Enzymatic biosynthesis of cephalexin
The reaction kinetics of the enzymatic of cephalexin from 7‐aminodea‐cetoxy cephalosporanic acid and phenylglycine methylester was studied using the synthesizing enzyme obtained from Xanthomonas citri. The activation energy, Km value for 7‐aminodeacetoxy cephalosporanic acid and phenylglycine methyl...
Gespeichert in:
| Veröffentlicht in: | Biotechnology and bioengineering 1980-06, Vol.22 (6), p.1237-1247 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1247 |
|---|---|
| container_issue | 6 |
| container_start_page | 1237 |
| container_title | Biotechnology and bioengineering |
| container_volume | 22 |
| creator | Rhee, D. K. Lee, S. B. Rhee, J. S. Ryu, Dewey D. Y. Hospodka, J. |
| description | The reaction kinetics of the enzymatic of cephalexin from 7‐aminodea‐cetoxy cephalosporanic acid and phenylglycine methylester was studied using the synthesizing enzyme obtained from Xanthomonas citri. The activation energy, Km value for 7‐aminodeacetoxy cephalosporanic acid and phenylglycine methylester, and Ki value for phenylglycine methylester were determined as 8.63 kcal/mol, 3.7mM, 14.5mM, and 70mM, respectively. The enzyme was found to be constitutive and susceptible to deactivation. |
| doi_str_mv | 10.1002/bit.260220610 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75118957</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>75118957</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4400-5827130f945204d83b075019b2a910e53e8a9af224f031e95a3cabdf04ecb0523</originalsourceid><addsrcrecordid>eNp9kE1Lw0AQhhdRaq0ePQo9iLfU2d1sNnvU0tZCUSqVHpdNOqGr-ajZBBt_vZGG4snTMLzPPAwvIdcURhSA3Ue2GrEAGIOAwgnpU1DSA6bglPQBIPC4UOycXDj33q4yDIIe6UkuQyFkn9xO8u8mM5WNh5EtXJNXW3TWDYtkGONua1Lc2_ySnCUmdXjVzQF5m05W4ydv8TKbjx8WXuz7AJ4ImaQcEuULBv4m5BFIAVRFzCgKKDiGRpmEMT8BTlEJw2MTbRLwMY5AMD4gdwfvriw-a3SVzqyLMU1NjkXttBSUhkrIFvQOYFwWzpWY6F1pM1M2moL-bUW3rehjKy1_04nrKMPNke5qaHN5yL9sis3_Mv04X_01d59YV-H-eGnKDx20dqHXzzMt1kBfl9OlXvMf73V6qQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>75118957</pqid></control><display><type>article</type><title>Enzymatic biosynthesis of cephalexin</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Rhee, D. K. ; Lee, S. B. ; Rhee, J. S. ; Ryu, Dewey D. Y. ; Hospodka, J.</creator><creatorcontrib>Rhee, D. K. ; Lee, S. B. ; Rhee, J. S. ; Ryu, Dewey D. Y. ; Hospodka, J.</creatorcontrib><description>The reaction kinetics of the enzymatic of cephalexin from 7‐aminodea‐cetoxy cephalosporanic acid and phenylglycine methylester was studied using the synthesizing enzyme obtained from Xanthomonas citri. The activation energy, Km value for 7‐aminodeacetoxy cephalosporanic acid and phenylglycine methylester, and Ki value for phenylglycine methylester were determined as 8.63 kcal/mol, 3.7mM, 14.5mM, and 70mM, respectively. The enzyme was found to be constitutive and susceptible to deactivation.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260220610</identifier><identifier>PMID: 7378557</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amidohydrolases - metabolism ; Benzoates - pharmacology ; Cephalexin - biosynthesis ; Enzyme Induction ; Kinetics ; Oxygen - pharmacology ; Penicillin Amidase - biosynthesis ; Penicillin Amidase - metabolism ; Phenylacetates - pharmacology ; Xanthomonas - enzymology</subject><ispartof>Biotechnology and bioengineering, 1980-06, Vol.22 (6), p.1237-1247</ispartof><rights>Copyright © 1980 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4400-5827130f945204d83b075019b2a910e53e8a9af224f031e95a3cabdf04ecb0523</citedby><cites>FETCH-LOGICAL-c4400-5827130f945204d83b075019b2a910e53e8a9af224f031e95a3cabdf04ecb0523</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbit.260220610$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.260220610$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7378557$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rhee, D. K.</creatorcontrib><creatorcontrib>Lee, S. B.</creatorcontrib><creatorcontrib>Rhee, J. S.</creatorcontrib><creatorcontrib>Ryu, Dewey D. Y.</creatorcontrib><creatorcontrib>Hospodka, J.</creatorcontrib><title>Enzymatic biosynthesis of cephalexin</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>The reaction kinetics of the enzymatic of cephalexin from 7‐aminodea‐cetoxy cephalosporanic acid and phenylglycine methylester was studied using the synthesizing enzyme obtained from Xanthomonas citri. The activation energy, Km value for 7‐aminodeacetoxy cephalosporanic acid and phenylglycine methylester, and Ki value for phenylglycine methylester were determined as 8.63 kcal/mol, 3.7mM, 14.5mM, and 70mM, respectively. The enzyme was found to be constitutive and susceptible to deactivation.