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Literature summary extracted from

  • Nihira, T.; Mori, T.; Asakura, M.; Okahata, Y.
    Kinetic studies of dextransucrase enzyme reactions on a substrate- or enzyme-immobilized 27 MHz quartz crystal microbalance (2011), Langmuir, 27, 2107-2111.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.5 additional information immobilisation of the enzyme directly on a 27 MHz quartz crystal microbalance, QCM, plate, or on a dextran-acceptor-QCM plate, method evaluation and binding kinetics,overview. The enzymatic activity of DSase is not affected by immobilization, possibly due to the use of a long PEG spacer group. Typical frequency changes of the dextran-immobilized QCM as a function of time in response to the addition of DSase and sucrose substrate in 50 mM acetate buffer pH 5.2, 150 mM NaCl, and 1 mM CaCl2 at 25°C Leuconostoc mesenteroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.5 additional information
-
 additional information DSase has a high affinity for dextran as first substrate with Kd of 18 nM, kinetic analysis of 27 MHz quartz crystal microbalance, QCM, plate-immobilized enzyme, overview Leuconostoc mesenteroides
2.4.1.5 3
-
 sucrose enzyme in bulk solution, pH 5.2, 25°C Leuconostoc mesenteroides
2.4.1.5 3.4
-
 sucrose dextran-QCM-immobilized enzyme, pH 5.2, 25°C Leuconostoc mesenteroides
2.4.1.5 7.2
-
 sucrose directly QCM-immobilized enzyme, pH 5.2, 25°C Leuconostoc mesenteroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.5 Ca2+ enhances activity Leuconostoc mesenteroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.5 sucrose + [(1->6)-alpha-D-glucosyl]n Leuconostoc mesenteroides
-
 D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.5 Leuconostoc mesenteroides
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.1.5 sucrose + [(1->6)-alpha-D-glucosyl]n = D-fructose + [(1->6)-alpha-D-glucosyl]n+1 catalytic reaction mechanism for dextran elongation, overview Leuconostoc mesenteroides
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.5 additional information DSase can quickly proceed to elongation because the decomposition rate of the ESdex complex is very small Leuconostoc mesenteroides ?
-
 ?
2.4.1.5 sucrose + [(1->6)-alpha-D-glucosyl]n
-
 Leuconostoc mesenteroides D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
 ?
2.4.1.5 sucrose + [(1->6)-alpha-D-glucosyl]n DSase-catalyzed dextran elongation Leuconostoc mesenteroides D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.5 DSase
-
 Leuconostoc mesenteroides
2.4.1.5 sucrose:1,6-alpha-D-glucan-6-alpha-D-glucosyltransferase
-
 Leuconostoc mesenteroides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.5 25
-
 assay at Leuconostoc mesenteroides

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.5 3.1
-
 sucrose directly QCM-immobilized enzyme, pH 5.2, 25°C Leuconostoc mesenteroides
2.4.1.5 3.5
-
 sucrose dextran-QCM-immobilized enzyme, pH 5.2, 25°C Leuconostoc mesenteroides

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.5 5.2
-
 assay at Leuconostoc mesenteroides