Literature summary for 2.4.1.9 extracted from

Charoenwongpaiboon, T.; Sitthiyotha, T.; Na Ayutthaya, P.P.; Wangpaiboon, K.; Chunsrivirot, S.; Hengsakul Prousoontorn, M.; Pichyangkura, R.
Modulation of fructooligosaccharide chain length and insight into the product binding motif of Lactobacillus reuteri 121 inulosucrase (2019), Carbohydr. Polym., 209, 111-121 .

Search for more literature for 2.4.1.9

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Limosilactobacillus reuteri

Protein Variants

Protein Variants	Comment	Organism
D479A	the mutant shows 80% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme	Limosilactobacillus reuteri
D689A	for hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme	Limosilactobacillus reuteri
N414A	the mutation does not affect fructooligosaccharide production but causes the production of shorter oligosaccharides compared to the wild type	Limosilactobacillus reuteri
N543A	the mutant shows 67% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme	Limosilactobacillus reuteri
N555A	the mutant shows 75% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme	Limosilactobacillus reuteri
N561A	the mutant enzyme incompletely hydrolyzes sucrose at 50°C though equivalent initial enzymatic activity is used	Limosilactobacillus reuteri
R483A	the mutant shows 73% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme	Limosilactobacillus reuteri
W551A	the mutant shows 58% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme. The mutant enzyme incompletely hydrolyzes sucrose at 50°C though equivalent initial enzymatic activity is used	Limosilactobacillus reuteri

Organism

Organism	UniProt	Comment	Textmining
Limosilactobacillus reuteri	-	-	-
Limosilactobacillus reuteri 121	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Toyopearl AF-Chelate-650M column chromatography	Limosilactobacillus reuteri

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme also hydrolyzes sucrose to D-fructose and D-glucose	Limosilactobacillus reuteri	?	-	-
additional information	the enzyme also hydrolyzes sucrose to D-fructose and D-glucose	Limosilactobacillus reuteri 121	?	-	-
sucrose + sucrose	-	Limosilactobacillus reuteri	1-kestose + nystose + fructooligosaccharides	-	?
sucrose + sucrose	-	Limosilactobacillus reuteri 121	1-kestose + nystose + fructooligosaccharides	-	?

Synonyms

Synonyms	Comment	Organism
INU	-	Limosilactobacillus reuteri

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
50	-	-	Limosilactobacillus reuteri

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5	6	-	Limosilactobacillus reuteri

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)