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

BRENDA support

Literature summary extracted from

  • Jacob, R.; Purschel, B.; Naim, H.Y.
    Sucrase is an intramolecular chaperone located at the C-terminal end of the sucrase-isomaltase enzyme complex (2002), J. Biol. Chem., 277, 32141-32148.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.48 expression of the cDNA constructs encoding the sucrase and isomaltase domains in transfected cells Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.48 membrane the isomaltase subunit is membrane associated and the sucrase subunit is hydrophilic Homo sapiens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.48 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. Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.48 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.48 glycoprotein the individual expression of isomaltase subunit in COS-1 cells results in a malfolded and transport-incompetent glycoprotein, during the sucrase subunit a transport-competent protein Homo sapiens