The mechanism of aminoacylation of transfer ribonucleic acid. Reactivity of enzyme-bound isoleucyl adenylate
Isoleucyl adenylate bound to isoleucine:tRNA ligase of Escherichia coli (EC 6.1.1.5; isoleucyl-tRNA synthetase) transfers the isoleucine moiety to tRNA-Ile-E. coli with a half-time of about 35 s at 0 degrees and pH 7.6 in the presence of spermine or Mg2+. If a limited amount of tRNA-Ile is supplied...
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| Veröffentlicht in: | The Journal of biological chemistry 1975-05, Vol.250 (10), p.3854-3860 |
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| container_end_page | 3860 |
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| container_issue | 10 |
| container_start_page | 3854 |
| container_title | The Journal of biological chemistry |
| container_volume | 250 |
| creator | Lõvgren, T N Heinonen, J Loftfield, R B |
| description | Isoleucyl adenylate bound to isoleucine:tRNA ligase of Escherichia coli (EC 6.1.1.5; isoleucyl-tRNA synthetase) transfers
the isoleucine moiety to tRNA-Ile-E. coli with a half-time of about 35 s at 0 degrees and pH 7.6 in the presence of spermine
or Mg2+. If a limited amount of tRNA-Ile is supplied to a mixture of free enzyme and enzyme-bound [14c]isoleucyl adenylate
in a medium containing spermine, ATP, and [3H]isoleucine, almost none of the resultant isoleucyl tRNA is derived from preformed
enzyme-bound [14C]isoleucyl adenylate. Almost all of the isoleucyl tRNA formed results directly from reaction of free enzyme,
ATP, and isoleucine with tRNA. Similar but less clearcut results are obtained when Mg2+ is substituted for spermine. We conclude
that isoleucyl adenylate bound to isoleucine:tRNA ligase is not a significant intermediate in the synthesis of isoleucyl tRNA
under these conditions. |
| doi_str_mv | 10.1016/S0021-9258(19)41476-2 |
| format | Article |
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the isoleucine moiety to tRNA-Ile-E. coli with a half-time of about 35 s at 0 degrees and pH 7.6 in the presence of spermine
or Mg2+. If a limited amount of tRNA-Ile is supplied to a mixture of free enzyme and enzyme-bound [14c]isoleucyl adenylate
in a medium containing spermine, ATP, and [3H]isoleucine, almost none of the resultant isoleucyl tRNA is derived from preformed
enzyme-bound [14C]isoleucyl adenylate. Almost all of the isoleucyl tRNA formed results directly from reaction of free enzyme,
ATP, and isoleucine with tRNA. Similar but less clearcut results are obtained when Mg2+ is substituted for spermine. We conclude
that isoleucyl adenylate bound to isoleucine:tRNA ligase is not a significant intermediate in the synthesis of isoleucyl tRNA
under these conditions.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)41476-2</identifier><identifier>PMID: 1092679</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Monophosphate ; Amino Acyl-tRNA Synthetases - isolation & purification ; Amino Acyl-tRNA Synthetases - metabolism ; Binding Sites ; Binding, Competitive ; Chromatography ; Escherichia coli - enzymology ; Isoleucine-tRNA Ligase - metabolism ; Kinetics ; Magnesium - pharmacology ; Protein Binding ; Spermine - pharmacology ; Transfer RNA Aminoacylation</subject><ispartof>The Journal of biological chemistry, 1975-05, Vol.250 (10), p.3854-3860</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-e0b851a305a123b70f2a3de49ee5d8089ce3e381652094a9a45c1dfbecc627123</citedby><cites>FETCH-LOGICAL-c379t-e0b851a305a123b70f2a3de49ee5d8089ce3e381652094a9a45c1dfbecc627123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1092679$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lõvgren, T N</creatorcontrib><creatorcontrib>Heinonen, J</creatorcontrib><creatorcontrib>Loftfield, R B</creatorcontrib><title>The mechanism of aminoacylation of transfer ribonucleic acid. Reactivity of enzyme-bound isoleucyl adenylate</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Isoleucyl adenylate bound to isoleucine:tRNA ligase of Escherichia coli (EC 6.1.1.5; isoleucyl-tRNA synthetase) transfers
the isoleucine moiety to tRNA-Ile-E. coli with a half-time of about 35 s at 0 degrees and pH 7.6 in the presence of spermine
or Mg2+. If a limited amount of tRNA-Ile is supplied to a mixture of free enzyme and enzyme-bound [14c]isoleucyl adenylate
in a medium containing spermine, ATP, and [3H]isoleucine, almost none of the resultant isoleucyl tRNA is derived from preformed
enzyme-bound [14C]isoleucyl adenylate. Almost all of the isoleucyl tRNA formed results directly from reaction of free enzyme,
ATP, and isoleucine with tRNA. Similar but less clearcut results are obtained when Mg2+ is substituted for spermine. We conclude
