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Literature summary for 2.4.1.9 extracted from

  • Olivares-Illana, V.; Lopez-Munguia, A.; Olvera, C.
    Molecular characterization of inulosucrase from Leuconostoc citreum: a fructosyltransferase within a glucosyltransferase (2003), J. Bacteriol., 185, 3606-3612.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of the full-length enzyme and two C-terminally truncated enzyme forms in Escherichia coli. Natural chimeric enzyme with three domains: the first and third with high identity with alternansucrase, the second domain, which is the catalytic one has similarity with levansucrase and inulosucrase Leuconostoc citreum

Protein Variants

Protein Variants Comment Organism
additional information when the C-terminal domain is deleted the resulting enzyme is more active and more hydrolytic than the wild-type enzyme but is more sensitive to inactivation at 40°C Leuconostoc citreum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup Leuconostoc citreum
-
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
?

Organism

Organism UniProt Comment Textmining
Leuconostoc citreum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
-
Leuconostoc citreum alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup wild-type and recombinant enzyme produce inulin from sucose Leuconostoc citreum alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
half-life of wild-type enzyme: 70 min, half-life of the two C-terminally truncated mutant enzymes is 20 min and 12 min Leuconostoc citreum