Biosynthesis and Incorporation into Protein of Norleucine by Escherichia coli
The methionine analog norleucine was produced during the synthesis of bovine somatotropin by Escherichia coli strain W3110G containing the recombinant plasmid pBGH1. Norleucine was generated by the leucine biosynthetic pathway from pyruvate or α-ketobutyrate in place of α-ketoisovalerate as the init...
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Veröffentlicht in: | The Journal of biological chemistry 1989-01, Vol.264 (1), p.531-539 |
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creator | Bogosian, G Violand, B N Dorward-King, E J Workman, W E Jung, P E Kane, J F |
description | The methionine analog norleucine was produced during the synthesis of bovine somatotropin by Escherichia coli strain W3110G containing the recombinant plasmid pBGH1. Norleucine was generated by the leucine biosynthetic pathway from pyruvate or α-ketobutyrate in place of α-ketoisovalerate as the initial substrate. The intracellular level of norleucine was high enough to permit the analog to compete successfully with methionine for incorporation into protein. Two ways were found to prevent either the formation of norleucine or its incorporation into protein. The endogenous synthesis of norleucine was eliminated by deleting the leucine Operon. The addition of sufficient methionine or 2-hydroxy-4-methylthiobutanoic acid, a precursor of methionine, to the culture medium prevented any norleucine from being incorporated into protein. |
doi_str_mv | 10.1016/S0021-9258(17)31291-7 |
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Norleucine was generated by the leucine biosynthetic pathway from pyruvate or α-ketobutyrate in place of α-ketoisovalerate as the initial substrate. The intracellular level of norleucine was high enough to permit the analog to compete successfully with methionine for incorporation into protein. Two ways were found to prevent either the formation of norleucine or its incorporation into protein. The endogenous synthesis of norleucine was eliminated by deleting the leucine Operon. The addition of sufficient methionine or 2-hydroxy-4-methylthiobutanoic acid, a precursor of methionine, to the culture medium prevented any norleucine from being incorporated into protein.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)31291-7</identifier><identifier>PMID: 2642478</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acids - analysis ; Aminoacids, peptides. Hormones. Neuropeptides ; Aminocaproates - biosynthesis ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cattle ; Chromatography, High Pressure Liquid ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - growth & development ; Fermentation ; Fundamental and applied biological sciences. Psychology ; Genotype ; Growth Hormone - biosynthesis ; Norleucine - biosynthesis ; Norleucine - metabolism ; Plasmids ; Proteins ; Recombinant Proteins - biosynthesis ; Transduction, Genetic</subject><ispartof>The Journal of biological chemistry, 1989-01, Vol.264 (1), p.531-539</ispartof><rights>1989 © 1989 ASBMB. 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Norleucine was generated by the leucine biosynthetic pathway from pyruvate or α-ketobutyrate in place of α-ketoisovalerate as the initial substrate. The intracellular level of norleucine was high enough to permit the analog to compete successfully with methionine for incorporation into protein. Two ways were found to prevent either the formation of norleucine or its incorporation into protein. The endogenous synthesis of norleucine was eliminated by deleting the leucine Operon. The addition of sufficient methionine or 2-hydroxy-4-methylthiobutanoic acid, a precursor of methionine, to the culture medium prevented any norleucine from being incorporated into protein.