Genetic Blocks and Unique Features in the Biosynthesis of 5'-Phosphoribosyl-N-formylglycinamide in Salmonella typhimurium
Purine-requiring mutants of Salmonella typhimurium have been examined for the ability to synthesize 5'-phosphoribosyl- N -formylglycinamide in a coupled reaction involving the first three enzymes of the biosynthetic pathway for purine nucleotides. Extracts prepared from mutants belonging to the...
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| Veröffentlicht in: | The Journal of biological chemistry 1969-04, Vol.244 (8), p.2095-2102 |
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| creator | Westby, C A Gots, J S |
| description | Purine-requiring mutants of Salmonella typhimurium have been examined for the ability to synthesize 5'-phosphoribosyl- N -formylglycinamide in a coupled reaction involving the first three enzymes of the biosynthetic pathway for purine nucleotides.
Extracts prepared from mutants belonging to the distinct genetic classes, pur F and pur D , were inactive in this assay but were active when mixed together. Further analysis showed that pur F mutants were deficient in the first enzyme, 5-phosphoribosyl 1-pyrophosphate amidotransferase (ribosylamine-5-phosphate:pyrophosphate
phosphoribosyltransferase, EC 2.4.2.14), and pur D mutants were apparently deficient in the second enzyme, phosphoribosylglycinamide synthetase (ribosylamine-5-phosphate:glycine
ligase, EC 6.3.1.3). The third enzyme, phosphoribosylglycinamide formyltransferase (5'-phosphoribosyl- N -formylglycineamide:tetrahydrofolate 5,10-formyltransferase, EC 2.1.2.2), was present in all mutants, and a genetic deficiency
for this enzyme has not been found. Attempts to limit the action of this enzyme by creating folate deficiencies were unsuccessful.
This and other considerations suggest a uniqueness in the formyltransferase system different from the equivalent nonbacterial
systems. |
| doi_str_mv | 10.1016/S0021-9258(18)94371-1 |
| format | Article |
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Extracts prepared from mutants belonging to the distinct genetic classes, pur F and pur D , were inactive in this assay but were active when mixed together. Further analysis showed that pur F mutants were deficient in the first enzyme, 5-phosphoribosyl 1-pyrophosphate amidotransferase (ribosylamine-5-phosphate:pyrophosphate
phosphoribosyltransferase, EC 2.4.2.14), and pur D mutants were apparently deficient in the second enzyme, phosphoribosylglycinamide synthetase (ribosylamine-5-phosphate:glycine
ligase, EC 6.3.1.3). The third enzyme, phosphoribosylglycinamide formyltransferase (5'-phosphoribosyl- N -formylglycineamide:tetrahydrofolate 5,10-formyltransferase, EC 2.1.2.2), was present in all mutants, and a genetic deficiency
for this enzyme has not been found. Attempts to limit the action of this enzyme by creating folate deficiencies were unsuccessful.
This and other considerations suggest a uniqueness in the formyltransferase system different from the equivalent nonbacterial
systems.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)94371-1</identifier><identifier>PMID: 4889464</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amides - biosynthesis ; Amino Acids - biosynthesis ; Cell-Free System ; Chromatography, Ion Exchange ; Folic Acid ; Formates - biosynthesis ; Genetics, Microbial ; Glycine ; Ligases - metabolism ; Mutation ; Nucleotides - biosynthesis ; Pentosephosphates ; Purines - biosynthesis ; Salmonella typhimurium - enzymology ; Salmonella typhimurium - metabolism ; Transferases - metabolism</subject><ispartof>The Journal of biological chemistry, 1969-04, Vol.244 (8), p.2095-2102</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-e85e007277f6c878abba2cd854616421ddd9b7960add1480f6bfe35cd7aa817c3</citedby><cites>FETCH-LOGICAL-c378t-e85e007277f6c878abba2cd854616421ddd9b7960add1480f6bfe35cd7aa817c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4889464$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Westby, C A</creatorcontrib><creatorcontrib>Gots, J S</creatorcontrib><title>Genetic Blocks and Unique Features in the Biosynthesis of 5'-Phosphoribosyl-N-formylglycinamide in Salmonella typhimurium</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Purine-requiring mutants of Salmonella typhimurium have been examined for the ability to synthesize 5'-phosphoribosyl- N -formylglycinamide in a coupled reaction involving the first three enzymes of the biosynthetic pathway for purine nucleotides.
Extracts prepared from mutants belonging to the distinct genetic classes, pur F and pur D , were inactive in this assay but were active when mixed together. Further analysis showed that pur F mutants were deficient in the first enzyme, 5-phosphoribosyl 1-pyrophosphate amidotransferase (ribosylamine-5-phosphate:pyrophosphate
phosphoribosyltransferase, EC 2.4.2.14), and pur D mutants were apparently deficient in the second enzyme, phosphoribosylglycinamide synthetase (ribosylamine-5-phosphate:glycine
ligase, EC 6.3.1.3). The third enzyme, phosphoribosylglycinamide formyltransferase (5'-phosphoribosyl- N -formylglycineamide:tetrahydrofolate 5,10-formyltransferase, EC 2.1.2.2), was present in all mutants, and a genetic deficiency
for this enzyme has not been found. Attempts to limit the action of this enzyme by creating folate deficiencies were unsuccessful.
