roots
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primarily distributed in the primary phloem and pith ray in the stems
-
additional information
GbANS transcripts are not detected in the stems and roots
additional information
-
GbANS transcripts are not detected in the stems and roots
additional information
abundant expression in the red cell line, weak expression in the yellow cell line. No expression in root
additional information
-
expression and tissue localization of ANS in different Cabernet Sauvignon samples, overview
additional information
-
expression and tissue localization of ANS in different Cabernet Sauvignon samples, overview
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
in the mesocarp vascular bundle and leaf bud cells
-
additional information
-
subcellular localization of ANS in different Cabernet Sauvignon samples, overview
-
additional information
-
subcellular localization of ANS in different Cabernet Sauvignon samples, overview
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-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of recombinant enzyme
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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
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)
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
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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
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
wild-type and ldox/fls1-2 double mutant, lacking leucoanthocyanidin dioxygenase and functional flavonol synthase 1-2, EC 1.14.11.23
additional information
-
the IbANS expression profile in different sweet potato cultivars corresponded to the pattern of anthocyanin accumulation
additional information
-
expression of maize leaf colour regulatory gene Lc results in increased mRNA levels for phenylalanine ammonia-lyase, chalcone synthase, flavanone 3beta-hydroxylase, dihydroxavonol 4-reductase, leucoanthocyanidin reductases, anthocyanidin synthase and anthocyanidin reductase. In leaf tissue of transgenic lines, increased levels are detected of the anthocyanin idaein, the flavan 3-ol epicatechin, and especially the isomeric catechin, and some distinct dimeric proanthocyanidins
additional information
-
shift in polyphenol profile and sublethal phenotype caused by silencing the enzyme, comparison to 4 transgenic plants of different lines
additional information
shift in polyphenol profile and sublethal phenotype caused by silencing the enzyme, comparison to 4 transgenic plants of different lines
additional information
down-regulation by antisense-RNA results in reduced anthocyanin and proanthocyanin levels, but has no impact on flavonol levels
additional information
-
down-regulation by antisense-RNA results in reduced anthocyanin and proanthocyanin levels, but has no impact on flavonol levels
additional information
expression in maize a2 mutant results in production of anthocyanins in the aleurione. Transgenic rice mutant Nootripathu plants which accumulate proanthocyanidins exclusively in pericarp, channel the proanthocyanidin precursors to the production of anthocyanidin upon overexpression of enzyme. Transgenic rice plants show an increased accumulation of a mixture of flavonoids and anthocyanins with concomitant decrease in proanthocyanidins
additional information
the mutation inside Ans gene in raspberry is responsible for yellow fruit phenotypes. An inactive ans allele in a yellow fruit raspberry (Anne) is identified. A 5 bp insertion in the coding region is identified and designated as ansC5. The insertion creates a premature stop codon resulting in a truncated protein of 264 amino acids, compared to 414 amino acids wild-type ANS protein. This mutation leads to loss of function of the encoded protein that might also result in transcriptional downregulation of Ans gene as a secondary effect, i.e., nonsense-mediated mRNA decay. Further, this mutation results in loss of visible and detectable anthocyanin pigments
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
C7S854
the specific primer pairs developed for rye ABP genes represent effective rye chromosome-specific markers and can be used for chromosome identification in wheat-rye hybrids
additional information
-
the specific primer pairs developed for rye ABP genes represent effective rye chromosome-specific markers and can be used for chromosome identification in wheat-rye hybrids
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.19)
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