IED ID | IndEnz0001000146 |
Enzyme Type ID | amylase000146 |
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 |