Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.1.48: sucrose alpha-glucosidase

This is an abbreviated version!
For detailed information about sucrose alpha-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.48

Reaction

isomaltose
+
H2O
= 2 D-glucose

Synonyms

alpha-glucosidase, glucosidase, sucrose alpha-, intestinal sucrase, isomaltase, More, PF0132, pro-SI, SI, sucrase, sucrase isomaltase, sucrase-invertase, sucrase-isomaltase, sucrase-isomaltase enzyme complex, sucrase/isomaltase, sucrose alpha-glucohydrolase, sucrose hydrolase, SUH

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.48 sucrose alpha-glucosidase

Crystallization

Crystallization on EC 3.2.1.48 - sucrose alpha-glucosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and enzyme in complex with the inhibitor kotalanol, hanging drop vapor diffusion method, 0.001 ml of reservoir solution containing 0.5 M NaCl, 0.1 M bis tris propane, pH 7.0, and 18% PEG 4000, is equilibrated over 0.0015 ml of protein solution and 0.003 ml of reservoir solution, containing 0.1 M MgCl2, 0.1 M bis tris propane, pH 7.0, 15% PEG 4000, X-ray diffraction structure determination and analysis at 3.2 and 2.15 A resolution, respectively, molecular replacement
purified mutant E322Q in complex with Tris or sucrose, E322Q SUH is crystallized by hanging-drop vapor-diffusion method at 22°C in a crystallization buffer consisting of 0.1 M HEPES, pH 6.5, 0.2 M calcium acetate, 16% PEG 3000, and 5 mM DTT, with 0.1 M caesium chloride, and crystallization of SeMet SUH sitting-drop method at 22°C in a crystallization buffer consisting of 0.1 M HEPES, pH 6.5, 0.2 M calcium acetate, 16% PEG 3000, and 5 mM DTT, with 0.1 M guanidine chloride, X-ray diffraction structure determination and analysis at 1.8 A resolution
purified enzyme in the resting state with an empty active site, X-ray diffraction structure determination and analysis at 1.9 A resolution
-