Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hiromoto, T.; Honjo, E.; Tamada, T.; Noda, N.; Kazuma, K.; Suzuki, M.; Kuroki, R.
    Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea (2013), J. Synchrotron Radiat., 20, 894-898.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.115 gene Ct3GT-A, recombinant His-tagged enzyme expression in Escherichia coli strain XL1 Blue Clitoria ternatea

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.115 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.115 additional information Clitoria ternatea the enzyme catalyzes glucosyl transfer from UDP-glucose to anthocyanidins such as delphinidin ?
-
 ?
2.4.1.115 UDP-D-glucose + delphinidin Clitoria ternatea
-
 UDP + delphinidin-3-O-beta-D-glucoside
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.115 Clitoria ternatea A4F1R4 gene Ct3GT-A
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.115 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.115 additional information the enzyme catalyzes glucosyl transfer from UDP-glucose to anthocyanidins such as delphinidin Clitoria ternatea ?
-
 ?
2.4.1.115 UDP-D-glucose + delphinidin
-
 Clitoria ternatea UDP + delphinidin-3-O-beta-D-glucoside
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.115 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

EC Number Synonyms Comment Organism
2.4.1.115 Ct3GT-A
-
 Clitoria ternatea
2.4.1.115 UDP-glucose:anthocyanidin 3-O-glucosyltransferase
-
 Clitoria ternatea

General Information

EC Number General Information Comment Organism
2.4.1.115 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
2.4.1.115 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
2.4.1.115 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