Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Kinetic mechanism for lysyl-tRNA synthetase
Bisubstrate kinetics and end product and dead end inhibition studies were performed on lysyl-tRNA synthetase isolated from rat liver. The kinetic patterns obtained are consistent with a sequential ordered mechanism of substrate addition, tRNA bound first, followed by lysine, and then by ATP. Pyropho...
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| Veröffentlicht in: | The Journal of biological chemistry 1983-11, Vol.258 (22), p.13592-13596 |
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| container_end_page | 13596 |
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| container_issue | 22 |
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| container_title | The Journal of biological chemistry |
| container_volume | 258 |
| creator | Hilderman, R H Zimmerman, J K Dang, C V Grothusen, J R |
| description | Bisubstrate kinetics and end product and dead end inhibition studies were performed on lysyl-tRNA synthetase isolated from rat liver. The kinetic patterns obtained are consistent with a sequential ordered mechanism of substrate addition, tRNA bound first, followed by lysine, and then by ATP. Pyrophosphate and AMP are released in a random fashion with aminoacylated tRNA the last product to dissociate from the enzyme. This is the first report of a kinetic mechanism for lysyl-tRNA synthetase. |
| doi_str_mv | 10.1016/S0021-9258(17)43956-1 |
| format | Article |
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Kinetic mechanism for lysyl-tRNA synthetase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Bisubstrate kinetics and end product and dead end inhibition studies were performed on lysyl-tRNA synthetase isolated from rat liver. The kinetic patterns obtained are consistent with a sequential ordered mechanism of substrate addition, tRNA bound first, followed by lysine, and then by ATP. Pyrophosphate and AMP are released in a random fashion with aminoacylated tRNA the last product to dissociate from the enzyme. This is the first report of a kinetic mechanism for lysyl-tRNA synthetase.</description><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Arginine-tRNA Ligase - metabolism</subject><subject>Biological and medical sciences</subject><subject>Diphosphates - pharmacology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Ligases</subject><subject>Liver - enzymology</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - pharmacology</subject><subject>Lysine-tRNA Ligase - metabolism</subject><subject>Male</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Rats</subject><subject>Zinc - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUcuO1DAQtBBoGRY-YSUfEIJDFrcdO_EJrUa8xAokHhI3y3E6E6MkHmzPwvAX-8ebeWi4IOFLW-qqru4qQi6AXQID9fILYxwKzWX9HKoXpdBSFXCPLIDVohASvt8nixPkIXmU0g82v1LDGTlTAmTFygW5XfY2Wpcx-j82-zDR0FFL-zCGFU4YNonauPLTdiionVo6bNP8zZ8_XtG0nXKP2SakLozrAX9Tn8JgM7a0i2Gk0WY6-BuMl_SDnzB7R0d0vZ18GmkX4r-HPSYPOjskfHKs5-Tbm9dfl--K609v3y-vrgsnagZFg8wpIRougTvkIFtlFXaykVCWlaxbPR_rODaqLBtnG-ZaAbrjAApVibU4J88Oc9cx_Nxgymb0yeEw2P3ZpmZVxbXmM1AegC6GlCJ2Zh39aOPWADO7KMw-CrPz2UBl9lEYmHkXR4FNM2J7Yh29n_tPj32bnB26aCfn0wmmS8204H9hvV_1v3xE0_jgehzNTo_zWUnut3x1gOHs2Y3HaJLzODlsZ4rLpg3-P_veAfbAs3s</recordid><startdate>19831125</startdate><enddate>19831125</enddate><creator>Hilderman, R H</creator><creator>Zimmerman, J K</creator><creator>Dang, C V</creator><creator>Grothusen, J R</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>19831125</creationdate><title>Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. 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Kinetic mechanism for lysyl-tRNA synthetase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1983-11-25</date><risdate>1983</risdate><volume>258</volume><issue>22</issue><spage>13592</spage><epage>13596</epage><pages>13592-13596</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Bisubstrate kinetics and end product and dead end inhibition studies were performed on lysyl-tRNA synthetase isolated from rat liver. The kinetic patterns obtained are consistent with a sequential ordered mechanism of substrate addition, tRNA bound first, followed by lysine, and then by ATP. Pyrophosphate and AMP are released in a random fashion with aminoacylated tRNA the last product to dissociate from the enzyme. 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| ispartof | The Journal of biological chemistry, 1983-11, Vol.258 (22), p.13592-13596 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80772992 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acyl-tRNA Synthetases - metabolism Analytical, structural and metabolic biochemistry Animals Arginine-tRNA Ligase - metabolism Biological and medical sciences Diphosphates - pharmacology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Kinetics Ligases Liver - enzymology Lysine - analogs & derivatives Lysine - pharmacology Lysine-tRNA Ligase - metabolism Male Multienzyme Complexes - metabolism Rats Zinc - pharmacology |
| title | Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Kinetic mechanism for lysyl-tRNA synthetase |
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