| IED ID | IndEnz0002018820 |
| Enzyme Type ID | protease018820 |
| 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 YNL239W N1118 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (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 ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MLPTSVSRSLYLKTFRSHLLRAPQIVLKRMSSSIDISKINSWNKEFQSDLTHQLATTVLKNYNADDALLNKTRLQKQDNRVFNTVVSTDSTPVTNQKSSGRCWLFAATNQLRLNVLSELNLKEFELSQAYLFFYDKLEKANYFLDQIVSSADQDIDSRLVQYLLAAPTEDGGQYSMFLNLVKKYGLIPKDLYGDLPYSTTASRKWNSLLTTKLREFAETLRTALKERSADDSIIVTLREQMQREIFRLMSLFMDIPPVQPNEQFTWEYVDKDKKIHTIKSTPLEFASKYAKLDPSTPVSLINDPRHPYGKLIKIDRLGNVLGGDAVIYLNVDNETLSKLVVKRLQNNKAVFFGSHTPKFMDKKTGVMDIELWNYPAIGYNLPQQKASRIRYHESLMTHAMLITGCHVDETSKLPLRYRVENSWGKDSGKDGLYVMTQKYFEEYCFQIVVDINELPKELASKFTSGKEEPIVLPIWDPMGALAK |
| Enzyme Length | 483 |
| Uniprot Accession Number | Q01532 |
| Absorption | |
| Active Site | ACT_SITE 102; ACT_SITE 398; ACT_SITE 421 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by E64, a specific inhibitor of cysteine proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions. {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8463237}. |
| 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. {ECO:0000269|PubMed:12555812, ECO:0000269|PubMed:16769724}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (14); Chain (1); Helix (20); Mutagenesis (4); Propeptide (1); Sequence conflict (1); Transit peptide (1); Turn (5) |
| Keywords | 3D-structure;Alternative initiation;Cytoplasm;DNA-binding;Direct protein sequencing;Hydrolase;Mitochondrion;Protease;Reference proteome;Thiol protease;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus of isoform Cytoplasmic is blocked. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1A6R; 1GCB; 2DZY; 2DZZ; 2E00; 2E01; 2E02; 2E03; 3GCB; |
| Mapped Pubmed ID | 10688190; 11101808; 11283351; 11743162; 12702462; 12855446; 14558142; 14690591; 15961354; 16269670; 16429126; 16554755; 17007609; 17506111; 18649367; 18719252; 18772282; 19061865; 19185714; 19264099; 19446584; 19536198; 20232931; 21124907; 21317551; 21589890; 21602906; 22306284; 24401081; 27077367; 27693354; 6352682; 6397123; 7476893; 8620487; 9309169; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,483 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.8 uM for arginine-4-methyl-7-coumarylamide {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; KM=0.33 mM for glutamine-beta-naphthylamide {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; KM=228 uM for lysine-4-methyl-7-coumarylamide {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; Vmax=2.56 umol/h/mg enzyme for arginine-4-methyl-7-coumarylamide {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; Vmax=370 nmol/min/mg enzyme for glutamine-beta-naphthylamide {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; Note=N-terminal acetylation of lysine-4-methyl-7-coumarylamide (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this substrate.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.13.23;3.4.22.40; |