Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase
The nucleotide sequence of the gene, ilvA, for biosynthetic threonine deaminase (Tda) from Salmonella typhimurium was determined. The deduced amino acid sequence was compared with the deduced amino acid sequences of the biosynthetic Tda from Escherichia coli K-12 (ilvA) and Saccharomyces cerevisiae...
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| Veröffentlicht in: | Gene 1988-03, Vol.63 (2), p.245-252 |
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| creator | Taillon, Bruce E. Little, Robert Lawther, Robert P. |
| description | The nucleotide sequence of the gene,
ilvA, for biosynthetic threonine deaminase (Tda) from
Salmonella typhimurium was determined. The deduced amino acid sequence was compared with the deduced amino acid sequences of the biosynthetic Tda from
Escherichia coli K-12 (ilvA) and
Saccharomyces cerevisiae (
ILV1) and the biodegradative Tda from
E. coli K-12 (
tdc). The comparison indicated the presence of two types of blocks of homologous amino acids. The first type of homology is in the N-terminal portion of all four isozymes of Tda and probably indicates amino acids involved in catalysis. The second type of homology is found in the C-terminal portion of the three biosynthetic isozymes and presumably is involved in either (i) the binding or interaction of the allosteric effector isoleucine with the enzyme, or (ii) subunit interactions. The sites of amino acid changes of two
E. coli K-12
ilvA alleles with altered response to isoleucine are consistent with the conclusion that the C-terminal portion of biosynthetic Tda is involved in allosteric regulation. |
| doi_str_mv | 10.1016/0378-1119(88)90528-8 |
| format | Article |
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ilvA, for biosynthetic threonine deaminase (Tda) from
Salmonella typhimurium was determined. The deduced amino acid sequence was compared with the deduced amino acid sequences of the biosynthetic Tda from
Escherichia coli K-12 (ilvA) and
Saccharomyces cerevisiae (
ILV1) and the biodegradative Tda from
E. coli K-12 (
tdc). The comparison indicated the presence of two types of blocks of homologous amino acids. The first type of homology is in the N-terminal portion of all four isozymes of Tda and probably indicates amino acids involved in catalysis. The second type of homology is found in the C-terminal portion of the three biosynthetic isozymes and presumably is involved in either (i) the binding or interaction of the allosteric effector isoleucine with the enzyme, or (ii) subunit interactions. The sites of amino acid changes of two
E. coli K-12
ilvA alleles with altered response to isoleucine are consistent with the conclusion that the C-terminal portion of biosynthetic Tda is involved in allosteric regulation.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/0378-1119(88)90528-8</identifier><identifier>PMID: 3290055</identifier><identifier>CODEN: GENED6</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Alleles ; allosteric regulation ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Enzymes and enzyme inhibitors ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli K-12 ; feedback inhibition ; Fundamental and applied biological sciences. Psychology ; Genes ; Genes, Bacterial ; genes, ilvA, ILV1, tdc ; Isoenzymes - genetics ; Isoenzymes - metabolism ; isozymes ; Lyases ; Mission oriented research ; Molecular Sequence Data ; Physiology and metabolism ; Recombinant DNA ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Salmonella typhimurium ; Salmonella typhimurium - enzymology ; Salmonella typhimurium - genetics ; Species Specificity ; Threonine Dehydratase - genetics ; Threonine Dehydratase - metabolism</subject><ispartof>Gene, 1988-03, Vol.63 (2), p.245-252</ispartof><rights>1988</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c332t-a1eccc92e592d1c5eea3937d851f9665d36ef91e4247f341c3f14431bea02a263</citedby><cites>FETCH-LOGICAL-c332t-a1eccc92e592d1c5eea3937d851f9665d36ef91e4247f341c3f14431bea02a263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0378-1119(88)90528-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7829809$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3290055$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Taillon, Bruce E.</creatorcontrib><creatorcontrib>Little, Robert</creatorcontrib><creatorcontrib>Lawther, Robert P.</creatorcontrib><title>Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase</title><title>Gene</title><addtitle>Gene</addtitle><description>The nucleotide sequence of the gene,
ilvA, for biosynthetic threonine deaminase (Tda) from
Salmonella typhimurium was determined. The deduced amino acid sequence was compared with the deduced amino acid sequences of the biosynthetic Tda from
Escherichia coli K-12 (ilvA) and
Saccharomyces cerevisiae (
ILV1) and the biodegradative Tda from
E. coli K-12 (
tdc). The comparison indicated the presence of two types of blocks of homologous amino acids. The first type of homology is in the N-terminal portion of all four isozymes of Tda and probably indicates amino acids involved in catalysis. The second type of homology is found in the C-terminal portion of the three biosynthetic isozymes and presumably is involved in either (i) the binding or interaction of the allosteric effector isoleucine with the enzyme, or (ii) subunit interactions. The sites of amino acid changes of two
E. coli K-12