This and other considerations suggest a uniqueness in the formyltransferase system different from the equivalent nonbacterial
systems.</description><subject>Amides - biosynthesis</subject><subject>Amino Acids - biosynthesis</subject><subject>Cell-Free System</subject><subject>Chromatography, Ion Exchange</subject><subject>Folic Acid</subject><subject>Formates - biosynthesis</subject><subject>Genetics, Microbial</subject><subject>Glycine</subject><subject>Ligases - metabolism</subject><subject>Mutation</subject><subject>Nucleotides - biosynthesis</subject><subject>Pentosephosphates</subject><subject>Purines - biosynthesis</subject><subject>Salmonella typhimurium - enzymology</subject><subject>Salmonella typhimurium - metabolism</subject><subject>Transferases - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1969</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kM1u1TAQhS0EKpfCI1SyWABdGDyJEztLWtGCVAFSqcTOcuxJY4jji50I5e2b9F7Vm7F0zpmfj5Az4B-BQ_3plvMCWFNU6gOo80aUEhg8IzvgqmRlBb-fk92T5SV5lfMfvj7RwAk5EUo1ohY7slzjiJO39GKI9m-mZnT0bvT_ZqRXaKY5YaZ-pFOP9MLHvIzrL_tMY0er9-xnH_O-j8m3qzSw76yLKSzD_bBYP5rgHW7hWzOEOOIwGDot-96HOfk5vCYvOjNkfHOsp-Tu6suvy6_s5sf1t8vPN8yWUk0MVYWcy0LKrrZKKtO2prBOVaKGWhTgnGta2dTcOAdC8a5uOywr66QxCqQtT8m7Q999iutZedLBZ7ttM2Kcs1ZijdUSVmN1MNoUc07Y6X3ywaRFA9cbcv2IXG88NSj9iFxvubPjgLkN6J5SR8ar_vag9_6-_-8T6tZH22PQhRBa6YI3VfkASh-KWA</recordid><startdate>19690425</startdate><enddate>19690425</enddate><creator>Westby, C A</creator><creator>Gots, J S</creator><general>American Society for Biochemistry and Molecular Biology</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>19690425</creationdate><title>Genetic Blocks and Unique Features in the Biosynthesis of 5'-Phosphoribosyl-N-formylglycinamide in Salmonella typhimurium</title><author>Westby, C A ; Gots, J S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-e85e007277f6c878abba2cd854616421ddd9b7960add1480f6bfe35cd7aa817c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1969</creationdate><topic>Amides - biosynthesis</topic><topic>Amino Acids - biosynthesis</topic><topic>Cell-Free System</topic><topic>Chromatography, Ion Exchange</topic><topic>Folic Acid</topic><topic>Formates - biosynthesis</topic><topic>Genetics, Microbial</topic><topic>Glycine</topic><topic>Ligases - metabolism</topic><topic>Mutation</topic><topic>Nucleotides - biosynthesis</topic><topic>Pentosephosphates</topic><topic>Purines - biosynthesis</topic><topic>Salmonella typhimurium - enzymology</topic><topic>Salmonella typhimurium - metabolism</topic><topic>Transferases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Westby, C A</creatorcontrib><creatorcontrib>Gots, J S</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Westby, C A</au><au>Gots, J S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genetic Blocks and Unique Features in the Biosynthesis of 5'-Phosphoribosyl-N-formylglycinamide in Salmonella typhimurium</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1969-04-25</date><risdate>1969</risdate><volume>244</volume><issue>8</issue><spage>2095</spage><epage>2102</epage><pages>2095-2102</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Purine-requiring mutants of Salmonella typhimurium have been examined for the ability to synthesize 5'-phosphoribosyl- N -formylglycinamide in a coupled reaction involving the first three enzymes of the biosynthetic pathway for purine nucleotides.
Extracts prepared from mutants belonging to the distinct genetic classes, pur F and pur D , were inactive in this assay but were active when mixed together. Further analysis showed that pur F mutants were deficient in the first enzyme, 5-phosphoribosyl 1-pyrophosphate amidotransferase (ribosylamine-5-phosphate:pyrophosphate
phosphoribosyltransferase, EC 2.4.2.14), and pur D mutants were apparently deficient in the second enzyme, phosphoribosylglycinamide synthetase (ribosylamine-5-phosphate:glycine
ligase, EC 6.3.1.3). The third enzyme, phosphoribosylglycinamide formyltransferase (5'-phosphoribosyl- N -formylglycineamide:tetrahydrofolate 5,10-formyltransferase, EC 2.1.2.2), was present in all mutants, and a genetic deficiency
for this enzyme has not been found. Attempts to limit the action of this enzyme by creating folate deficiencies were unsuccessful.
This and other considerations suggest a uniqueness in the formyltransferase system different from the equivalent nonbacterial
systems.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>4889464</pmid><doi>10.1016/S0021-9258(18)94371-1</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1969-04, Vol.244 (8), p.2095-2102 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84148671 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amides - biosynthesis Amino Acids - biosynthesis Cell-Free System Chromatography, Ion Exchange Folic Acid Formates - biosynthesis Genetics, Microbial Glycine Ligases - metabolism Mutation Nucleotides - biosynthesis Pentosephosphates Purines - biosynthesis Salmonella typhimurium - enzymology Salmonella typhimurium - metabolism Transferases - metabolism |
| title | Genetic Blocks and Unique Features in the Biosynthesis of 5'-Phosphoribosyl-N-formylglycinamide in Salmonella typhimurium |
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