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UniProt functional annotation for Q01532 | ||
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| UniProt code: Q01532. |
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| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
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| 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}. |
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| 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; |
| 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}. |
| 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.; pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:1400467, ECO:0000269|PubMed:8063738, ECO:0000269|PubMed:8463237}; |
| Subunit: | |
Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA. {ECO:0000269|PubMed:7638617}. |
| Subcellular location: | |
[Isoform Cytoplasmic]: Cytoplasm. |
| Subcellular location: | |
[Isoform Mitochondrial]: Mitochondrion. |
| Ptm: | |
The N-terminus of isoform Cytoplasmic is blocked. |
| Mass spectrometry: | |
Mass=51830; Method=Electrospray; Evidence={ECO:0000269|PubMed:9374524}; |
| Miscellaneous: | |
Present with 521 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Miscellaneous: | |
[Isoform Cytoplasmic]: Produced by alternative initiation at Met-30 of isoform Mitochondrial. {ECO:0000305}. |
| Similarity: | |
Belongs to the peptidase C1 family. {ECO:0000255|PROSITE- ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}. |
Annotations taken from UniProtKB at the EBI.