| IED ID | IndEnz0001000101 |
| Enzyme Type ID | amylase000101 |
| Protein Name |
Alpha-amylase inhibitor HOE-467A Tendamistat |
| Gene Name | |
| Organism | Streptomyces tendae |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces tendae |
| Enzyme Sequence | MRVRALRLAALVGAGAALALSPLAAGPASADTTVSEPAPSCVTLYQSWRYSQADNGCAQTVTVKVVYEDDTEGLCYAVAPGQITTVGDGYIGSHGHARYLARCL |
| Enzyme Length | 104 |
| Uniprot Accession Number | P01092 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | 3D-structure;Alpha-amylase inhibitor;Direct protein sequencing;Disulfide bond;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000269|PubMed:6605909 |
| Structure 3D | NMR spectroscopy (3); X-ray crystallography (3) |
| Cross Reference PDB | 1BVN; 1HOE; 1OK0; 2AIT; 3AIT; 4AIT; |
| Mapped Pubmed ID | 14501112; |
| Motif | |
| Gene Encoded By | |
| Mass | 10,759 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |