Detail Information for IndEnz0001000008
IED ID IndEnz0001000008
Enzyme Type ID amylase000008
Protein Name Alpha-amylase 1
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase 1
Salivary and hepatic alpha-amylase
Gene Name Amy1 Amy-1-a Amy1a
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 MKFFLLLSLIGFCWAQYDPHTQYGRTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGVGAQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEFKYGAKLGKVMRKWDGEKMSYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYYWPRNFQNGKDVNDWVGPPNNNGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVVNGQPFANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISGDKVDGNCTGIKVYVGNDGKAHFSISNSAEDPFIAIHAESKI
Enzyme Length 511
Uniprot Accession Number P00687
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); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Sequence conflict (11); Signal peptide (1); Site (1)
Keywords Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 16; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|Ref.8
Post Translational Modification
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000269|Ref.8
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 1021597; 10464095; 10842072; 1141004; 1348427; 1360278; 1401878; 14681479; 1617215; 1794058; 18554416; 2002257; 20391537; 2040456; 21267068; 21677750; 22529374; 23012479; 2328996; 2332419; 2338144; 23449223; 23684747; 2410924; 2431276; 2450406; 2451911; 2476716; 25410786; 2565740; 25715394; 2571572; 25918232; 26098870; 26132294; 2824476; 284003; 2897103; 2902233; 2903254; 2987507; 2989529; 3038891; 34446743; 3872721; 3877171; 4745489; 489953; 6091898; 6160178; 6160849; 6161122; 6163812; 6176569; 6200103; 6207174; 6375655; 6529441; 7493641; 7523515; 7558020; 7608209; 7829080; 7859283; 7873877; 7894156; 7905852; 7946325; 7949740; 8001974; 8094303; 8144363; 8390965; 8482578; 8486361; 8589528; 8604219; 8661735; 8666240; 9121556; 9250879; 93520; 94264;
Motif
Gene Encoded By
Mass 57,644
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