Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro

Asparaginase II of Saccharomyces cerevisiae is a cell wall mannan containing glycoprotein. Recent studies have demonstrated that asparaginase II activity increases in exponentially growing cell cultures and then decreases as the cells enter the stationary phase. Enzyme inactivation has been attribut...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochemistry (Easton) 1983-05, Vol.22 (11), p.2704-2707
Hauptverfasser: Kim, Kyu Won, Roon, Robert J
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 2707
container_issue 11
container_start_page 2704
container_title Biochemistry (Easton)
container_volume 22
creator Kim, Kyu Won
Roon, Robert J
description Asparaginase II of Saccharomyces cerevisiae is a cell wall mannan containing glycoprotein. Recent studies have demonstrated that asparaginase II activity increases in exponentially growing cell cultures and then decreases as the cells enter the stationary phase. Enzyme inactivation has been attributed to a Zn2+-dependent protease which is synthesized de novo during the late exponential phase [Pauling, K.D., & Jones, G.E. (1980) J. Gen. Microbiol. 117, 423-430; Pauling, K.D., & Jones, G.E. (1980) Biochim. Biophys. Acta 616, 271-282]. We have investigated the mechanism of asparaginase II inactivation using both whole cell suspensions and highly purified enzyme. Our data indicate that the rate of asparaginase II inactivation in cell suspensions is primarily influenced by pH changes that occur as a consequence of cell growth and glucose fermentation and that enzyme inactivation is not dependent on Zn2+ or on de novo protein synthesis. Also, in vitro studies with purified enzyme show kinetics of inactivation that are similar to those observed in vivo. Consequently, involvement of a yeast protease in the inactivation process is relatively unlikely.
doi_str_mv 10.1021/bi00280a018
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80565160</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>13595487</sourcerecordid><originalsourceid>FETCH-LOGICAL-a300t-fd93cf4a8c12328a189395f97d9c04ed1d43464a7046b8c504f900a01e6420543</originalsourceid><addsrcrecordid>eNqF0M9P2zAUB3ALbYKO7bTzJJ_GYQo8_0y8GyA2KpCoBLvsYl4dh5k1cbHTauWvX6pUaIdJnGzr-9Gz3peQjwyOGXB2Mg8AvAIEVu2RCVMcCmmMekMmAKALbjQckHc5Pw5PCaXcJ_tayJIrNiH3p3mJCR9Ch9nT6ZTGht6ic78wxXbjfKbOJ78OOaD_Sl1sBx1y7LbOd8-b1tPc4zwsQr-hoaPrsI4Uu3q89ym-J28bXGT_YXcekh_fLu7OL4vrm-_T89PrAgVAXzS1Ea6RWDnGBa-QVUYY1ZiyNg6kr1kthdQSS5B6XjkFsjGwXdlryUFJcUg-j3OXKT6tfO5tG7LziwV2Pq6yrUBpxTS8CplQRsmqHOCXEboUc06-scsUWkwby8Bui7f_FD_oT7uxq3nr6xe7a3rIizEPufd_XmJMv60uRans3ezWns3Ofl7xK2Fngz8aPbpsH-MqdUN7__35L4gdmFw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>13595487</pqid></control><display><type>article</type><title>Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro</title><source>MEDLINE</source><source>ACS Publications</source><creator>Kim, Kyu Won ; Roon, Robert J</creator><creatorcontrib>Kim, Kyu Won ; Roon, Robert J</creatorcontrib><description>Asparaginase II of Saccharomyces cerevisiae is a cell wall mannan containing glycoprotein. Recent studies have demonstrated that asparaginase II activity increases in exponentially growing cell cultures and then decreases as the cells enter the stationary phase. Enzyme inactivation has been attributed to a Zn2+-dependent protease which is synthesized de novo during the late exponential phase [Pauling, K.D., &amp; Jones, G.E. (1980) J. Gen. Microbiol. 117, 423-430; Pauling, K.D., &amp; Jones, G.E. (1980) Biochim. Biophys. Acta 616, 271-282]. We have investigated the mechanism of asparaginase II inactivation using both whole cell suspensions and highly purified enzyme. Our data indicate that the rate of asparaginase II inactivation in cell suspensions is primarily influenced by pH changes that occur as a consequence of cell growth and glucose fermentation and that enzyme inactivation is not dependent on Zn2+ or on de novo protein synthesis. Also, in vitro studies with purified enzyme show kinetics of inactivation that are similar to those observed in vivo. Consequently, involvement of a yeast protease in the inactivation process is relatively unlikely.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00280a018</identifier><identifier>PMID: 6347251</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>asparaginase ; Asparaginase - genetics ; Asparaginase - metabolism ; Drug Stability ; Kinetics ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics</subject><ispartof>Biochemistry (Easton), 1983-05, Vol.22 (11), p.2704-2707</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a300t-fd93cf4a8c12328a189395f97d9c04ed1d43464a7046b8c504f900a01e6420543</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00280a018$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00280a018$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6347251$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Kyu Won</creatorcontrib><creatorcontrib>Roon, Robert J</creatorcontrib><title>Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Asparaginase II of Saccharomyces cerevisiae is a cell wall mannan containing glycoprotein. Recent studies have demonstrated that asparaginase II activity increases in exponentially growing cell cultures and then decreases as the cells enter the stationary phase. Enzyme inactivation has been attributed to a Zn2+-dependent protease which is synthesized de novo during the late exponential phase [Pauling, K.D., &amp; Jones, G.E. (1980) J. Gen. Microbiol. 