| IED ID | IndEnz0001000341 |
| Enzyme Type ID | amylase000341 |
| Protein Name |
Sucrase-isomaltase, intestinal Cleaved into: Sucrase EC 3.2.1.48 ; Isomaltase EC 3.2.1.10 |
| Gene Name | SI |
| Organism | Homo sapiens (Human) |
| 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 Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDSGKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMTTTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEFTGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISTRLPSDYIYGIGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSNAMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRWNYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQKYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNPNCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMYSKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAHWLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSRNHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHEFYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDMYLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDTIQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMNAHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGCVWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRVEVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRSSGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPPGYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGPTPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDIDYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVFVKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVDFYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEAEQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGDNYARWDNMDKSIIGMMEFSLFGMSYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNIANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKPTWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDTINLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLYLSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNEDTTNMILRIDLTTHNVTLEEPIEINWS |
| Enzyme Length | 1827 |
| Uniprot Accession Number | P14410 |
| Absorption | |
| Active Site | ACT_SITE 505; /note="Nucleophile; for isomaltase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10066, ECO:0000269|PubMed:20356844"; ACT_SITE 604; /note="For isomaltase activity"; /evidence="ECO:0000269|PubMed:20356844"; ACT_SITE 1394; /note="Nucleophile; for sucrase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10066, ECO:0000269|PubMed:20356844"; ACT_SITE 1397; /note="For sucrase activity"; /evidence="ECO:0000250"; ACT_SITE 1500; /note="Proton donor; for isomaltase activity"; /evidence="ECO:0000250" |
| Activity Regulation | |
| Binding Site | BINDING 264; /note=Substrate; BINDING 388; /note=Substrate; BINDING 588; /note=Substrate; BINDING 662; /note=Substrate |
| 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. {ECO:0000269|PubMed:20356844}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (5); Beta strand (56); Binding site (4); Chain (3); Disulfide bond (5); Domain (2); Glycosylation (18); Helix (26); Initiator methionine (1); Modified residue (8); Natural variant (15); Region (3); Sequence conflict (15); Topological domain (2); Transmembrane (1); Turn (10) |
| Keywords | 3D-structure;Cell membrane;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;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; Single-pass type II membrane protein. Note=Brush border. |
| Modified Residue | MOD_RES 7; /note=Phosphoserine; by PKA; /evidence=ECO:0000269|PubMed:8521865; MOD_RES 237; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 239; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 391; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 400; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 667; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 763; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 765; /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:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3LPO; 3LPP; |
| Mapped Pubmed ID | 12547908; 1256470; 15522234; 15944403; 16543230; 16802690; 17194452; 19121318; 20841351; 21165628; 23103650; 23418305; 25452324; 27749612; 28062276; 29408290; 34242650; 3800897; 3897250; 5849827; 7906143; 807575; 9446624; |
| Motif | |
| Gene Encoded By | |
| Mass | 209,453 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.10;3.2.1.48; |