</description><subject>Amino Acids - analysis</subject><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Aminocaproates - biosynthesis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - growth & development</subject><subject>Fermentation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genotype</subject><subject>Growth Hormone - biosynthesis</subject><subject>Norleucine - biosynthesis</subject><subject>Norleucine - metabolism</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Transduction, Genetic</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo67j6ExZaENFDa76TPokuqy6sH6CCt5BUV9uRnmRMepT59_bsDHPdutShnqp6eQi5YPQVo0y__kYpZ23HlX3BzEvBeMdac4-sGLWiFYr9vE9WJ-QheVTrb7qU7NgZOeNacmnsinx6F3PdpXnEGmvjU99cJ8hlk4ufY05NTHNuvpY8Y0xNHprPuUy4hZiwCbvmqsKIJcIYfQN5io_Jg8FPFZ8c-zn58f7q--XH9ubLh-vLtzctyE7MrRaBIvVKMyuDARk64TlVNigKwsjAQXs9MBNCr8EgVxACZd6iNV6Izotz8vxwd1Pyny3W2a1jBZwmnzBvqzPWSt5xfifIFO201HoB1QGEkmstOLhNiWtfdo5Rt_ftbn27vUzHjLv17cyyd3F8sA1r7E9bR8HL_Nlx7iv4aSg-QawnzAhKDd3nfHrAxvhr_BcLuhDz4na9P-SYU4ItzJsDg4vZvxGLqxAxAfYLD7Prc7wj7H_hH6ck</recordid><startdate>19890105</startdate><enddate>19890105</enddate><creator>Bogosian, G</creator><creator>Violand, B N</creator><creator>Dorward-King, E J</creator><creator>Workman, W E</creator><creator>Jung, P E</creator><creator>Kane, J F</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19890105</creationdate><title>Biosynthesis and Incorporation into Protein of Norleucine by Escherichia coli</title><author>Bogosian, G ; Violand, B N ; Dorward-King, E J ; Workman, W E ; Jung, P E ; Kane, J F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-63b0e0a56184b7c4b93a2058b50c374b2c6a6f17bbd6c7e25cbb01a8e87a339a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acids - analysis</topic><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Aminocaproates - biosynthesis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - growth & development</topic><topic>Fermentation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genotype</topic><topic>Growth Hormone - biosynthesis</topic><topic>Norleucine - biosynthesis</topic><topic>Norleucine - metabolism</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Transduction, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bogosian, G</creatorcontrib><creatorcontrib>Violand, B N</creatorcontrib><creatorcontrib>Dorward-King, E J</creatorcontrib><creatorcontrib>Workman, W E</creatorcontrib><creatorcontrib>Jung, P E</creatorcontrib><creatorcontrib>Kane, J F</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</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>Bogosian, G</au><au>Violand, B N</au><au>Dorward-King, E J</au><au>Workman, W E</au><au>Jung, P E</au><au>Kane, J F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biosynthesis and Incorporation into Protein of Norleucine by Escherichia coli</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-01-05</date><risdate>1989</risdate><volume>264</volume><issue>1</issue><spage>531</spage><epage>539</epage><pages>531-539</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The methionine analog norleucine was produced during the synthesis of bovine somatotropin by Escherichia coli strain W3110G containing the recombinant plasmid pBGH1. Norleucine was generated by the leucine biosynthetic pathway from pyruvate or α-ketobutyrate in place of α-ketoisovalerate as the initial substrate. The intracellular level of norleucine was high enough to permit the analog to compete successfully with methionine for incorporation into protein. Two ways were found to prevent either the formation of norleucine or its incorporation into protein. The endogenous synthesis of norleucine was eliminated by deleting the leucine Operon. The addition of sufficient methionine or 2-hydroxy-4-methylthiobutanoic acid, a precursor of methionine, to the culture medium prevented any norleucine from being incorporated into protein.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2642478</pmid><doi>10.1016/S0021-9258(17)31291-7</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acids - analysis Aminoacids, peptides. Hormones. Neuropeptides Aminocaproates - biosynthesis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Chromatography, High Pressure Liquid Escherichia coli Escherichia coli - genetics Escherichia coli - growth & development Fermentation Fundamental and applied biological sciences. Psychology Genotype Growth Hormone - biosynthesis Norleucine - biosynthesis Norleucine - metabolism Plasmids Proteins Recombinant Proteins - biosynthesis Transduction, Genetic |
title | Biosynthesis and Incorporation into Protein of Norleucine by Escherichia coli |
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