Literature summary for 2.4.1.115 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.

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Cloned(Commentary)

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

Crystallization (Commentary)

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

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Clitoria ternatea	A4F1R4	gene Ct3GT-A	-

Purification (Commentary)

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 and Products (Substrate)

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

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

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

General Information

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