Homoserine Kinase from Escherichia coli K12
Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr= 60000) composed of apparently identical polypeptide chains (Mr= 29 000). Its amino acid composition and N‐terminal sequence have been...
Gespeichert in:
| Veröffentlicht in: | European journal of biochemistry 1976-03, Vol.62 (3), p.519-526 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 526 |
|---|---|
| container_issue | 3 |
| container_start_page | 519 |
| container_title | European journal of biochemistry |
| container_volume | 62 |
| creator | BURR, Benjamin WALKER, John TRUFFA‐BACHI, Paolo COHEN, Georges N. |
| description | Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr= 60000) composed of apparently identical polypeptide chains (Mr= 29 000). Its amino acid composition and N‐terminal sequence have been determined. l‐Threonine is a competitive inhibitor of the substrate l‐homoserine; this inhibition is straightforward and shows no sign of co‐operativity. Evidence is presented that homoserine and threotine bind to the same site of this non‐allosteric enzyme. The binding of homoserine and threonine can also be studied by difference spectroscopy; the latter studies reveal an unexpected effect of magnesium ions, which might be the basis for the unusual high Mg2+ requirement for optimal enzyme reaction |
| doi_str_mv | 10.1111/j.1432-1033.1976.tb10186.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83374381</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>83374381</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4879-862e0f359b53c60345b323c9e823e38586ff644bfb93da4dddb3393251ee52fb3</originalsourceid><addsrcrecordid>eNqVkD1PwzAQhi3EVyn8A4aIgQUl2D7bsVkqqFqKWokBmK3YsdVUSVPiVrT_noRWMHPLSfd-nPQgdENwQtq5XySEAY0JBkiISkWyNgQTKZLtEer9SseohzFhMVVcnKOLEBYYY6FEeoZOSZpSCT10N6mrOrimWLpoWiyz4CLf1FU0CnbeXu28yCJbl0U0JfQSnfisDO7qsPvoYzx6H07i2evzy_BxFlsmUxVLQR32wJXhYAUGxg1QsMpJCg4kl8J7wZjxRkGesTzPDYACyolznHoDfXS771019efGhbWuimBdWWZLV2-ClgApA0la48PeaJs6hMZ5vWqKKmt2mmDdgdIL3dHQHQ3dgdIHUHrbhq8PXzamcvlf9IdMKw_28ldRut0_ivV49PTGiYJvIP12Mg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83374381</pqid></control><display><type>article</type><title>Homoserine Kinase from Escherichia coli K12</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>BURR, Benjamin ; WALKER, John ; TRUFFA‐BACHI, Paolo ; COHEN, Georges N.</creator><creatorcontrib>BURR, Benjamin ; WALKER, John ; TRUFFA‐BACHI, Paolo ; COHEN, Georges N.</creatorcontrib><description>Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr= 60000) composed of apparently identical polypeptide chains (Mr= 29 000). Its amino acid composition and N‐terminal sequence have been determined. l‐Threonine is a competitive inhibitor of the substrate l‐homoserine; this inhibition is straightforward and shows no sign of co‐operativity. Evidence is presented that homoserine and threotine bind to the same site of this non‐allosteric enzyme. The binding of homoserine and threonine can also be studied by difference spectroscopy; the latter studies reveal an unexpected effect of magnesium ions, which might be the basis for the unusual high Mg2+ requirement for optimal enzyme reaction</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1976.tb10186.x</identifier><identifier>PMID: 177283</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Amino Acids - analysis ; Binding Sites ; Enzyme Activation - drug effects ; Escherichia coli - enzymology ; Homoserine ; Kinetics ; Macromolecular Substances ; Magnesium - pharmacology ; Molecular Weight ; Peptide Fragments - analysis ; Phosphotransferases - isolation & purification ; Phosphotransferases - metabolism ; Protein Binding ; Spectrophotometry, Ultraviolet ; Threonine - pharmacology</subject><ispartof>European journal of biochemistry, 1976-03, Vol.62 (3), p.519-526</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4879-862e0f359b53c60345b323c9e823e38586ff644bfb93da4dddb3393251ee52fb3</citedby><cites>FETCH-LOGICAL-c4879-862e0f359b53c60345b323c9e823e38586ff644bfb93da4dddb3393251ee52fb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/177283$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BURR, Benjamin</creatorcontrib><creatorcontrib>WALKER, John</creatorcontrib><creatorcontrib>TRUFFA‐BACHI, Paolo</creatorcontrib><creatorcontrib>COHEN, Georges N.