Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli
Ethoxyformic anhydride was used to demonstrate the existence of a second important histidine in succinyl-CoA synthetase from Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important histidine per alpha beta catalytic unit. Data are pre...
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| Veröffentlicht in: | The Journal of biological chemistry 1979-11, Vol.254 (21), p.10925-10930 |
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| container_title | The Journal of biological chemistry |
| container_volume | 254 |
| creator | Collier, G E Nishimura, J S |
| description | Ethoxyformic anhydride was used to demonstrate the existence of a second important histidine in succinyl-CoA synthetase from
Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important
histidine per alpha beta catalytic unit. Data are presented suggesting that this residue and an important thiol group on the
beta subunit (Collier, G., and Nishimura, J.S. (1978) J. Biol. Chem. 253, 4938-4943) interact with each other during catalysis.
A mechanism of action involving these 2 residues is proposed for one of the partial reactions catalyzed by succinyl-CoA synthetase. |
| doi_str_mv | 10.1016/S0021-9258(19)86612-7 |
| format | Article |
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Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important
histidine per alpha beta catalytic unit. Data are presented suggesting that this residue and an important thiol group on the
beta subunit (Collier, G., and Nishimura, J.S. (1978) J. Biol. Chem. 253, 4938-4943) interact with each other during catalysis.
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Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important
histidine per alpha beta catalytic unit. Data are presented suggesting that this residue and an important thiol group on the
beta subunit (Collier, G., and Nishimura, J.S. (1978) J. Biol. Chem. 253, 4938-4943) interact with each other during catalysis.
A mechanism of action involving these 2 residues is proposed for one of the partial reactions catalyzed by succinyl-CoA synthetase.</description><subject>Binding Sites</subject><subject>Coenzyme A Ligases - metabolism</subject><subject>Diethyl Pyrocarbonate - pharmacology</subject><subject>Escherichia coli - enzymology</subject><subject>Histidine</subject><subject>Kinetics</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Succinate-CoA Ligases - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtqGzEUhkVJ2rhu3yAFLUJoF9PqjDy6LINxmoAhi6TQndBozmRUZkauNE7w20e2g8_mX_yXAx8h34D9BAbi1yNjJRS6rNR30D-UEFAW8gOZAVO84BX8PSOzU-SCfE7pH8u30PCJfORKSgEz4lYvvsHRIW1DpJYmdGFsaOfT5Bs_IrUTnbosbvIvSJOfkIaWpq1zftz1xTLc0LQbc2SyKY_EMNBVch1G7zpvqQu9_0LOW9sn_Pquc_LndvW0vCvWD7_vlzfrwnGpp0JwIcuW1VXtSrQ1a2UlJWqUXAgJSltbV6wFiaVAWSqntWBN3QjNdKPAOT4n18fdTQz_t5gmM_jksO_tiGGbjFxIxRWDHKyOQRdDShFbs4l-sHFngJk9W3Nga_bgDGhzYGtk7l2-P9jWAzan1hFmtq-Oduefu1cf0dQ-ZBSDKauFyXvA8iJ_A81kgMc</recordid><startdate>19791110</startdate><enddate>19791110</enddate><creator>Collier, G E</creator><creator>Nishimura, J S</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>19791110</creationdate><title>Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli</title><author>Collier, G E ; Nishimura, J S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-63672f0b5bc2eab0f7577e9e73667189aab50f17e26e728c9960dbd6909d81cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Binding Sites</topic><topic>Coenzyme A Ligases - metabolism</topic><topic>Diethyl Pyrocarbonate - pharmacology</topic><topic>Escherichia coli - enzymology</topic><topic>Histidine</topic><topic>Kinetics</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Succinate-CoA Ligases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Collier, G E</creatorcontrib><creatorcontrib>Nishimura, J S</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>Collier, G E</au><au>Nishimura, J S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1979-11-10</date><risdate>1979</risdate><volume>254</volume><issue>21</issue><spage>10925</spage><epage>10930</epage><pages>10925-10930</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Ethoxyformic anhydride was used to demonstrate the existence of a second important histidine in succinyl-CoA synthetase from
Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important
histidine per alpha beta catalytic unit. Data are presented suggesting that this residue and an important thiol group on the
beta subunit (Collier, G., and Nishimura, J.S. (1978) J. Biol. Chem. 253, 4938-4943) interact with each other during catalysis.
A mechanism of action involving these 2 residues is proposed for one of the partial reactions catalyzed by succinyl-CoA synthetase.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>387761</pmid><doi>10.1016/S0021-9258(19)86612-7</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1979-11, Vol.254 (21), p.10925-10930 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Binding Sites Coenzyme A Ligases - metabolism Diethyl Pyrocarbonate - pharmacology Escherichia coli - enzymology Histidine Kinetics Phosphorylation Protein Binding Spectrophotometry, Ultraviolet Succinate-CoA Ligases - metabolism |
| title | Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli |
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