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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

Molecular Weight

Molecular Weight on EC 3.2.1.48 - sucrose alpha-glucosidase

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112000
-
1 * 112000 + 1* 100000, hetero-dimer, 2 catalytically active sites for maltase and sucrase
130000
-
gel filtration, density gradient, equilibrium centrifugation, sucrase subunit
140000
145000
-
1 * 145000, sucrase + 1* 151000, isomaltase
150000
-
SDS-PAGE, intact pancreatic duct, subunit II
210000
-
x * 210000, about
220000
245000
-
fully glycosylated enzyme in the Golgi apparatus
260000
270000
-
SDS-PAGE
280000
290000
-
gel filtration, sucrase-isomaltase complex, intestinal mucosa
380000
-
380000 sucrase + 543000 isomaltase, enzyme complex after solubilisation by emulphogen and papain
64000
1 * 64000, SDS-PAGE
99320
-
gene coding sucrase cloned in pPNG102 contains a ORF which defines a polypeptide of 99319 Da, the sequence shows similarity to previously sequenced sucrose-hydrolyzing enzymes
additional information
-
The enzyme complex is a pseudo-dimeric assembly of a correctly folded and an enzymatically active pro-SI. The sucrase subunit functions as an intramolecular chaperone implicated in the folding of isomaltase subunit. After acquisition of a correct folding in the sucrase subunit this mature form binds tightly to the isomaltase, disrupting its interaction with calnexin. The consequence is that the isomaltase subunit acquires correct folding and sucrase subunit is no longer secreted into the external milieu.