Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase
Chicken liver mevalonate-5-pyrophosphate decarboxylase (ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33.) is inactivated by phenylglyoxal in triethanolamine buffer at pH 8.15. The reaction follows pseudo-first-order kinetics with a second-order rate constant of 108 m −1 min −1. Ap...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1983-08, Vol.225 (1), p.338-343 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Jabalquinto, Ana María Eyzaguirre, Jaime Cardemil, Emilio |
| description | Chicken liver mevalonate-5-pyrophosphate decarboxylase (ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33.) is inactivated by phenylglyoxal in triethanolamine buffer at pH 8.15. The reaction follows pseudo-first-order kinetics with a second-order rate constant of 108
m
−1 min
−1. Appropriate treatment of the kinetic data for the inactivation reaction indicates that the reaction of a single phenylglyoxal molecule per active unit of the enzyme is enough to completely inactivate the protein. The partially inactivated enzyme shows unaltered
K
m
but decreased
V as compared to native mevalonate-5-pyrophosphate decarboxylase. The dissociation constants for the enzyme-substrate complexes were estimated from inactivation reactions at different concentrations of substrates. From the data it is concluded that the modified amino acid is important for the binding of both substrates. |
| doi_str_mv | 10.1016/0003-9861(83)90038-3 |
| format | Article |
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m
−1 min
−1. Appropriate treatment of the kinetic data for the inactivation reaction indicates that the reaction of a single phenylglyoxal molecule per active unit of the enzyme is enough to completely inactivate the protein. The partially inactivated enzyme shows unaltered
K
m
but decreased
V as compared to native mevalonate-5-pyrophosphate decarboxylase. The dissociation constants for the enzyme-substrate complexes were estimated from inactivation reactions at different concentrations of substrates. From the data it is concluded that the modified amino acid is important for the binding of both substrates.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(83)90038-3</identifier><identifier>PMID: 6614925</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Arginine - metabolism ; Binding Sites ; Carboxy-Lyases - antagonists & inhibitors ; Carboxy-Lyases - metabolism ; Chickens ; Kinetics ; Liver - enzymology ; Phenylglyoxal - pharmacology ; Substrate Specificity</subject><ispartof>Archives of biochemistry and biophysics, 1983-08, Vol.225 (1), p.338-343</ispartof><rights>1983</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-e1e29780dfc64223a176d2665bafd6b0a4f2e7a9c2d52911fde29c66e1eb374e3</citedby><cites>FETCH-LOGICAL-c357t-e1e29780dfc64223a176d2665bafd6b0a4f2e7a9c2d52911fde29c66e1eb374e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(83)90038-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6614925$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jabalquinto, Ana María</creatorcontrib><creatorcontrib>Eyzaguirre, Jaime</creatorcontrib><creatorcontrib>Cardemil, Emilio</creatorcontrib><title>Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Chicken liver mevalonate-5-pyrophosphate decarboxylase (ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33.) is inactivated by phenylglyoxal in triethanolamine buffer at pH 8.15. The reaction follows pseudo-first-order kinetics with a second-order rate constant of 108
m
−1 min
−1. Appropriate treatment of the kinetic data for the inactivation reaction indicates that the reaction of a single phenylglyoxal molecule per active unit of the enzyme is enough to completely inactivate the protein. The partially inactivated enzyme shows unaltered
K
m
but decreased
V as compared to native mevalonate-5-pyrophosphate decarboxylase. The dissociation constants for the enzyme-substrate complexes were estimated from inactivation reactions at different concentrations of substrates. From the data it is concluded that the modified amino acid is important for the binding of both substrates.</description><subject>Animals</subject><subject>Arginine - metabolism</subject><subject>Binding Sites</subject><subject>Carboxy-Lyases - antagonists & inhibitors</subject><subject>Carboxy-Lyases - metabolism</subject><subject>Chickens</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Phenylglyoxal - pharmacology</subject><subject>Substrate Specificity</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAUhYMo4zj6DxSyEl1Uk7RN240gw_iAATe6jmly60TbpiadYv-9KTO4dHU53HPu40PonJIbSii_JYTEUZFzepXH10UQeRQfoDklBY-CSA7R_M9yjE68_ySE0oSzGZpxTpOCpXP0vhqMhlYBthUG76HtjayxdB-mHWvswBu9BY9Ni9XGqC9ocW0GcLiBQda2lT1EadSNznYb67tN0FiDkq60P2MtPZyio0rWHs72dYHeHlavy6do_fL4vLxfRypOsz4CCqzIcqIrxRPGYkkzrhnnaSkrzUsik4pBJgvFdMoKSisd_IrzkCvjLIF4gS53cztnv8PFvWiMV1DXsgW79SInPGWEFcGY7IzKWe8dVKJzppFuFJSICayYqImJmshDncCKOMQu9vO3ZQP6L7QnGfp3uz6EJwcDTnhlJrDaOFC90Nb8v-AXUueJNQ</recordid><startdate>198308</startdate><enddate>198308</enddate><creator>Jabalquinto, Ana María</creator><creator>Eyzaguirre, Jaime</creator><creator>Cardemil, Emilio</creator><general>Elsevier Inc</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>198308</creationdate><title>Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase</title><author>Jabalquinto, Ana María ; Eyzaguirre, Jaime ; Cardemil, Emilio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-e1e29780dfc64223a176d2665bafd6b0a4f2e7a9c2d52911fde29c66e1eb374e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Animals</topic><topic>Arginine - metabolism</topic><topic>Binding Sites</topic><topic>Carboxy-Lyases - antagonists & inhibitors</topic><topic>Carboxy-Lyases - metabolism</topic><topic>Chickens</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Phenylglyoxal - pharmacology</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jabalquinto, Ana María</creatorcontrib><creatorcontrib>Eyzaguirre, Jaime</creatorcontrib><creatorcontrib>Cardemil, Emilio</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jabalquinto, Ana María</au><au>Eyzaguirre, Jaime</au><au>Cardemil, Emilio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1983-08</date><risdate>1983</risdate><volume>225</volume><issue>1</issue><spage>338</spage><epage>343</epage><pages>338-343</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Chicken liver mevalonate-5-pyrophosphate decarboxylase (ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33.) is inactivated by phenylglyoxal in triethanolamine buffer at pH 8.15. The reaction follows pseudo-first-order kinetics with a second-order rate constant of 108
m
−1 min
−1. Appropriate treatment of the kinetic data for the inactivation reaction indicates that the reaction of a single phenylglyoxal molecule per active unit of the enzyme is enough to completely inactivate the protein. The partially inactivated enzyme shows unaltered
K
m
but decreased
V as compared to native mevalonate-5-pyrophosphate decarboxylase. The dissociation constants for the enzyme-substrate complexes were estimated from inactivation reactions at different concentrations of substrates. From the data it is concluded that the modified amino acid is important for the binding of both substrates.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6614925</pmid><doi>10.1016/0003-9861(83)90038-3</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1983-08, Vol.225 (1), p.338-343 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80652029 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Arginine - metabolism Binding Sites Carboxy-Lyases - antagonists & inhibitors Carboxy-Lyases - metabolism Chickens Kinetics Liver - enzymology Phenylglyoxal - pharmacology Substrate Specificity |
| title | Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase |
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