117, 423-430; Pauling, K.D., &amp; Jones, G.E. (1980) Biochim. Biophys. Acta 616, 271-282]. We have investigated the mechanism of asparaginase II inactivation using both whole cell suspensions and highly purified enzyme. Our data indicate that the rate of asparaginase II inactivation in cell suspensions is primarily influenced by pH changes that occur as a consequence of cell growth and glucose fermentation and that enzyme inactivation is not dependent on Zn2+ or on de novo protein synthesis. Also, in vitro studies with purified enzyme show kinetics of inactivation that are similar to those observed in vivo. Consequently, involvement of a yeast protease in the inactivation process is relatively unlikely.</description><subject>asparaginase</subject><subject>Asparaginase - genetics</subject><subject>Asparaginase - metabolism</subject><subject>Drug Stability</subject><subject>Kinetics</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0M9P2zAUB3ALbYKO7bTzJJ_GYQo8_0y8GyA2KpCoBLvsYl4dh5k1cbHTauWvX6pUaIdJnGzr-9Gz3peQjwyOGXB2Mg8AvAIEVu2RCVMcCmmMekMmAKALbjQckHc5Pw5PCaXcJ_tayJIrNiH3p3mJCR9Ch9nT6ZTGht6ic78wxXbjfKbOJ78OOaD_Sl1sBx1y7LbOd8-b1tPc4zwsQr-hoaPrsI4Uu3q89ym-J28bXGT_YXcekh_fLu7OL4vrm-_T89PrAgVAXzS1Ea6RWDnGBa-QVUYY1ZiyNg6kr1kthdQSS5B6XjkFsjGwXdlryUFJcUg-j3OXKT6tfO5tG7LziwV2Pq6yrUBpxTS8CplQRsmqHOCXEboUc06-scsUWkwby8Bui7f_FD_oT7uxq3nr6xe7a3rIizEPufd_XmJMv60uRans3ezWns3Ofl7xK2Fngz8aPbpsH-MqdUN7__35L4gdmFw</recordid><startdate>19830501</startdate><enddate>19830501</enddate><creator>Kim, Kyu Won</creator><creator>Roon, Robert J</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19830501</creationdate><title>Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro</title><author>Kim, Kyu Won ; Roon, Robert J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a300t-fd93cf4a8c12328a189395f97d9c04ed1d43464a7046b8c504f900a01e6420543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>asparaginase</topic><topic>Asparaginase - genetics</topic><topic>Asparaginase - metabolism</topic><topic>Drug Stability</topic><topic>Kinetics</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Kyu Won</creatorcontrib><creatorcontrib>Roon, Robert J</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Kyu Won</au><au>Roon, Robert J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1983-05-01</date><risdate>1983</risdate><volume>22</volume><issue>11</issue><spage>2704</spage><epage>2707</epage><pages>2704-2707</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Asparaginase II of Saccharomyces cerevisiae is a cell wall mannan containing glycoprotein. Recent studies have demonstrated that asparaginase II activity increases in exponentially growing cell cultures and then decreases as the cells enter the stationary phase. Enzyme inactivation has been attributed to a Zn2+-dependent protease which is synthesized de novo during the late exponential phase [Pauling, K.D., &amp; Jones, G.E. (1980) J. Gen. Microbiol. 117, 423-430; Pauling, K.D., &amp; Jones, G.E. (1980) Biochim. Biophys. Acta 616, 271-282]. We have investigated the mechanism of asparaginase II inactivation using both whole cell suspensions and highly purified enzyme. Our data indicate that the rate of asparaginase II inactivation in cell suspensions is primarily influenced by pH changes that occur as a consequence of cell growth and glucose fermentation and that enzyme inactivation is not dependent on Zn2+ or on de novo protein synthesis. Also, in vitro studies with purified enzyme show kinetics of inactivation that are similar to those observed in vivo. Consequently, involvement of a yeast protease in the inactivation process is relatively unlikely.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>6347251</pmid><doi>10.1021/bi00280a018</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2960
ispartof Biochemistry (Easton), 1983-05, Vol.22 (11), p.2704-2707
issn 0006-2960
1520-4995
language eng
recordid cdi_proquest_miscellaneous_80565160
source MEDLINE; ACS Publications
subjects asparaginase
Asparaginase - genetics
Asparaginase - metabolism
Drug Stability
Kinetics
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
title Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T09%3A26%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Asparaginase%20II%20of%20Saccharomyces%20cerevisiae:%20comparison%20of%20enzyme%20stability%20in%20vivo%20and%20in%20vitro&rft.jtitle=Biochemistry%20(Easton)&rft.au=Kim,%20Kyu%20Won&rft.date=1983-05-01&rft.volume=22&rft.issue=11&rft.spage=2704&rft.epage=2707&rft.pages=2704-2707&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00280a018&rft_dat=%3Cproquest_cross%3E13595487%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=13595487&rft_id=info:pmid/6347251&rfr_iscdi=true