ilvA alleles with altered response to isoleucine are consistent with the conclusion that the C-terminal portion of biosynthetic Tda is involved in allosteric regulation.</description><subject>Alleles</subject><subject>allosteric regulation</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli K-12</subject><subject>feedback inhibition</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>genes, ilvA, ILV1, tdc</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>isozymes</subject><subject>Lyases</subject><subject>Mission oriented research</subject><subject>Molecular Sequence Data</subject><subject>Physiology and metabolism</subject><subject>Recombinant DNA</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Salmonella typhimurium</subject><subject>Salmonella typhimurium - enzymology</subject><subject>Salmonella typhimurium - genetics</subject><subject>Species Specificity</subject><subject>Threonine Dehydratase - genetics</subject><subject>Threonine Dehydratase - metabolism</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vFSEUhonR1Gv1H2jCwpi6GOVjPmBj0jTVmjTpRteEC2cUw8AVuDXzH_ujZHrHu1LLBsL7nHPenBehl5S8o4T27wkfREMplWdCvJWkY6IRj9CGikE2hHDxGG2OyFP0LOcfpJ6uYyfohDO5PDfo7jxoP2eXcRxx-Q543AdTXKy_2MZJu3CvbF3Mc6h6caZiCWJwAbAFPbmgM-DtjE2cdjq5HMOfXosYsTbO4gw_9xAMrHMSAP7lvG3KvKuc9-CrVOK_ylYPFr4lbXVxt_A3F8_Rk1H7DC_W-xR9_Xj55eKqub759Pni_LoxnLPSaArGGMmgk8xS0wFoLvlgRUdH2fed5T2MkkLL2mHkLTV8pG3L6RY0YZr1_BS9OfTdpVj95aImlw14rwPEfVaDYAMTlD0I0q6O6DtawfYAmhRzTjCqXXKTTrOiRC1pqyVKtUSphFD3aStRy16t_ffbCeyxaI236q9XXWej_Zh0MC4fsepTCiIr9uGAQV3arYOksnHL2q1LYIqy0f3fx28W7ssH</recordid><startdate>19880331</startdate><enddate>19880331</enddate><creator>Taillon, Bruce E.</creator><creator>Little, Robert</creator><creator>Lawther, Robert P.</creator><general>Elsevier B.V</general><general>Elsevier</general><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>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19880331</creationdate><title>Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase</title><author>Taillon, Bruce E. ; Little, Robert ; Lawther, Robert P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c332t-a1eccc92e592d1c5eea3937d851f9665d36ef91e4247f341c3f14431bea02a263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Alleles</topic><topic>allosteric regulation</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli K-12</topic><topic>feedback inhibition</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Genes, Bacterial</topic><topic>genes, ilvA, ILV1, tdc</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>isozymes</topic><topic>Lyases</topic><topic>Mission oriented research</topic><topic>Molecular Sequence Data</topic><topic>Physiology and metabolism</topic><topic>Recombinant DNA</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Salmonella typhimurium</topic><topic>Salmonella typhimurium - enzymology</topic><topic>Salmonella typhimurium - genetics</topic><topic>Species Specificity</topic><topic>Threonine Dehydratase - genetics</topic><topic>Threonine Dehydratase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Taillon, Bruce E.</creatorcontrib><creatorcontrib>Little, Robert</creatorcontrib><creatorcontrib>Lawther, Robert P.</creatorcontrib><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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Taillon, Bruce E.</au><au>Little, Robert</au><au>Lawther, Robert P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>1988-03-31</date><risdate>1988</risdate><volume>63</volume><issue>2</issue><spage>245</spage><epage>252</epage><pages>245-252</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><coden>GENED6</coden><abstract>The nucleotide sequence of the gene,
ilvA, for biosynthetic threonine deaminase (Tda) from
Salmonella typhimurium was determined. The deduced amino acid sequence was compared with the deduced amino acid sequences of the biosynthetic Tda from
Escherichia coli K-12 (ilvA) and
Saccharomyces cerevisiae (
ILV1) and the biodegradative Tda from
E. coli K-12 (
tdc). The comparison indicated the presence of two types of blocks of homologous amino acids. The first type of homology is in the N-terminal portion of all four isozymes of Tda and probably indicates amino acids involved in catalysis. The second type of homology is found in the C-terminal portion of the three biosynthetic isozymes and presumably is involved in either (i) the binding or interaction of the allosteric effector isoleucine with the enzyme, or (ii) subunit interactions. The sites of amino acid changes of two
E. coli K-12
ilvA alleles with altered response to isoleucine are consistent with the conclusion that the C-terminal portion of biosynthetic Tda is involved in allosteric regulation.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>3290055</pmid><doi>10.1016/0378-1119(88)90528-8</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1119 |
| ispartof | Gene, 1988-03, Vol.63 (2), p.245-252 |
| issn | 0378-1119 1879-0038 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78272812 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Alleles allosteric regulation Amino Acid Sequence Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Enzymes and enzyme inhibitors Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli K-12 feedback inhibition Fundamental and applied biological sciences. Psychology Genes Genes, Bacterial genes, ilvA, ILV1, tdc Isoenzymes - genetics Isoenzymes - metabolism isozymes Lyases Mission oriented research Molecular Sequence Data Physiology and metabolism Recombinant DNA Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Salmonella typhimurium Salmonella typhimurium - enzymology Salmonella typhimurium - genetics Species Specificity Threonine Dehydratase - genetics Threonine Dehydratase - metabolism |
| title | Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase |
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