Functional arginine residues involved in coenzyme binding by dihydrofolate reductase
Reaction of dihydrofolate reductase from amethopterin-resistant Lactobacillus casei with phenylglyoxal results in a complete loss of enzyme activity. This inactivation is concomitant with the modification of five of a total of eight arginine residues per mole of enzyme. In the presence of the reduce...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1976-02, Vol.68 (3), p.937-941 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Vehar, Gordon A. Freisheim, James H. |
| description | Reaction of dihydrofolate reductase from amethopterin-resistant
Lactobacillus
casei
with phenylglyoxal results in a complete loss of enzyme activity. This inactivation is concomitant with the modification of five of a total of eight arginine residues per mole of enzyme. In the presence of the reduced coenzyme, NADPH, two of the five reactive arginines are protected from chemical modification with complete retention of enzyme activity. The results suggest the involvement of essential arginine residues at or near the coenzyme binding site and thus at or near the active center of the enzyme. |
| doi_str_mv | 10.1016/0006-291X(76)91235-3 |
| format | Article |
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Lactobacillus
casei
with phenylglyoxal results in a complete loss of enzyme activity. This inactivation is concomitant with the modification of five of a total of eight arginine residues per mole of enzyme. In the presence of the reduced coenzyme, NADPH, two of the five reactive arginines are protected from chemical modification with complete retention of enzyme activity. The results suggest the involvement of essential arginine residues at or near the coenzyme binding site and thus at or near the active center of the enzyme.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(76)91235-3</identifier><identifier>PMID: 816356</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Arginine - analysis ; Binding Sites ; Drug Resistance, Microbial ; Glyoxal ; Kinetics ; Lactobacillus casei - drug effects ; Lactobacillus casei - metabolism ; Methotrexate - pharmacology ; Protein Binding ; Tetrahydrofolate Dehydrogenase - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1976-02, Vol.68 (3), p.937-941</ispartof><rights>1976</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-cf740f5cad472eb777fb0690a59d7ad79601b997e48780e61d0c0b863d2e3d783</citedby><cites>FETCH-LOGICAL-c356t-cf740f5cad472eb777fb0690a59d7ad79601b997e48780e61d0c0b863d2e3d783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(76)91235-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/816356$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vehar, Gordon A.</creatorcontrib><creatorcontrib>Freisheim, James H.</creatorcontrib><title>Functional arginine residues involved in coenzyme binding by dihydrofolate reductase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Reaction of dihydrofolate reductase from amethopterin-resistant
Lactobacillus
casei
with phenylglyoxal results in a complete loss of enzyme activity. This inactivation is concomitant with the modification of five of a total of eight arginine residues per mole of enzyme. In the presence of the reduced coenzyme, NADPH, two of the five reactive arginines are protected from chemical modification with complete retention of enzyme activity. The results suggest the involvement of essential arginine residues at or near the coenzyme binding site and thus at or near the active center of the enzyme.</description><subject>Arginine - analysis</subject><subject>Binding Sites</subject><subject>Drug Resistance, Microbial</subject><subject>Glyoxal</subject><subject>Kinetics</subject><subject>Lactobacillus casei - drug effects</subject><subject>Lactobacillus casei - metabolism</subject><subject>Methotrexate - pharmacology</subject><subject>Protein Binding</subject><subject>Tetrahydrofolate Dehydrogenase - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoP4Vav_wMOeRA-rk8022VwEKX6B4KWCt5BNZmtkm9Rkt1B_vVsrPXqagXnfd2YeQs4pXFOg_AYAeF5I-n4p-JWkBZvkbI-MKEjICwrlPhntJMfkJKVPAEpLLo_IYUU5m_ARmT303nQueN1mOs6ddx6ziMnZHlPm_Cq0K7RDk5mA_nu9wKx23jo_z-p1Zt3H2sbQhFZ3G5vtTacTnpKDRrcJz_7qmLw93M-mT_nL6-Pz9O4lN8PuLjeNKKGZGG1LUWAthGhq4BL0RFqhrZAcaC2lwLISFSCnFgzUFWe2QGZFxcbkYpu7jOFruLdTC5cMtq32GPqkKsZ4IQQdhOVWaGJIKWKjltEtdFwrCmrDUm1AqQ0oJbj6ZanYYDv_y-_rBdqdaQtvGN9uxzj8uHIYVTIOvUHrIppO2eD-z_8BXGyEeQ</recordid><startdate>19760209</startdate><enddate>19760209</enddate><creator>Vehar, Gordon A.</creator><creator>Freisheim, James H.</creator><general>Elsevier Inc</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>19760209</creationdate><title>Functional arginine residues involved in coenzyme binding by dihydrofolate reductase</title><author>Vehar, Gordon A. ; Freisheim, James H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-cf740f5cad472eb777fb0690a59d7ad79601b997e48780e61d0c0b863d2e3d783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Arginine - analysis</topic><topic>Binding Sites</topic><topic>Drug Resistance, Microbial</topic><topic>Glyoxal</topic><topic>Kinetics</topic><topic>Lactobacillus casei - drug effects</topic><topic>Lactobacillus casei - metabolism</topic><topic>Methotrexate - pharmacology</topic><topic>Protein Binding</topic><topic>Tetrahydrofolate Dehydrogenase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vehar, Gordon A.</creatorcontrib><creatorcontrib>Freisheim, James H.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vehar, Gordon A.</au><au>Freisheim, James H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional arginine residues involved in coenzyme binding by dihydrofolate reductase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1976-02-09</date><risdate>1976</risdate><volume>68</volume><issue>3</issue><spage>937</spage><epage>941</epage><pages>937-941</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Reaction of dihydrofolate reductase from amethopterin-resistant
Lactobacillus
casei
with phenylglyoxal results in a complete loss of enzyme activity. This inactivation is concomitant with the modification of five of a total of eight arginine residues per mole of enzyme. In the presence of the reduced coenzyme, NADPH, two of the five reactive arginines are protected from chemical modification with complete retention of enzyme activity. The results suggest the involvement of essential arginine residues at or near the coenzyme binding site and thus at or near the active center of the enzyme.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>816356</pmid><doi>10.1016/0006-291X(76)91235-3</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1976-02, Vol.68 (3), p.937-941 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_83362771 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Arginine - analysis Binding Sites Drug Resistance, Microbial Glyoxal Kinetics Lactobacillus casei - drug effects Lactobacillus casei - metabolism Methotrexate - pharmacology Protein Binding Tetrahydrofolate Dehydrogenase - metabolism |
| title | Functional arginine residues involved in coenzyme binding by dihydrofolate reductase |
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