Detail Information for IndEnz0001000013
IED ID IndEnz0001000013
Enzyme Type ID amylase000013
Protein Name Pancreatic alpha-amylase
PA
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name Amy2 Amy2a
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MKFVLLLSLIGFCWAQYDPHTSDGRTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVHNPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAGNPAGTSSTCGSYLNPNNREFPAVPYSAWDFNDNKCNGEIDNYNDAYQVRNCRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGSSILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRWNRNFQNGKDQNDWIGPPNNNGVTKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVVNGQPFSNWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISGDKVDGNCTGLRVNVGSDGKAHFSISNSAEDPFIAIHADSKL
Enzyme Length 508
Uniprot Accession Number P00688
Absorption
Active Site ACT_SITE 209; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 245; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746
Activity Regulation
Binding Site BINDING 207; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 310; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 349; /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); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Natural variant (12); Sequence conflict (6); Signal peptide (1); Site (1)
Keywords 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, extracellular space.
Modified Residue MOD_RES 16; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:6165618
Post Translational Modification
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000269|PubMed:6165618
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10078553; 10471501; 11044404; 11062007; 11478809; 11784060; 11891983; 12101187; 12189445; 12399441; 12559489; 12917290; 1302014; 1370487; 14970313; 15003629; 15280211; 15467835; 15680365; 15793245; 16169491; 1617222; 16326147; 16418487; 16423820; 1673105; 1676977; 16786601; 16920096; 1699843; 1716634; 17185046; 17223109; 17366624; 1970802; 2294404; 2328996; 2410924; 2413838; 2450406; 2451911; 2574151; 2676841; 2824476; 2897103; 2989529; 30487608; 3641189; 3877171; 4461036; 4745489; 489953; 6091898; 6160849; 6161122; 6163812; 6176569; 6207174; 6360562; 7493641; 7600975; 7678001; 7894156; 7935793; 8034307; 8034329; 8294906; 8404042; 8413315; 8449508; 8452817; 8482578; 8543783; 9121556; 9403069; 9851981;
Motif
Gene Encoded By
Mass 57,318
Kinetics
Metal Binding METAL 115; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 170; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746; METAL 179; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 213; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746
Rhea ID
Cross Reference Brenda