that isoleucyl adenylate bound to isoleucine:tRNA ligase is not a significant intermediate in the synthesis of isoleucyl tRNA
under these conditions.</description><subject>Adenosine Monophosphate</subject><subject>Amino Acyl-tRNA Synthetases - isolation & purification</subject><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Chromatography</subject><subject>Escherichia coli - enzymology</subject><subject>Isoleucine-tRNA Ligase - metabolism</subject><subject>Kinetics</subject><subject>Magnesium - pharmacology</subject><subject>Protein Binding</subject><subject>Spermine - pharmacology</subject><subject>Transfer RNA Aminoacylation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkE1r3DAQhkVoSDeb_ISAoVCag7caybKlYwlNWlgIJCnkJmR5HCvYUirZDZtfn_XuUjKXgXk_Bh5CLoCugEL5_Z5SBrliQn4DdVlAUZU5OyILoJLnXMDjJ7L4b_lMTlN6ptspFJyQE6CKlZVakP6hw2xA2xnv0pCFNjOD88HYTW9GF_x8GaPxqcWYRVcHP9kenc2Mdc0qu0NjR_fPjZvZiP5tM2Beh8k3mUuhx2nbk5kG_VyHZ-S4NX3C88Nekj_XPx-ufuXr25vfVz_WueWVGnOktRRgOBUGGK8r2jLDGywUomgklcoiRy6hFIyqwihTCAtNW6O1Jau2kSX5uu99ieHvhGnUg0sW-954DFPSkkkQsDOKvdHGkFLEVr9EN5i40UD1TFnvKOsZoQald5T1nLs4PJjqAZsPqR3Wrf5lr3fuqXt1EXXtgu1w0EzMxZpLUfB3AkaFdw</recordid><startdate>19750525</startdate><enddate>19750525</enddate><creator>Lõvgren, T N</creator><creator>Heinonen, J</creator><creator>Loftfield, R B</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>19750525</creationdate><title>The mechanism of aminoacylation of transfer ribonucleic acid. Reactivity of enzyme-bound isoleucyl adenylate</title><author>Lõvgren, T N ; Heinonen, J ; Loftfield, R B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-e0b851a305a123b70f2a3de49ee5d8089ce3e381652094a9a45c1dfbecc627123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Adenosine Monophosphate</topic><topic>Amino Acyl-tRNA Synthetases - isolation & purification</topic><topic>Amino Acyl-tRNA Synthetases - metabolism</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Chromatography</topic><topic>Escherichia coli - enzymology</topic><topic>Isoleucine-tRNA Ligase - metabolism</topic><topic>Kinetics</topic><topic>Magnesium - pharmacology</topic><topic>Protein Binding</topic><topic>Spermine - pharmacology</topic><topic>Transfer RNA Aminoacylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lõvgren, T N</creatorcontrib><creatorcontrib>Heinonen, J</creatorcontrib><creatorcontrib>Loftfield, R B</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>Lõvgren, T N</au><au>Heinonen, J</au><au>Loftfield, R B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The mechanism of aminoacylation of transfer ribonucleic acid. Reactivity of enzyme-bound isoleucyl adenylate</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1975-05-25</date><risdate>1975</risdate><volume>250</volume><issue>10</issue><spage>3854</spage><epage>3860</epage><pages>3854-3860</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Isoleucyl adenylate bound to isoleucine:tRNA ligase of Escherichia coli (EC 6.1.1.5; isoleucyl-tRNA synthetase) transfers
the isoleucine moiety to tRNA-Ile-E. coli with a half-time of about 35 s at 0 degrees and pH 7.6 in the presence of spermine
or Mg2+. If a limited amount of tRNA-Ile is supplied to a mixture of free enzyme and enzyme-bound [14c]isoleucyl adenylate
in a medium containing spermine, ATP, and [3H]isoleucine, almost none of the resultant isoleucyl tRNA is derived from preformed
enzyme-bound [14C]isoleucyl adenylate. Almost all of the isoleucyl tRNA formed results directly from reaction of free enzyme,
ATP, and isoleucine with tRNA. Similar but less clearcut results are obtained when Mg2+ is substituted for spermine. We conclude
that isoleucyl adenylate bound to isoleucine:tRNA ligase is not a significant intermediate in the synthesis of isoleucyl tRNA
under these conditions.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1092679</pmid><doi>10.1016/S0021-9258(19)41476-2</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1975-05, Vol.250 (10), p.3854-3860 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82815112 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Adenosine Monophosphate Amino Acyl-tRNA Synthetases - isolation & purification Amino Acyl-tRNA Synthetases - metabolism Binding Sites Binding, Competitive Chromatography Escherichia coli - enzymology Isoleucine-tRNA Ligase - metabolism Kinetics Magnesium - pharmacology Protein Binding Spermine - pharmacology Transfer RNA Aminoacylation |
| title | The mechanism of aminoacylation of transfer ribonucleic acid. Reactivity of enzyme-bound isoleucyl adenylate |
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