| IED ID | IndEnz0002004009 |
| Enzyme Type ID | protease004009 |
| Protein Name |
Alpha-amylase inhibitor Fragment |
| Gene Name | |
| Organism | Secale cereale (Rye) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Secale Secale cereale (Rye) |
| Enzyme Sequence | SEDCTPWTATPITVLAGCRDYVGEQ |
| Enzyme Length | 25 |
| Uniprot Accession Number | P83048 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Inhibits alpha-amylases but not trypsin. Is more effective against insect alpha-amylases than those of mammals. {ECO:0000269|PubMed:11137459}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Alpha-amylase inhibitor;Direct protein sequencing;Glycoprotein;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: May exist both in a glycosylated and in an unglycosylated form. {ECO:0000303|PubMed:11137459}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,713 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |