| IED ID | IndEnz0002000029 |
| Enzyme Type ID | protease000029 |
| Protein Name |
Cysteine proteinase 1, mitochondrial EC 3.4.22.40 Bleomycin hydrolase BLM hydrolase Homocysteine-thiolactonase HTLase Hcy-thiolactonase Leucine aminopeptidase 3 Y3 |
| Gene Name | LAP3 BLH1 GAL6 YCP1 EC1118_1N9_1035g |
| Organism | Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) |
| Enzyme Sequence | MLPTSVSRSLYLKTFRSHLLRAPQIVLKRMSSSIDISKINSWNKEFQSDLTHQLATTVLKNYNADDALLNKTRLQKQDNRVFNTVVSTDSTPVTNQKSSGRCWLFAATNQLRLNVLSELNLKEFELSQAYLFFYDKLEKANYFLDQIVSSADQDIDSRLVQYLLAAPTEDGGQYSMFLNLVKKYGLIPKDLYGDLPYSTTASRKWNSLLTTKLREFAETLRTALKERSADDSIIVTLREQMQREIFRLMSLFMDIPPVQPNEQFTWEYVDKDKKIHTIKSTPLEFASKYAKLDPSTPVSLINDPRHPYGKLIKIDRLGNVLGGDAVIYLNVDNETLSKLVVKRLQNNKAVFFGSHTPKFMDKKTGVMDIELWNYPAIGYNLPQQKASRIRYHESLMTHAMLITGCHVDETSKLPLRYRVENSWGKDSGKDGLYVMTQKYFEEYCFQIVVDINELPKELASKFTSGKEEPIVLPIWDPMGALAK |
| Enzyme Length | 483 |
| Uniprot Accession Number | C8ZFZ7 |
| Absorption | |
| Active Site | ACT_SITE 102; /evidence=ECO:0000250; ACT_SITE 398; /evidence=ECO:0000250; ACT_SITE 421; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by E64, a specific inhibitor of cysteine proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.; EC=3.4.22.40; |
| DNA Binding | |
| EC Number | 3.4.22.40 |
| Enzyme Function | FUNCTION: The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (1); Propeptide (1); Transit peptide (1) |
| Keywords | Alternative initiation;Cytoplasm;DNA-binding;Hydrolase;Mitochondrion;Protease;Thiol protease;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus of isoform Cytoplasmic is blocked. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,483 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |