The Divergence in Reactivity of Aminoacyl Transfer Ribonucleic Acid Synthetases of Escherichia coli with Hydroxylamine
Fourteen partially purified Escherichia coli aminoacyl transfer ribonucleic acid synthetases were tested for their rates of amino acid hydroxamate formation relative to the rates of aminoacyl-tRNA formation. Three groups of reactivity were observed: tyrosyl-, phenylalanyl-, tryptophanyl-, and methio...
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| Veröffentlicht in: | The Journal of biological chemistry 1968-11, Vol.243 (21), p.5724-5730 |
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| container_title | The Journal of biological chemistry |
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| creator | Hirsh, D I Lipmann, F |
| description | Fourteen partially purified Escherichia coli aminoacyl transfer ribonucleic acid synthetases were tested for their rates of amino acid hydroxamate formation relative
to the rates of aminoacyl-tRNA formation. Three groups of reactivity were observed: tyrosyl-, phenylalanyl-, tryptophanyl-,
and methionyl-tRNA synthetases catalyze hydroxamate formation at rates comparable to those for aminoacyl-tRNA formation; with
lysyl-, alanyl-, isoleucyl-, glycyl-, cysteinyl-, leucyl-, seryl-, and valyl-tRNA synthetases, the relative rates of hydroxamate
formation progressively decrease; and glutaminyl- and threonyl-tRNA synthetases do not catalyze hydroxamate formation. In
an unfractionated enzyme extract, threonine hydroxamate forms, but this is totally accounted for by the mistaken activation
of threonine by the valyl-tRNA synthetase. Purified threonyl-tRNA synthetase catalyzes hydroxamate formation only when tRNA
is present, by catalyzing the formation of threonyl-tRNA, which reacts nonenzymatically with hydroxylamine. The mammalian
threonyl-tRNA synthetase also fails to catalyze formation of threonine hydroxamate from amino acid and ATP. |
| doi_str_mv | 10.1016/S0021-9258(18)91925-3 |
| format | Article |
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to the rates of aminoacyl-tRNA formation. Three groups of reactivity were observed: tyrosyl-, phenylalanyl-, tryptophanyl-,
and methionyl-tRNA synthetases catalyze hydroxamate formation at rates comparable to those for aminoacyl-tRNA formation; with
lysyl-, alanyl-, isoleucyl-, glycyl-, cysteinyl-, leucyl-, seryl-, and valyl-tRNA synthetases, the relative rates of hydroxamate
formation progressively decrease; and glutaminyl- and threonyl-tRNA synthetases do not catalyze hydroxamate formation. In
an unfractionated enzyme extract, threonine hydroxamate forms, but this is totally accounted for by the mistaken activation
of threonine by the valyl-tRNA synthetase. Purified threonyl-tRNA synthetase catalyzes hydroxamate formation only when tRNA
is present, by catalyzing the formation of threonyl-tRNA, which reacts nonenzymatically with hydroxylamine. The mammalian
threonyl-tRNA synthetase also fails to catalyze formation of threonine hydroxamate from amino acid and ATP.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)91925-3</identifier><identifier>PMID: 4301683</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Alanine ; Amino Acids ; Carbon Isotopes ; Chromatography, Ion Exchange ; Cysteine ; Escherichia coli - enzymology ; Glutamates ; Glycine ; Hydroxylamines ; Isoleucine ; Kinetics ; Leucine ; Ligases - isolation & purification ; Lysine ; Methionine ; Periodic Acid ; Phenylalanine ; RNA, Bacterial ; RNA, Transfer ; Threonine ; Tryptophan ; Tyrosine</subject><ispartof>The Journal of biological chemistry, 1968-11, Vol.243 (21), p.5724-5730</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-67346f3508f0f72989e84a66bd9d0f7665abacb671ef4940b0a8e4b399e03fe93</citedby><cites>FETCH-LOGICAL-c379t-67346f3508f0f72989e84a66bd9d0f7665abacb671ef4940b0a8e4b399e03fe93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4301683$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hirsh, D I</creatorcontrib><creatorcontrib>Lipmann, F</creatorcontrib><title>The Divergence in Reactivity of Aminoacyl Transfer Ribonucleic Acid Synthetases of Escherichia coli with Hydroxylamine</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Fourteen partially purified Escherichia coli aminoacyl transfer ribonucleic acid synthetases were tested for their rates of amino acid hydroxamate formation relative
to the rates of aminoacyl-tRNA formation. Three groups of reactivity were observed: tyrosyl-, phenylalanyl-, tryptophanyl-,
and methionyl-tRNA synthetases catalyze hydroxamate formation at rates comparable to those for aminoacyl-tRNA formation; with
lysyl-, alanyl-, isoleucyl-, glycyl-, cysteinyl-, leucyl-, seryl-, and valyl-tRNA synthetases, the relative rates of hydroxamate
formation progressively decrease; and glutaminyl- and threonyl-tRNA synthetases do not catalyze hydroxamate formation. In
an unfractionated enzyme extract, threonine hydroxamate forms, but this is totally accounted for by the mistaken activation
of threonine by the valyl-tRNA synthetase. Purified threonyl-tRNA synthetase catalyzes hydroxamate formation only when tRNA