</creatorcontrib><title>Homoserine Kinase from Escherichia coli K12</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr= 60000) composed of apparently identical polypeptide chains (Mr= 29 000). Its amino acid composition and N‐terminal sequence have been determined. l‐Threonine is a competitive inhibitor of the substrate l‐homoserine; this inhibition is straightforward and shows no sign of co‐operativity. Evidence is presented that homoserine and threotine bind to the same site of this non‐allosteric enzyme. The binding of homoserine and threonine can also be studied by difference spectroscopy; the latter studies reveal an unexpected effect of magnesium ions, which might be the basis for the unusual high Mg2+ requirement for optimal enzyme reaction</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Binding Sites</subject><subject>Enzyme Activation - drug effects</subject><subject>Escherichia coli - enzymology</subject><subject>Homoserine</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Magnesium - pharmacology</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - analysis</subject><subject>Phosphotransferases - isolation & purification</subject><subject>Phosphotransferases - metabolism</subject><subject>Protein Binding</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Threonine - pharmacology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkD1PwzAQhi3EVyn8A4aIgQUl2D7bsVkqqFqKWokBmK3YsdVUSVPiVrT_noRWMHPLSfd-nPQgdENwQtq5XySEAY0JBkiISkWyNgQTKZLtEer9SseohzFhMVVcnKOLEBYYY6FEeoZOSZpSCT10N6mrOrimWLpoWiyz4CLf1FU0CnbeXu28yCJbl0U0JfQSnfisDO7qsPvoYzx6H07i2evzy_BxFlsmUxVLQR32wJXhYAUGxg1QsMpJCg4kl8J7wZjxRkGesTzPDYACyolznHoDfXS771019efGhbWuimBdWWZLV2-ClgApA0la48PeaJs6hMZ5vWqKKmt2mmDdgdIL3dHQHQ3dgdIHUHrbhq8PXzamcvlf9IdMKw_28ldRut0_ivV49PTGiYJvIP12Mg</recordid><startdate>197603</startdate><enddate>197603</enddate><creator>BURR, Benjamin</creator><creator>WALKER, John</creator><creator>TRUFFA‐BACHI, Paolo</creator><creator>COHEN, Georges N.</creator><general>Blackwell Publishing Ltd</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>197603</creationdate><title>Homoserine Kinase from Escherichia coli K12</title><author>BURR, Benjamin ; WALKER, John ; TRUFFA‐BACHI, Paolo ; COHEN, Georges N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4879-862e0f359b53c60345b323c9e823e38586ff644bfb93da4dddb3393251ee52fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Binding Sites</topic><topic>Enzyme Activation - drug effects</topic><topic>Escherichia coli - enzymology</topic><topic>Homoserine</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Magnesium - pharmacology</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - analysis</topic><topic>Phosphotransferases - isolation & purification</topic><topic>Phosphotransferases - metabolism</topic><topic>Protein Binding</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Threonine - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BURR, Benjamin</creatorcontrib><creatorcontrib>WALKER, John</creatorcontrib><creatorcontrib>TRUFFA‐BACHI, Paolo</creatorcontrib><creatorcontrib>COHEN, Georges N.</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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BURR, Benjamin</au><au>WALKER, John</au><au>TRUFFA‐BACHI, Paolo</au><au>COHEN, Georges N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Homoserine Kinase from Escherichia coli K12</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1976-03</date><risdate>1976</risdate><volume>62</volume><issue>3</issue><spage>519</spage><epage>526</epage><pages>519-526</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr= 60000) composed of apparently identical polypeptide chains (Mr= 29 000). Its amino acid composition and N‐terminal sequence have been determined. l‐Threonine is a competitive inhibitor of the substrate l‐homoserine; this inhibition is straightforward and shows no sign of co‐operativity. Evidence is presented that homoserine and threotine bind to the same site of this non‐allosteric enzyme. The binding of homoserine and threonine can also be studied by difference spectroscopy; the latter studies reveal an unexpected effect of magnesium ions, which might be the basis for the unusual high Mg2+ requirement for optimal enzyme reaction</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>177283</pmid><doi>10.1111/j.1432-1033.1976.tb10186.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1976-03, Vol.62 (3), p.519-526 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_83374381 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino Acids - analysis Binding Sites Enzyme Activation - drug effects Escherichia coli - enzymology Homoserine Kinetics Macromolecular Substances Magnesium - pharmacology Molecular Weight Peptide Fragments - analysis Phosphotransferases - isolation & purification Phosphotransferases - metabolism Protein Binding Spectrophotometry, Ultraviolet Threonine - pharmacology |
| title | Homoserine Kinase from Escherichia coli K12 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T06%3A34%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Homoserine%20Kinase%20from%20Escherichia%20coli%20K12&rft.jtitle=European%20journal%20of%20biochemistry&rft.au=BURR,%20Benjamin&rft.date=1976-03&rft.volume=62&rft.issue=3&rft.spage=519&rft.epage=526&rft.pages=519-526&rft.issn=0014-2956&rft.eissn=1432-1033&rft_id=info:doi/10.1111/j.1432-1033.1976.tb10186.x&rft_dat=%3Cproquest_cross%3E83374381%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=83374381&rft_id=info:pmid/177283&rfr_iscdi=true |