Flavonol 3-O-glucosyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.1.91 | ||||||||
CAS no. | 50812-18-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a flavonol 3-O-glucosyltransferase ( EC 2.4.1.91) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are UDP-glucose and flavonol, whereas its two products are UDP and flavonol 3-O-beta-D-glucoside. The flavonoids that can act as substrates within this reaction include quercetin, kaempferol, dihydrokaempferol, kaempferid, fisetin, and isorhamnetin. Flavonol 3-O-glucosyltransferase is a hexosyl group transfer enzyme. [1]
This enzyme is known by the systematic name UPD-glucose:flavonol 3-O-D glucosyltransferase, and it participates in flavonoid biosynthesis and causes the formation of anthocyanins. Anthocyanins produce a purple color in the plant tissues that they are present in. [2]
It is an enzyme found most notably in grapes ( Vitis vinifera). [3] This enzyme is found within a number of other plants as well—such as snapdragons ( Antirrhinum majus), kale ( Brassica oleracea), and grapefruit ( Citrus x paradisi). [4]
This enzyme is involved in the biosynthesis of secondary metabolites. The primary function of this enzyme within its pathway is binding a glucoside onto a flavonol molecule, forming a flavonol 3-O-glucoside. [5] It is through this mechanism that the enzyme converts anthocyanidins to anthocyanins as a part of the phenylpropanoid pathway. One specific example would be this enzymes actions on pelargonidin. Flavonol 3-O-glucosyltransferase binds the glucoside to this protein, making pelargonidin 3-O-glucoside. This enzyme is also involved in the flavone glycoside pathway, and daphnetin modification in some organisms. The role of the enzyme in these pathways is, again, to bind a glucoside to the substrate to construct a flavonol 3-O-glucoside. [6]
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:flavonol 3-O-D-glucosyltransferase. Other names in common use include:
Among those, UFGT is divided into UDP-glucose: Flavonoid 3-O-glucosyltransferase (UF3GT) and UDP-glucose: Flavonoid 5-O-glucosyltransferase (UF5GT), which are responsible for the glucosylation of anthocyanins to produce stable molecules. [7]
Some of the inhibitors of this enzyme include CaCl2, CoCl2, Cu+2, CuCl2, KCl, Mg+2, and Mn+2. [8] The primary active site residue of this enzyme is Asp181, as determined by studies of how mutations affect enzyme capacity. [9] There are several documentations of the crystalline structure of flavonol 3-O-glucosyltransferase (2C1X, 2C1Z, and 2C9Z), [10] and, based on these renderings of the enzyme, there is only one subunit in the quaternary structure of the molecule.
Flavonol 3-O-glucosyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.4.1.91 | ||||||||
CAS no. | 50812-18-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a flavonol 3-O-glucosyltransferase ( EC 2.4.1.91) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are UDP-glucose and flavonol, whereas its two products are UDP and flavonol 3-O-beta-D-glucoside. The flavonoids that can act as substrates within this reaction include quercetin, kaempferol, dihydrokaempferol, kaempferid, fisetin, and isorhamnetin. Flavonol 3-O-glucosyltransferase is a hexosyl group transfer enzyme. [1]
This enzyme is known by the systematic name UPD-glucose:flavonol 3-O-D glucosyltransferase, and it participates in flavonoid biosynthesis and causes the formation of anthocyanins. Anthocyanins produce a purple color in the plant tissues that they are present in. [2]
It is an enzyme found most notably in grapes ( Vitis vinifera). [3] This enzyme is found within a number of other plants as well—such as snapdragons ( Antirrhinum majus), kale ( Brassica oleracea), and grapefruit ( Citrus x paradisi). [4]
This enzyme is involved in the biosynthesis of secondary metabolites. The primary function of this enzyme within its pathway is binding a glucoside onto a flavonol molecule, forming a flavonol 3-O-glucoside. [5] It is through this mechanism that the enzyme converts anthocyanidins to anthocyanins as a part of the phenylpropanoid pathway. One specific example would be this enzymes actions on pelargonidin. Flavonol 3-O-glucosyltransferase binds the glucoside to this protein, making pelargonidin 3-O-glucoside. This enzyme is also involved in the flavone glycoside pathway, and daphnetin modification in some organisms. The role of the enzyme in these pathways is, again, to bind a glucoside to the substrate to construct a flavonol 3-O-glucoside. [6]
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:flavonol 3-O-D-glucosyltransferase. Other names in common use include:
Among those, UFGT is divided into UDP-glucose: Flavonoid 3-O-glucosyltransferase (UF3GT) and UDP-glucose: Flavonoid 5-O-glucosyltransferase (UF5GT), which are responsible for the glucosylation of anthocyanins to produce stable molecules. [7]
Some of the inhibitors of this enzyme include CaCl2, CoCl2, Cu+2, CuCl2, KCl, Mg+2, and Mn+2. [8] The primary active site residue of this enzyme is Asp181, as determined by studies of how mutations affect enzyme capacity. [9] There are several documentations of the crystalline structure of flavonol 3-O-glucosyltransferase (2C1X, 2C1Z, and 2C9Z), [10] and, based on these renderings of the enzyme, there is only one subunit in the quaternary structure of the molecule.