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Literature summary for 3.2.1.11 extracted from

  • Kim, Y.M.; Shimizu, R.; Nakai, H.; Mori, H.; Okuyama, M.; Kang, M.S.; Fujimoto, Z.; Funane, K.; Kim, D.; Kimura, A.
    Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity (2011), Appl. Microbiol. Biotechnol., 91, 329-339.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) CodonPlus-RIL Streptococcus mutans

Protein Variants

Protein Variants Comment Organism
additional information generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview Streptococcus mutans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
89800
-
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE Streptococcus mutans
94537
-
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE Streptococcus mutans
95400
-
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE Streptococcus mutans

Organism

Organism UniProt Comment Textmining
Streptococcus mutans F5BA50
-
-
Streptococcus mutans ATCC 25175 F5BA50
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) CodonPlus-RIL by nickel affinity chromatography, ultrafilatration, and hydrophobic interaction and anion exchange chromatography Streptococcus mutans

Source Tissue

Source Tissue Comment Organism Textmining
additional information cells are cultivated in brain-heart infusion medium Streptococcus mutans
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.02
-
purified recombinant enzyme SmDex95, the 95 kDa variant, pH 5.0, temperature not specified in the publication Streptococcus mutans
8.21
-
purified recombinant enzyme SmDex90, the 90 kDa variant, pH 5.0, temperature not specified in the publication Streptococcus mutans

Storage Stability

Storage Stability Organism
4°C, 2 mM NaN3, 6 months, the purified SmDex90 is proteolytically degraded to more than seven polypeptides of 23-70 kDa during long storage Streptococcus mutans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dextran + H2O
-
Streptococcus mutans ?
-
?
dextran + H2O
-
Streptococcus mutans ATCC 25175 ?
-
?

Subunits

Subunits Comment Organism
? x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE Streptococcus mutans
More the enzyme comprises four regions from the N- to C-termini: N-terminal variable region, N-VR, conserved region, CR, glucan-binding site, GBS, and C-terminal variable region, C-VR Streptococcus mutans

Synonyms

Synonyms Comment Organism
endo-dextranase
-
Streptococcus mutans
More the enzyme belongs to the glycoside hydrolase family (GH) 66 Streptococcus mutans
SmDex
-
Streptococcus mutans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
purified recombinant enzymes, stable up to Streptococcus mutans

General Information

General Information Comment Organism
additional information N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site Streptococcus mutans