| IED ID | IndEnz0001000030 |
| Enzyme Type ID | amylase000030 |
| Protein Name |
Sucrase-isomaltase, intestinal Cleaved into: Sucrase EC 3.2.1.48 ; Isomaltase EC 3.2.1.10 Fragments |
| Gene Name | SI |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MARKKFSGLEIXLIVLFAIVLSIAIALVVVXASKXPAVIKLPSDPIPTLRMEMTYHTDYMLE |
| Enzyme Length | 62 |
| Uniprot Accession Number | P56729 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.; EC=3.2.1.48; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10; |
| DNA Binding | |
| EC Number | 3.2.1.48; 3.2.1.10 |
| Enzyme Function | FUNCTION: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Initiator methionine (1); Modified residue (2); Non-adjacent residues (1); Non-terminal residue (1); Sequence uncertainty (7); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Direct protein sequencing;Glycosidase;Hydrolase;Membrane;Multifunctional enzyme;Phosphoprotein;Reference proteome;Repeat;Signal-anchor;Sulfation;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Brush border. {ECO:0000250}. |
| Modified Residue | MOD_RES 7; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P14410; MOD_RES 59; /note=Sulfotyrosine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.; PTM: Sulfated. {ECO:0000269|PubMed:3121301}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,893 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |