Literature summary for 3.2.1.48 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.

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Cloned(Commentary)

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

Localization

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

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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

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Release 2023.1 (January 2023)