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

BRENDA support

Literature summary for 2.4.1.9 extracted from

  • Ozimek, L.K.; van Hijum, S.A.; van Koningsveld, G.A.; van Der Maarel, M.J.; van Geel-Schutten, G.H.; Dijkhuizen, L.
    Site-directed mutagenesis study of the three catalytic residues of the fructosyltransferases of Lactobacillus reuteri 121 (2004), FEBS Lett., 560, 131-133.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of Myc/His-tagged wild-type and mutant enzymes in Escherichia coli Limosilactobacillus reuteri

Protein Variants

Protein Variants Comment Organism
D272N site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Limosilactobacillus reuteri
D424N site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Limosilactobacillus reuteri
E523Q site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Limosilactobacillus reuteri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + (2,1-beta-D-fructosyl)n Limosilactobacillus reuteri
-
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
?
sucrose + (2,1-beta-D-fructosyl)n Limosilactobacillus reuteri 121
-
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
recombinant Myc/His-tagged wild-type and mutant enzymes from Escherichia coli Limosilactobacillus reuteri

Reaction

Reaction Comment Organism Reaction ID
sucrose + [(beta-D-Fruf-(2->1))n]-alpha-D-Glup = alpha-D-glucose + [(beta-D-Fruf-(2->1))n+1]-alpha-D-Glup catalytic triad formed by essential residues D272, D424, and E523 Limosilactobacillus reuteri

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00032
-
purified recombinant mutant D272N, inulin synthesizing activity Limosilactobacillus reuteri
0.00066
-
purified recombinant mutant D424N, inulin synthesizing activity Limosilactobacillus reuteri
0.0028
-
purified recombinant mutant E523Q, inulin synthesizing activity Limosilactobacillus reuteri
47
-
purified recombinant wild-type enzyme, inulin synthesizing activity Limosilactobacillus reuteri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + (2,1-beta-D-fructosyl)n
-
Limosilactobacillus reuteri alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
?
sucrose + (2,1-beta-D-fructosyl)n transferase activity Limosilactobacillus reuteri alpha-D-glucose + (2,1-beta-D-fructosyl)n+1 i.e. inulin ?
sucrose + (2,1-beta-D-fructosyl)n
-
Limosilactobacillus reuteri 121 alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
?
sucrose + (2,1-beta-D-fructosyl)n transferase activity Limosilactobacillus reuteri 121 alpha-D-glucose + (2,1-beta-D-fructosyl)n+1 i.e. inulin ?
sucrose + H2O hydrolytic activity Limosilactobacillus reuteri alpha-D-glucose + beta-D-fructose
-
?
sucrose + H2O hydrolytic activity Limosilactobacillus reuteri 121 alpha-D-glucose + beta-D-fructose
-
?

Synonyms

Synonyms Comment Organism
fructosyltransferase
-
Limosilactobacillus reuteri
FTF
-
Limosilactobacillus reuteri
More enzyme belongs to the family 68 of glucoside hydrolases Limosilactobacillus reuteri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Limosilactobacillus reuteri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
assay at Limosilactobacillus reuteri