| IED ID | IndEnz0002015321 |
| Enzyme Type ID | protease015321 |
| Protein Name |
Proteinase inhibitor LUTI |
| Gene Name | |
| Organism | Linum usitatissimum (Flax) (Linum humile) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Linaceae Linum Linum usitatissimum (Flax) (Linum humile) |
| Enzyme Sequence | SRRCPGKNAWPELVGKSGNMAAATVERENRNVHAIVLKEGSAMTKDFRCDRVWVIVNDHGVVTSVPHIT |
| Enzyme Length | 69 |
| Uniprot Accession Number | P82381 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: In vitro, strong inhibitor of bovine beta-trypsin, weak inhibitor of alpha-chymotrypsin, subtilisin BPN', subtilisin Carlsberg and cathepsin G. {ECO:0000269|PubMed:11828426}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (3); Chain (1); Disulfide bond (1); Helix (2); Modified residue (1); Site (1) |
| Keywords | 3D-structure;Acetylation;Direct protein sequencing;Disulfide bond;Protease inhibitor;Serine protease inhibitor |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 1; /note=N-acetylserine; /evidence=ECO:0000269|PubMed:11828426 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1DWM; |
| Mapped Pubmed ID | 11183783; |
| Motif | |
| Gene Encoded By | |
| Mass | 7,613 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |