Purification and characterization of tripeptidyl peptidase I from Dictyostelium discoideum
10.1080/15216549900202203.absA tripeptidyl peptidase I from Dictyostelium discoideum was purified 744‐fold to near homogeneity. The enzyme is 214 kDa in size and is composed of two monomers with a Mr of 107 kDa. It has two pH optima at pH 4.5 and 5.9 and is a serine peptidase with no aminopeptidase...
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| Veröffentlicht in: | Biochemistry and molecular biology international 1999-06, Vol.47 (6), p.1079-1088 |
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| creator | Krimper, Robert P. Jones, Theodore H. D. |
| description | 10.1080/15216549900202203.absA tripeptidyl peptidase I from Dictyostelium discoideum was purified 744‐fold to near homogeneity. The enzyme is 214 kDa in size and is composed of two monomers with a Mr of 107 kDa. It has two pH optima at pH 4.5 and 5.9 and is a serine peptidase with no aminopeptidase or dipeptidyl peptidase activity. The enzyme was relatively specific showing activity on ala‐ala‐phe‐p‐nitroaniline but also acted on substrates with proline in the Pi position in contrast to mammalian TPP I. The Km values of the enzyme at pH 4.5 for ala‐ala‐phe‐, ala‐phe‐pro‐ and ala‐ala‐pro‐p‐nitroanilines were 271μM, 437μM and 888μM, respectively. The enzyme is most abundant during the amoeba stage of the life cycle but is present in the early stages of development and may therefore have a dual role in the organism in mobilizing amino acids or in processing specific peptides or proteins. |
| doi_str_mv | 10.1080/15216549900202203 |
| format | Article |
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D.</creator><creatorcontrib>Krimper, Robert P. ; Jones, Theodore H. D.</creatorcontrib><description>10.1080/15216549900202203.absA tripeptidyl peptidase I from Dictyostelium discoideum was purified 744‐fold to near homogeneity. The enzyme is 214 kDa in size and is composed of two monomers with a Mr of 107 kDa. It has two pH optima at pH 4.5 and 5.9 and is a serine peptidase with no aminopeptidase or dipeptidyl peptidase activity. The enzyme was relatively specific showing activity on ala‐ala‐phe‐p‐nitroaniline but also acted on substrates with proline in the Pi position in contrast to mammalian TPP I. The Km values of the enzyme at pH 4.5 for ala‐ala‐phe‐, ala‐phe‐pro‐ and ala‐ala‐pro‐p‐nitroanilines were 271μM, 437μM and 888μM, respectively. The enzyme is most abundant during the amoeba stage of the life cycle but is present in the early stages of development and may therefore have a dual role in the organism in mobilizing amino acids or in processing specific peptides or proteins.</description><identifier>ISSN: 1521-6543</identifier><identifier>ISSN: 1039-9712</identifier><identifier>EISSN: 1521-6551</identifier><identifier>DOI: 10.1080/15216549900202203</identifier><identifier>PMID: 10410254</identifier><language>eng</language><publisher>UK: Informa Healthcare</publisher><subject>aminopeptidase ; Aminopeptidases ; Animals ; Dictyostelium ; Dictyostelium - enzymology ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases ; Endopeptidases - chemistry ; Endopeptidases - isolation & purification ; Hydrogen-Ion Concentration ; Kinetics ; Molecular Weight ; peptidase ; peptide processing ; Peptides - metabolism ; prohormone ; protein degradation ; Serine Endopeptidases - chemistry ; Serine Proteases ; Serine Proteinase Inhibitors - pharmacology ; Substrate Specificity ; Time Factors ; TPP ; tripeptidyl peptidase</subject><ispartof>Biochemistry and molecular biology international, 1999-06, Vol.47 (6), p.1079-1088</ispartof><rights>Copyright © 1999 International Union of Biochemistry and Molecular Biology</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4169-2f954172b6926531b8cb278cf6f32061d5b0bd088712615e6d1cfa3fab2d04b73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1080%2F15216549900202203$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1080%2F15216549900202203$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10410254$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Krimper, Robert P.</creatorcontrib><creatorcontrib>Jones, Theodore H. D.</creatorcontrib><title>Purification and characterization of tripeptidyl peptidase I from Dictyostelium discoideum</title><title>Biochemistry and molecular biology international</title><addtitle>Biochem Mol Biol Int</addtitle><description>10.1080/15216549900202203.absA tripeptidyl peptidase I from Dictyostelium discoideum was purified 744‐fold to near homogeneity. The enzyme is 214 kDa in size and is composed of two monomers with a Mr of 107 kDa. It has two pH optima at pH 4.5 and 5.9 and is a serine peptidase with no aminopeptidase or dipeptidyl peptidase activity. The enzyme was relatively specific showing activity on ala‐ala‐phe‐p‐nitroaniline but also acted on substrates with proline in the Pi position in contrast to mammalian TPP I. The Km values of the enzyme at pH 4.5 for ala‐ala‐phe‐, ala‐phe‐pro‐ and ala‐ala‐pro‐p‐nitroanilines were 271μM, 437μM and 888μM, respectively. The enzyme is most abundant during the amoeba stage of the life cycle but is present in the early stages of development and may therefore have a dual role in the organism in mobilizing amino acids or in processing specific peptides or proteins.