| IED ID | IndEnz0001000243 |
| Enzyme Type ID | amylase000243 |
| Protein Name |
Alpha-amylase 2B EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase 2B Carcinoid alpha-amylase |
| Gene Name | AMY2B |
| 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 | MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLVGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL |
| Enzyme Length | 511 |
| Uniprot Accession Number | P19961 |
| Absorption | |
| Active Site | ACT_SITE 212; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 248; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 210; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 313; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 352; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (2); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Alternative splicing;Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 16; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P04746 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10769135; 15299664; 16152770; 20195357; 20711500; 28659346; 30938472; 31478242; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,710 |
| Kinetics | |
| Metal Binding | METAL 115; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 173; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746; METAL 182; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 216; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746 |
| Rhea ID | |
| Cross Reference Brenda |