</description><subject>Amidohydrolases - metabolism</subject><subject>Benzoates - pharmacology</subject><subject>Cephalexin - biosynthesis</subject><subject>Enzyme Induction</subject><subject>Kinetics</subject><subject>Oxygen - pharmacology</subject><subject>Penicillin Amidase - biosynthesis</subject><subject>Penicillin Amidase - metabolism</subject><subject>Phenylacetates - pharmacology</subject><subject>Xanthomonas - enzymology</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AQhhdRaq0ePQo9iLfU2d1sNnvU0tZCUSqVHpdNOqGr-ajZBBt_vZGG4snTMLzPPAwvIdcURhSA3Ue2GrEAGIOAwgnpU1DSA6bglPQBIPC4UOycXDj33q4yDIIe6UkuQyFkn9xO8u8mM5WNh5EtXJNXW3TWDYtkGONua1Lc2_ySnCUmdXjVzQF5m05W4ydv8TKbjx8WXuz7AJ4ImaQcEuULBv4m5BFIAVRFzCgKKDiGRpmEMT8BTlEJw2MTbRLwMY5AMD4gdwfvriw-a3SVzqyLMU1NjkXttBSUhkrIFvQOYFwWzpWY6F1pM1M2moL-bUW3rehjKy1_04nrKMPNke5qaHN5yL9sis3_Mv04X_01d59YV-H-eGnKDx20dqHXzzMt1kBfl9OlXvMf73V6qQ</recordid><startdate>198006</startdate><enddate>198006</enddate><creator>Rhee, D. K.</creator><creator>Lee, S. B.</creator><creator>Rhee, J. S.</creator><creator>Ryu, Dewey D. Y.</creator><creator>Hospodka, J.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</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>7X8</scope></search><sort><creationdate>198006</creationdate><title>Enzymatic biosynthesis of cephalexin</title><author>Rhee, D. K. ; Lee, S. B. ; Rhee, J. S. ; Ryu, Dewey D. Y. ; Hospodka, J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4400-5827130f945204d83b075019b2a910e53e8a9af224f031e95a3cabdf04ecb0523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Amidohydrolases - metabolism</topic><topic>Benzoates - pharmacology</topic><topic>Cephalexin - biosynthesis</topic><topic>Enzyme Induction</topic><topic>Kinetics</topic><topic>Oxygen - pharmacology</topic><topic>Penicillin Amidase - biosynthesis</topic><topic>Penicillin Amidase - metabolism</topic><topic>Phenylacetates - pharmacology</topic><topic>Xanthomonas - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rhee, D. K.</creatorcontrib><creatorcontrib>Lee, S. B.</creatorcontrib><creatorcontrib>Rhee, J. S.</creatorcontrib><creatorcontrib>Ryu, Dewey D. Y.</creatorcontrib><creatorcontrib>Hospodka, 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>MEDLINE - Academic</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rhee, D. K.</au><au>Lee, S. B.</au><au>Rhee, J. S.</au><au>Ryu, Dewey D. Y.</au><au>Hospodka, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic biosynthesis of cephalexin</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1980-06</date><risdate>1980</risdate><volume>22</volume><issue>6</issue><spage>1237</spage><epage>1247</epage><pages>1237-1247</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><abstract>The reaction kinetics of the enzymatic of cephalexin from 7‐aminodea‐cetoxy cephalosporanic acid and phenylglycine methylester was studied using the synthesizing enzyme obtained from Xanthomonas citri. The activation energy, Km value for 7‐aminodeacetoxy cephalosporanic acid and phenylglycine methylester, and Ki value for phenylglycine methylester were determined as 8.63 kcal/mol, 3.7mM, 14.5mM, and 70mM, respectively. The enzyme was found to be constitutive and susceptible to deactivation.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>7378557</pmid><doi>10.1002/bit.260220610</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3592 |
| ispartof | Biotechnology and bioengineering, 1980-06, Vol.22 (6), p.1237-1247 |
| issn | 0006-3592 1097-0290 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75118957 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amidohydrolases - metabolism Benzoates - pharmacology Cephalexin - biosynthesis Enzyme Induction Kinetics Oxygen - pharmacology Penicillin Amidase - biosynthesis Penicillin Amidase - metabolism Phenylacetates - pharmacology Xanthomonas - enzymology |
| title | Enzymatic biosynthesis of cephalexin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T16%3A33%3A47IST&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=Enzymatic%20biosynthesis%20of%20cephalexin&rft.jtitle=Biotechnology%20and%20bioengineering&rft.au=Rhee,%20D.%20K.&rft.date=1980-06&rft.volume=22&rft.issue=6&rft.spage=1237&rft.epage=1247&rft.pages=1237-1247&rft.issn=0006-3592&rft.eissn=1097-0290&rft_id=info:doi/10.1002/bit.260220610&rft_dat=%3Cproquest_cross%3E75118957%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=75118957&rft_id=info:pmid/7378557&rfr_iscdi=true |