Cloned (Comment) | Organism |
---|---|
gene Ct3GT-A, recombinant His-tagged enzyme expression in Escherichia coli strain XL1 Blue | Clitoria ternatea |
Crystallization (Comment) | Organism |
---|---|
purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of protein in 20 mM Tris-HCl, pH 7.4, 200 mM NaCl and 2 mM CaCl2, with reservoir solution containing 0.1 M sodium citrate tribasic dihydrate, pH 5.6, 0.2 M ammonium acetate and 26% w/v PEG 4000, equilibration against reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.85 A resolution | Clitoria ternatea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Clitoria ternatea | the enzyme catalyzes glucosyl transfer from UDP-glucose to anthocyanidins such as delphinidin | ? | - |
? | |
UDP-D-glucose + delphinidin | Clitoria ternatea | - |
UDP + delphinidin-3-O-beta-D-glucoside | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clitoria ternatea | A4F1R4 | gene Ct3GT-A | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain XL1 Blue by nickel affinity chromatography, removal of the N-terminal His-tag by digestion using recombinant enterokinase, followed by cation exchange chromatography, to homogeneity | Clitoria ternatea |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme catalyzes glucosyl transfer from UDP-glucose to anthocyanidins such as delphinidin | Clitoria ternatea | ? | - |
? | |
UDP-D-glucose + delphinidin | - |
Clitoria ternatea | UDP + delphinidin-3-O-beta-D-glucoside | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like beta/alpha/beta domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrate, structure-function relationship analysis, overview | Clitoria ternatea |
Synonyms | Comment | Organism |
---|---|---|
Ct3GT-A | - |
Clitoria ternatea |
UDP-glucose:anthocyanidin 3-O-glucosyltransferase | - |
Clitoria ternatea |
General Information | Comment | Organism |
---|---|---|
evolution | conparison of structure and substrate specificity of UDP-glucose:anthocyanidin 3-O-glucosyltransferase, Ct3GT-A, from Clitoria ternatea and flavonoid glycosyltransferase, VvGT1, from Vitis vinifera detailed overview | Clitoria ternatea |
metabolism | the enzyme catalyzes the first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin | Clitoria ternatea |
additional information | the structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like beta/alpha/beta domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates, structure-function relationship analysis, overview. The donor-binding site conserved as a UGT signature PSPG motif is located in the C-domain of Ct3GT-A, and the C-terminal helix comprising residues 431-445 participates in forming the N-domain after crossing the cleft. The acceptor-binding site is formed mostly by the residues from the N-domain. Besides the hydrophobic residues Phe12, Phe116, Trp135, Tyr145, Phe192 and Leu196, the hydrophilic residues Asn137, Asp181 and Asp367 are arranged to form the acceptor-binding site | Clitoria ternatea |