</description><subject>aminopeptidase</subject><subject>Aminopeptidases</subject><subject>Animals</subject><subject>Dictyostelium</subject><subject>Dictyostelium - enzymology</subject><subject>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</subject><subject>Endopeptidases - chemistry</subject><subject>Endopeptidases - isolation & purification</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>peptidase</subject><subject>peptide processing</subject><subject>Peptides - metabolism</subject><subject>prohormone</subject><subject>protein degradation</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Proteases</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><subject>Substrate Specificity</subject><subject>Time Factors</subject><subject>TPP</subject><subject>tripeptidyl peptidase</subject><issn>1521-6543</issn><issn>1039-9712</issn><issn>1521-6551</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAUhYMozjj6A9xIV-6quUmTNuDGGV8DI7oYN25KmgdG2mlNWqT-ejt0EMGFd3Mvh-8cLgehU8AXgDN8CYwAZ4kQGBNMCKZ7aLrVYs4Y7P_cCZ2goxDe8TApFodoAjgBTFgyRa_PnXfWKdm6ehPJjY7Um_RStca7r1GsbdR615imdbovo_GQwUTLyPq6im6cavs6tKZ0XRVpF1TttOmqY3RgZRnMyW7P0Mvd7XrxEK-e7peL61WsEuAiJlawBFJScEE4o1BkqiBppiy3lGAOmhW40DjLUiAcmOEalJXUyoJonBQpnaHzMbfx9UdnQptXww-mLOXG1F3IucgEpxkfQBhB5esQvLF5410lfZ8DzreF5n8KHTxnu_CuqIz-5RgbHICrEfh0pen_T8zX88d5ygBSyqig368dgYo</recordid><startdate>199906</startdate><enddate>199906</enddate><creator>Krimper, Robert P.</creator><creator>Jones, Theodore H. D.</creator><general>Informa Healthcare</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199906</creationdate><title>Purification and characterization of tripeptidyl peptidase I from Dictyostelium discoideum</title><author>Krimper, Robert P. ; Jones, Theodore H. D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4169-2f954172b6926531b8cb278cf6f32061d5b0bd088712615e6d1cfa3fab2d04b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>aminopeptidase</topic><topic>Aminopeptidases</topic><topic>Animals</topic><topic>Dictyostelium</topic><topic>Dictyostelium - enzymology</topic><topic>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</topic><topic>Endopeptidases - chemistry</topic><topic>Endopeptidases - isolation & purification</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>peptidase</topic><topic>peptide processing</topic><topic>Peptides - metabolism</topic><topic>prohormone</topic><topic>protein degradation</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Proteases</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Substrate Specificity</topic><topic>Time Factors</topic><topic>TPP</topic><topic>tripeptidyl peptidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Krimper, Robert P.</creatorcontrib><creatorcontrib>Jones, Theodore H. D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry and molecular biology international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Krimper, Robert P.</au><au>Jones, Theodore H. D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of tripeptidyl peptidase I from Dictyostelium discoideum</atitle><jtitle>Biochemistry and molecular biology international</jtitle><addtitle>Biochem Mol Biol Int</addtitle><date>1999-06</date><risdate>1999</risdate><volume>47</volume><issue>6</issue><spage>1079</spage><epage>1088</epage><pages>1079-1088</pages><issn>1521-6543</issn><issn>1039-9712</issn><eissn>1521-6551</eissn><abstract>10.1080/15216549900202203.absA tripeptidyl peptidase I from Dictyostelium discoideum was purified 744‐fold to near homogeneity. The enzyme is 214 kDa in size and is composed of two monomers with a Mr of 107 kDa. It has two pH optima at pH 4.5 and 5.9 and is a serine peptidase with no aminopeptidase or dipeptidyl peptidase activity. The enzyme was relatively specific showing activity on ala‐ala‐phe‐p‐nitroaniline but also acted on substrates with proline in the Pi position in contrast to mammalian TPP I. The Km values of the enzyme at pH 4.5 for ala‐ala‐phe‐, ala‐phe‐pro‐ and ala‐ala‐pro‐p‐nitroanilines were 271μM, 437μM and 888μM, respectively. The enzyme is most abundant during the amoeba stage of the life cycle but is present in the early stages of development and may therefore have a dual role in the organism in mobilizing amino acids or in processing specific peptides or proteins.</abstract><cop>UK</cop><pub>Informa Healthcare</pub><pmid>10410254</pmid><doi>10.1080/15216549900202203</doi><tpages>10</tpages></addata></record> |
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| source | MEDLINE; Access via Wiley Online Library; Wiley Online Library (Open Access Collection) |
| subjects | aminopeptidase Aminopeptidases Animals Dictyostelium Dictyostelium - enzymology Dipeptidyl-Peptidases and Tripeptidyl-Peptidases Endopeptidases - chemistry Endopeptidases - isolation & purification Hydrogen-Ion Concentration Kinetics Molecular Weight peptidase peptide processing Peptides - metabolism prohormone protein degradation Serine Endopeptidases - chemistry Serine Proteases Serine Proteinase Inhibitors - pharmacology Substrate Specificity Time Factors TPP tripeptidyl peptidase |
| title | Purification and characterization of tripeptidyl peptidase I from Dictyostelium discoideum |
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