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Literature summary extracted from

  • Osmani, S.A.; Bak, S.; Imberty, A.; Olsen, C.E.; Moller, B.L.
    Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses (2008), Plant Physiol., 148, 1295-1308.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.254 expression in Escherichia coli Bellis perennis

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.254 D152A mutation decreases the activity with cyanidin 3-O-beta-D-glucoside to less than 15% of wild type Bellis perennis
2.4.1.254 N123A mutation decreases the activity with cyanidin 3-O-beta-D-glucoside to less than 15% of wild type Bellis perennis
2.4.1.254 R25G mutant enzyme exhibits only 0.5% to 2.5% of wild-type activity with UDP-D-glucuronate, but shows a 3fold increase in activity with UDP-D-glucose Bellis perennis
2.4.1.254 R25K mutant enzyme exhibits only 0.5% to 2.5% of wild-type activity with UDP-D-glucuronate, but shows a 3fold increase in activity with UDP-D-glucose Bellis perennis
2.4.1.254 R25S mutant enzyme exhibits only 0.5% to 2.5% of wild-type activity with UDP-D-glucuronate, but shows a 3fold increase in activity with UDP-D-glucose Bellis perennis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.254 0.8
-
 cyanidin 3-O-beta-glucoside pH 7.5, 30°C, wild-type enzyme Bellis perennis
2.4.1.254 1
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme I187A Bellis perennis
2.4.1.254 1.1
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, wild-type enzyme Bellis perennis
2.4.1.254 1.4
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme R25S Bellis perennis
2.4.1.254 1.6
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme N123A Bellis perennis
2.4.1.254 1.9
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme L148A Bellis perennis
2.4.1.254 2.1
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme R25G Bellis perennis
2.4.1.254 2.7
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme D152A Bellis perennis
2.4.1.254 7
-
 UDP-beta-D-glucuronate pH 7.5, 30°C, mutant enzyme R25K Bellis perennis

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.254 Bellis perennis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.254
-
 Bellis perennis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.254 UDP-beta-D-glucuronate + cyanidin 3-O-beta-D-glucoside highly specific with respect to the sugar donor UDP-GlcUA. Activity with other activated sugars such as UDP-Glc, UDP-Gal, and UDP-Xyl is very low. Wild-type enzyme activity toward delphinidin-3-O-glucoside is only 5% to 10% of the activity with cyanidin 3-O-beta-D-glucoside. A few specific amino acid residues as well as the overall size and shape of the acceptor pocket define substrate specificity Bellis perennis UDP + cyanidin 3-O-beta-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.254 BpUGT94B1
-
 Bellis perennis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.254 30
-
 assay at Bellis perennis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.254 additional information
-
 additional information relative kcat-values for wild-type enzyme and mutant enzymes Bellis perennis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.254 7.5
-
 assay at Bellis perennis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.1.254 additional information
-
 additional information relative kcat/KM values for wild-type enzyme and mutant enzymes Bellis perennis