IED ID | IndEnz0001000593 |
Enzyme Type ID | amylase000593 |
Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Fragment |
Gene Name | |
Organism | Bacillus sp. |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. |
Enzyme Sequence | AHQLPMGTLCNFYEWYRRDD |
Enzyme Length | 20 |
Uniprot Accession Number | P86331 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by Hg (2+). Inhibited by Zn (2+). Activated by Fe (2+), Mg (2+) and Ba (2+). {ECO:0000269|PubMed:20109486}. |
Binding Site | |
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:0000269|PubMed:20109486}; |
DNA Binding | |
EC Number | 3.2.1.1 |
Enzyme Function | FUNCTION: Alpha-amylase active towards amylose, starch, amylopectin and maltodextrins. Has lower activity towards glycogen, and is not active towards alpha/beta-cyclodextrin. {ECO:0000269|PubMed:20109486}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Active from 30 to 75 degrees Celsius, inactivated following 150 minutes incubation at 85 degrees Celsius. {ECO:0000269|PubMed:20109486}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. Stable from pH 4.0-7.5, activity decreases drastically above pH 7.5 and below pH 3.5. {ECO:0000269|PubMed:20109486}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Non-terminal residue (1) |
Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 2,516 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.1; |