is present, by catalyzing the formation of threonyl-tRNA, which reacts nonenzymatically with hydroxylamine. The mammalian
threonyl-tRNA synthetase also fails to catalyze formation of threonine hydroxamate from amino acid and ATP.</description><subject>Alanine</subject><subject>Amino Acids</subject><subject>Carbon Isotopes</subject><subject>Chromatography, Ion Exchange</subject><subject>Cysteine</subject><subject>Escherichia coli - enzymology</subject><subject>Glutamates</subject><subject>Glycine</subject><subject>Hydroxylamines</subject><subject>Isoleucine</subject><subject>Kinetics</subject><subject>Leucine</subject><subject>Ligases - isolation & purification</subject><subject>Lysine</subject><subject>Methionine</subject><subject>Periodic Acid</subject><subject>Phenylalanine</subject><subject>RNA, Bacterial</subject><subject>RNA, Transfer</subject><subject>Threonine</subject><subject>Tryptophan</subject><subject>Tyrosine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1968</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEFr3DAQhUVpSLZpf0JAECjtwam0km3puKRpUwgEki30JmR5FE-wrUTybup_H212yVxmmHnvDXyEnHF2wRmvftwztuSFXpbqG1ffNc9TIT6QBWdKFKLk_z6SxbvkhHxK6ZHlkpofk2MpcoQSC7Jdd0B_4hbiA4wOKI70DqybcIvTTIOnqwHHYN3c03W0Y_IQ6R02Ydy4HtDRlcOW3s_j1MFkE6Sd5Sq5DiK6Di11oUf6glNHr-c2hv9zb3MgfCZH3vYJvhz6Kfn762p9eV3c3P7-c7m6KZyo9VRUtZCVFyVTnvl6qZUGJW1VNa1u86KqSttY11Q1By-1ZA2zCmQjtAYmPGhxSr7uc59ieN5AmsyAyUHf2xHCJhlVMil0rbKw3AtdDClF8OYp4mDjbDgzO97mjbfZwTRcmTfeRmTf2eHBphmgfXcdAOf7-f7e4UP3ghFMgyHjGcxSCpMDyzoPr1RCiKQ</recordid><startdate>19681110</startdate><enddate>19681110</enddate><creator>Hirsh, D I</creator><creator>Lipmann, F</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>19681110</creationdate><title>The Divergence in Reactivity of Aminoacyl Transfer Ribonucleic Acid Synthetases of Escherichia coli with Hydroxylamine</title><author>Hirsh, D I ; Lipmann, F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-67346f3508f0f72989e84a66bd9d0f7665abacb671ef4940b0a8e4b399e03fe93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1968</creationdate><topic>Alanine</topic><topic>Amino Acids</topic><topic>Carbon Isotopes</topic><topic>Chromatography, Ion Exchange</topic><topic>Cysteine</topic><topic>Escherichia coli - enzymology</topic><topic>Glutamates</topic><topic>Glycine</topic><topic>Hydroxylamines</topic><topic>Isoleucine</topic><topic>Kinetics</topic><topic>Leucine</topic><topic>Ligases - isolation & purification</topic><topic>Lysine</topic><topic>Methionine</topic><topic>Periodic Acid</topic><topic>Phenylalanine</topic><topic>RNA, Bacterial</topic><topic>RNA, Transfer</topic><topic>Threonine</topic><topic>Tryptophan</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirsh, D I</creatorcontrib><creatorcontrib>Lipmann, F</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>Hirsh, D I</au><au>Lipmann, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Divergence in Reactivity of Aminoacyl Transfer Ribonucleic Acid Synthetases of Escherichia coli with Hydroxylamine</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1968-11-10</date><risdate>1968</risdate><volume>243</volume><issue>21</issue><spage>5724</spage><epage>5730</epage><pages>5724-5730</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Fourteen partially purified Escherichia coli aminoacyl transfer ribonucleic acid synthetases were tested for their rates of amino acid hydroxamate formation relative
to the rates of aminoacyl-tRNA formation. Three groups of reactivity were observed: tyrosyl-, phenylalanyl-, tryptophanyl-,
and methionyl-tRNA synthetases catalyze hydroxamate formation at rates comparable to those for aminoacyl-tRNA formation; with
lysyl-, alanyl-, isoleucyl-, glycyl-, cysteinyl-, leucyl-, seryl-, and valyl-tRNA synthetases, the relative rates of hydroxamate
formation progressively decrease; and glutaminyl- and threonyl-tRNA synthetases do not catalyze hydroxamate formation. In
an unfractionated enzyme extract, threonine hydroxamate forms, but this is totally accounted for by the mistaken activation
of threonine by the valyl-tRNA synthetase. Purified threonyl-tRNA synthetase catalyzes hydroxamate formation only when tRNA
is present, by catalyzing the formation of threonyl-tRNA, which reacts nonenzymatically with hydroxylamine. The mammalian
threonyl-tRNA synthetase also fails to catalyze formation of threonine hydroxamate from amino acid and ATP.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>4301683</pmid><doi>10.1016/S0021-9258(18)91925-3</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1968-11, Vol.243 (21), p.5724-5730 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Alanine Amino Acids Carbon Isotopes Chromatography, Ion Exchange Cysteine Escherichia coli - enzymology Glutamates Glycine Hydroxylamines Isoleucine Kinetics Leucine Ligases - isolation & purification Lysine Methionine Periodic Acid Phenylalanine RNA, Bacterial RNA, Transfer Threonine Tryptophan Tyrosine |
| title | The Divergence in Reactivity of Aminoacyl Transfer Ribonucleic Acid Synthetases of Escherichia coli with Hydroxylamine |
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