Detail Information for IndEnz0001000593
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;