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ChemicalBook--->CAS DataBase List--->9032-14-8

9032-14-8

9032-14-8 Structure

9032-14-8 Structure
IdentificationBack Directory
[Name]

DEXTRAN SUCRASE
[CAS]

9032-14-8
[Synonyms]

EC 2.4.1.5
DEXTRAN SUCRASE
dextran sucrase from leuconostoc*mesenteroides
Dextransucrase,from Leuconstoc mesenteroides
Glucosyltransferase, sucrose-1,6-.alpha.-glucan
Native Leuconostoc mesenteroides Dextran Sucrase
Glucansucrase 70D from Streptococcus mutans, Recombinant
Glucansucrase 70C from Streptococcus mutans, Recombinant
Glucansucrase 70B from Streptococcus mutans, Recombinant
[EINECS(EC#)]

821-951-5
[MDL Number]

MFCD00130936
Chemical PropertiesBack Directory
[density ]

1.33-1.42g/cm3 at 20℃
[vapor pressure ]

0.002-0.008Pa at 25℃
[storage temp. ]

-20°C
[solubility ]

H2O: soluble0.9-1.1mg/mL, clear to slightly hazy, colorless to light yellow
[form ]

lyophilized powder
[biological source]

bacterial (Leuconostoc mesenteroides)
[Water Solubility ]

H2O: soluble 0.9-1.1mg/mL, clear to slightly hazy, colorless to light yellow
[Specific Activity]

≥100units/mg protein
[LogP]

-1.3 at 20℃ and pH5.7-5.8
Safety DataBack Directory
[WGK Germany ]

3
Hazard InformationBack Directory
[Uses]

Dextran sucrase from Leuconostoc mesenteroides has been used in a study to investigate the functional and structural characterization of α-(1→2) branching sucrase derived from DSR-E glucansucrase. Dextran sucrase from Leuconostoc mesenteroides has also been used in a study to investigate the bioengineering of Leuconostoc mesenteroides glucansucrases.
[General Description]

Dextran Sucrase from Leuconostoc mesenteroides belongs to glycoside hydrolase family 70 (GH70). It functions through a retaining mechanism and uses two catalytic acidic residues. Dextran sucrase has a dextran binding site in the C-terminal domain.
[Biochem/physiol Actions]

Dextransucrases are glucansucrases that are able to produce dextran, a glucose polymer linked mainly through α1-6 bonds. However, α1-3, α1-6, α1-4 and α1-2 bonds are also found, in both the main chain and the branching linkages. The peptide has approximately 1600 amino acids. The aspartic acid in position 551 is essential for catalytic activity, while glutamic acid 589 and aspartic acid 662 complement the catalytic triad. The activity of dextransucrase is decreased by EDTA, and is restored by the addition of calcium ions. Zinc, cadmium, lead, mercury and copper ions are inhibitory to various degrees.
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