| IED ID | IndEnz0001000362 |
| Enzyme Type ID | amylase000362 |
| Protein Name |
Sucrase-isomaltase, intestinal Cleaved into: Sucrase EC 3.2.1.48 ; Isomaltase EC 3.2.1.10 |
| Gene Name | SI |
| Organism | Suncus murinus (Asian house shrew) (Musk shrew) |
| 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 Eulipotyphla (hedgehogs shrews moles and others) Soricidae (shrews) Crocidurinae Suncus (musk shrews) Suncus murinus (Asian house shrew) (Musk shrew) |
| Enzyme Sequence | MARKKSSGLKITLIVLLAIVTIIAIALVAILPTKTPAVELVSTIPGKCPSAENDRLDEKINCIPDQFPTQALCAMQGCCWNPRNESPTPWCSFANNHGYEFEKISNPNINFEPNLKKNSPPTLFGDNITNLLLTTQSQTANRFRFKITDPNNQRYEVPHQFVNKDFSGPPASNPLYDVKITENPFSIKVIRKSNNKILFDTSIGPLVYSNQYLQISTKLPSKYIYGLGEHVHKRFRHDLYWKTWPIFTRDQLPGDNNNNLYGHQTFFMSIEDTSGKSFGVFLMNSNAMEVFIQPTPIVTYRVIGGILDFYIFLGDTPGQVVQQYQELTGRPAMPSYWSLGFQLSRWNYGSLDAVKEVVKRNRDARIPFDAQVTDIDYMEDKKDFTYNNKTFYGLPEFVKDLHDHGQKYIIILDPAISITSLANGNHYKTYERGNEQKVWVYQSDGTTPLIGEVWPGLTVYPDFTNPKCLDWWTNECSIFHEEIKYDGLWIDMNEVSSFVHGSTKGCSDNKLNYPPFIPDILDKLMYAKTICMDAIQHWGKQYDVHSLYGYSMAIATEKAIEKVFPNKRSFILTRSTFAGTGKHATHWLGDNTPSWEHMEWSITPMLEFGLFGMPFIGADICGFVVDTTEELCRRWMQIGAFYPYFRDHNAGGYMPQDPAYFGQDSLLVNTSRHYLDIWYTLLPYLYNLLYKAYVYGETVARPFLYEFYEDTNSWIEDLQFLWGSALLITPVLRQGADRMSAYIPDATWYDYETGGKRTWRKQRVEMYLPGDKIGLHVRGGYIIPTQQPAVNTTASRKNPLGLIIALDNNAAKGDFFWDDGESKDSIEKGKYILYTFSVLNNELDIICTHSSYQEGTTLAFETIKILGLANTVTQVQVAENNQQTIIHNSFTYHASNQSLIIDNLKLNLGKNFTVQWNQVSLDSEKIDCFPDNNPENKQNCEERGCLWEPNSAAEGPRCYFPKQYNPYLVKSTQYSSMGITVDLELNTATARIKMPSNPISVLRLEVKYHKNDMLQFKIYDPQNKRYEVPIPMDIPTTPTSTYENRLYDVNIKGNPFGIQIRRRSTGRIFWDSCLPWGLLLMNQFIQISTRLPSEYVYGFGGVGHRQFKQDLNWHKWGMFNRDQPSGYKISSYGFQPYIYMALGDGGNAHGVFLLNSNAMDVTFQPNPALTYRTIGGILDFYMFLGPNPEVATKQYHEVIGRPVKPPYWALGFHLCRYGYENTSEIRQLYEDMVSAQIPYDVQYTDIDYMERQLDFTIGKGFQDLPEFVDKIRDEGMKYIIILDPAISGNETQDYLAFQRGIEKDVFVKWPNTQDICWAKVWPDLPNITIDDSLTEDEAVNASRAHVAFPDFLKTSTAEWWATEIEDFYNTYMKFDGLWIDMNEPSSFVHGSVDNKCRNEILNYPPYMPALTKRNEGLHFRTMCMETQQTLSNGSSVLHYDVHNLYGWSQAKPTYDALQKTTGKRGIVISRSTYPSAGRWAGHWLGDNYANWDKIGKSIIGMMEFSLFGISFTGADICGFFNNSDYELCARWMQVGAFYPYSRNHNITDTRRQDPVSWNETFASMSTDILNIRYNLLPYFYTQMHDIHANGGTVIRPLLHEFFSETGTWDIYKQFLWGPAFMVTPVVEPYSESVTGYVPDGRWLDYHTGQDIGLRKRLHTLDAPLYKINLHVCGGHILPCQEPAQNTYFSRQNYMKLIVAADDNQTAQGYLFWDDGESIDTYEKGQYLLVQFNLNKATLTSTILKNGYINTREMRLGFINVWGKGNTVVQEVNITYKGNKESVKFSQEANKQILNIDLTANNIVLDEPIEISWT |
| Enzyme Length | 1813 |
| Uniprot Accession Number | O62653 |
| Absorption | |
| Active Site | ACT_SITE 491; /note=Nucleophile; for isomaltase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10066; ACT_SITE 590; /note=For isomaltase activity; /evidence=ECO:0000250; ACT_SITE 1380; /note=Nucleophile; for sucrase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10066; ACT_SITE 1383; /note=For sucrase activity; /evidence=ECO:0000250; ACT_SITE 1486; /note=Proton donor; for sucrase activity; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 250; /note=Substrate; /evidence=ECO:0000250; BINDING 374; /note=Substrate; /evidence=ECO:0000250; BINDING 574; /note=Substrate; /evidence=ECO:0000250; BINDING 648; /note=Substrate; /evidence=ECO:0000250 |
| 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 | Active site (5); Binding site (4); Chain (3); Disulfide bond (5); Domain (2); Glycosylation (16); Modified residue (5); Region (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Membrane;Multifunctional enzyme;Phosphoprotein;Repeat;Signal-anchor;Sulfation;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. |
| Modified Residue | MOD_RES 7; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P14410; MOD_RES 377; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1294; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1368; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1371; /note=Sulfotyrosine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen. {ECO:0000250}.; PTM: Sulfated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 208,305 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.10; |