| http://purl.uniprot.org/citations/3886641 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3886641 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/3886641 | http://www.w3.org/2000/01/rdf-schema#comment | "A newly recognized peptidase, designated proteinase yscD, was purified from the yeast Saccharomyces cerevisiae. The enzyme cleaves the Pro-Phe bond of the synthetic peptide substrate Bz-Pro-Phe-Arg-4-nitroanilide and the Ala-Ala bond of Ac-Ala-Ala-Pro-Ala-4-nitroanilide, Ac-Ala-Ala-Pro-Phe-4-nitroanilide, and MeO-Suc-Ala-Ala-Pro-Met-4-nitroanilide with high efficiency (Bz-, Ac-, and MeO-Suc are defined as benzoyl, acetyl, and methoxy-succinyl, respectively). [3H]Methylcasein does not serve as a substrate. Optimum pH for cleavage of Bz-Pro-Phe-Arg-4-nitroanilide is in the range of 6.5 to 7; for Ac-Ala-Ala-Pro-Ala-4-nitroanilide the range is between 5.75 and 6. For MeO-Suc-Ala-Ala-Pro-Met-4-nitroanilide the pH optimum was found to be 5.5. The purified enzyme has an apparent Stokes radius of Rs = 37.9 A as judged by gel chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicates a molecular weight of approximately 83,000 for the enzyme. Mercurials and EDTA were found to be potent inhibitors of proteinase yscD activity."xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)89111-6"xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/author | "Achstetter T."xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/author | "Wolf D.H."xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/author | "Ehmann C."xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/date | "1985"xsd:gYear |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/pages | "4585-4590"xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/title | "Proteinase yscD. Purification and characterization of a new yeast peptidase."xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://purl.uniprot.org/core/volume | "260"xsd:string |
| http://purl.uniprot.org/citations/3886641 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3886641 |
| http://purl.uniprot.org/citations/3886641 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3886641 |
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| http://purl.uniprot.org/citations/3886641 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3886641 |
| http://purl.uniprot.org/enzyme/3.4.24.37 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3886641 |
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| http://purl.uniprot.org/uniprot/P25375 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/3886641 |