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Literature summary for 2.4.1.254 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
Search for more literature for 2.4.1.254

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bellis perennis

Protein Variants

Protein Variants Comment Organism
D152A mutation decreases the activity with cyanidin 3-O-beta-D-glucoside to less than 15% of wild type Bellis perennis
N123A mutation decreases the activity with cyanidin 3-O-beta-D-glucoside to less than 15% of wild type Bellis perennis
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
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
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]

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

Organism

Organism UniProt Comment Textmining
Bellis perennis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bellis perennis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
BpUGT94B1
-
 Bellis perennis

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

kcat/KM [mM/s]

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