Literature summary for 3.2.1.10 extracted from

Rodriguez, D.; Ramsay, A.J.; Quesada, V.; Garabaya, C.; Campo, E.; Freije, J.M.; Lopez-Otin, C.
Functional analysis of sucrase-isomaltase mutations from chronic lymphocytic leukemia patients (2013), Hum. Mol. Genet., 22, 2273-2282.

Search for more literature for 3.2.1.10

Application

Application	Comment	Organism
medicine	metabolic enzyme sucrase-isomaltase is one of the most frequently mutated genes in a cohort of 105 chronic lymphocytic leukemia patients. Mutations result in loss of enzyme function by preventing the biosynthesis of catalytically competent sucrase-isomaltase at the cell surface. Mutations impair enzyme function by altering its trafficking along the secretory pathway. Loss-of-function mutations in sucrase-isomaltase result in gene expression patterns that depict ample metabolic reprogramming, pinpointing sucrase-isomaltase as a putative player in the cancer-associated metabolic switch	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D1193N	mutation identified in chronic lymphocytic leukemia patient. Mutation is located in the C-terminal sucrase domain and results in a 25% decrease in activity and decrease of complex glycosylated forms of the mature enzyme	Homo sapiens
R91T	mutation identified in chronic lymphocytic leukemia patient. Mutation is inserted in a trefoil motif situated N-terminal to the isomaltase domain and results in a 75% decrease in activity and decrease of complex glycosylated forms of the mature enzyme	Homo sapiens
T1680I	mutation identified in chronic lymphocytic leukemia patient. Mutation is located in the C-terminal sucrase domain, leads to decrease of complex glycosylated forms of the mature enzyme	Homo sapiens
W1493C	mutation identified in chronic lymphocytic leukemia patient. Mutation is located in the C-terminal sucrase domain with almost complete loss of activity and decrease of complex glycosylated forms of the mature enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14410	-	-

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Release 2023.1 (January 2023)