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Literature summary for 2.4.1.9 extracted from

  • Pijning, T.; Anwar, M.A.; Boeger, M.; Dobruchowska, J.M.; Leemhuis, H.; Kralj, S.; Dijkhuizen, L.; Dijkstra, B.W.
    Crystal structure of inulosucrase from Lactobacillus: insights into the substrate specificity and product specificity of GH68 fructansucrases (2011), J. Mol. Biol., 412, 80-93.
    View publication on PubMed
Search for more literature for 2.4.1.9

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His-tagged fragment of inulosucrase comprising residues 145-708 Lactobacillus johnsonii

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant C-terminally His-tagged inulosucrase residues 145-708 fragment, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement Lactobacillus johnsonii

Protein Variants

Protein Variants Comment Organism
additional information deletion of residues 301-303 reduces the enzyme activity Lactobacillus johnsonii
N301A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Lactobacillus johnsonii
N301S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Lactobacillus johnsonii
N305A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Lactobacillus johnsonii
N305S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Lactobacillus johnsonii

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for activity, binding site structure, overview Lactobacillus johnsonii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + [(2->1)-beta-D-fructosyl]n Lactobacillus johnsonii
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 glucose + [(2->1)-beta-D-fructosyl]n+1
-
 ?
sucrose + [(2->1)-beta-D-fructosyl]n Lactobacillus johnsonii NCC 533
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 glucose + [(2->1)-beta-D-fructosyl]n+1
-
 ?

Organism

Organism UniProt Comment Textmining
Lactobacillus johnsonii
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-
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Lactobacillus johnsonii NCC 533
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + [(2->1)-beta-D-fructosyl]n
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 Lactobacillus johnsonii glucose + [(2->1)-beta-D-fructosyl]n+1
-
 ?
sucrose + [(2->1)-beta-D-fructosyl]n via first transfructosylation product 1-kestose, binding mode, overview, an inulin-type linkage is formed. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases Lactobacillus johnsonii glucose + [(2->1)-beta-D-fructosyl]n+1
-
 ?
sucrose + [(2->1)-beta-D-fructosyl]n
-
 Lactobacillus johnsonii NCC 533 glucose + [(2->1)-beta-D-fructosyl]n+1
-
 ?
sucrose + [(2->1)-beta-D-fructosyl]n via first transfructosylation product 1-kestose, binding mode, overview, an inulin-type linkage is formed. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases Lactobacillus johnsonii NCC 533 glucose + [(2->1)-beta-D-fructosyl]n+1
-
 ?

Synonyms

Synonyms Comment Organism
GH68 fructansucrase
-
 Lactobacillus johnsonii
InuJ
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 Lactobacillus johnsonii

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycoside hydroylase family GH68 Lactobacillus johnsonii
malfunction mutation of two of the asparagine residues (N301 and N305) in the 1B-1C loop to serine or alanine significantly decreases the total enzyme activity of InuJ. Deletion of residues 301-303 from this loop even further reduces the activity Lactobacillus johnsonii
additional information three-dimensional structure of a truncated active GH68 inulosucrase InuJ of Lactobacillus johnsonii strain NCC533, comprising residues 145-708, in its apo form, with a bound substrate sucrose, and with a transfructosylation product 1-kestose, overview. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases. Residues 210-662 of InuJ constitute the globular catalytic core domain, adopting the five-bladed beta-propeller fold typical of GH68 enzymes. Domain and active site structure analysis, overview Lactobacillus johnsonii