Recombinant Human Sucrase-isomaltase, intestinal (SI), partial

1. Three biosynthetic phenotypes for the novel SI mutations were identified. The first biosynthetic phenotype was defined by mutants that are intracellularly transported in a fashion similar to wild type SI and with normal, but varying, levels of enzymatic activity. The second biosynthetic phenotype was defined by mutants with delayed maturation and trafficking kinetics and reduced activity. The third is inactive. PMID: 28062276
2. Novel compound heterozygote V577G/C1531W SI mutations, which lead to lack of SI expression in the duodenal brush border, were found in a family with congenital sucrase-isomaltase deficiency. PMID: 27749612
3. A common mutation was found in the sucrase-isomaltase gene, c.273_274delAG, to be responsible for the high prevalence of congenital sucrase-isomaltase deficiency among Inuit people. PMID: 25452324
4. SI mutations result in loss of enzyme function by preventing the biosynthesis of catalytically competent SI at the cell surface in lymphocytic leukemia PMID: 23418305
5. study found four common mutations in the SI gene (3 of the 4 are in the sucrase domain, with 1 in the isomaltase domain) account for 59 percent of clinical symptoms of congenital sucrase-isomaltase deficiency (CSID); the remaining 41 percent were rare events PMID: 23103650
6. investigation of EIS (enzyme-inhibitor-substrate) complex of sucrase: kinetic studies of complex formation/stability; role of complex in prevention of hyperglycemia by L-arabinose PMID: 21165628
7. Core2 O-glycan structure is essential for expression of SI and DDP-IV during intestinal cell differentiation. PMID: 20841351
8. These results suggest that sucrase-isomaltase transcription might be unchanged or lower in maturity-onset diabetes of the young (MODY) type 3, but greater in MODY5. PMID: 15522234
9. phenylalanine cluster is required for shielding a folding determinant in the extracellular domain of SI; substitution of a Q by a P at residue 1098 of sucrase disrupts this determinant and elicits retention of SI(Q1098P) in ER and cis-Golgi PMID: 15944403
10. The sucrase-isomaltase (SI) gene from 11 patients of Hungarian origin with congenital sucrase-isomaltase deficiency was analysed.In six out of the 11 patients the phenotype of CSID could be explained by compound heterozygosity. PMID: 16329100
11. analysis of a mutation which affects an epitope responsible for the apical targeting fidelity of sucrase-isomaltase in congenital sucrase-isomaltase deficiency PMID: 16543230
12. hepatocyte nuclear factor (HNF)-1alpha and HNF-1beta would contribute to constitutive expression of the SI gene in the differentiated state in Caco-2 cells PMID: 16802690
13. glucose regulation of sucrase-isomaltase gene expression was attenuated in HNF-1alphaT539fsdelC cells, but was well maintained in empty vector & HNF-1betaR177X cells.Results suggest that HNF-1alpha participates in glucose regulation of SI gene expression. PMID: 17194452
14. The effects of mutations in the sucrase domain of SIC1229Y and SIF1745C indicate the importance of a direct interaction between isomaltase and sucrose and the role of sucrose as an intermolecular chaperone in the intracellular transport of SI PMID: 19121318

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HGNC: 10856

OMIM: 222900

KEGG: hsa:6476

STRING: 9606.ENSP00000264382

UniGene: Hs.429596