Loading…

Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase

Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85400 +/- 1941, and its subunits were not resolv...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 1982-09, Vol.21 (19), p.4646-4650
Main Authors: Alvear, Marysol, Jabalquinto, Ana Maria, Eyzaguirre, Jaime, Cardemil, Emilio
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a439t-a89ce14c010db43998aaa3d622e1d756d7683537d6e3fe962d5019ce1aab01823
cites
container_end_page 4650
container_issue 19
container_start_page 4646
container_title Biochemistry (Easton)
container_volume 21
creator Alvear, Marysol
Jabalquinto, Ana Maria
Eyzaguirre, Jaime
Cardemil, Emilio
description Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85400 +/- 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5'-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.
doi_str_mv 10.1021/bi00262a020
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_74285835</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>74285835</sourcerecordid><originalsourceid>FETCH-LOGICAL-a439t-a89ce14c010db43998aaa3d622e1d756d7683537d6e3fe962d5019ce1aab01823</originalsourceid><addsrcrecordid>eNptkEFr3DAQRkVpSTebnnorFHxqD8XtSJZk-VhCNw0EmpLNIScxluSuUq_lSPaS7a-PFy8hh57EzHv6GD5C3lP4SoHRb7UHYJIhMHhFFlQwyHlViddkAQAyZ5WEt-Q0pftp5FDyE3IiFeVc0QW5ux6jb7zBwYcuw85mZoMRzeCi_zcvQ5PhzmOXtX7nYrZ1O2xDh4PLRd7vY-g3IfWbac6sMxjr8LhvMbkz8qbBNrl3x3dJblc_1uc_86tfF5fn369y5EU15Kgq4yg3QMHW06ZSiFhYyZijthTSllIVoiitdEXjKsmsAHr4glgDVaxYkk9zbh_Dw-jSoLc-Gde22LkwJl1ypsQhYkm-zKKJIaXoGt1Hv8W41xT0oUj9osjJ_niMHeuts8_usbmJ5zP3aXCPzxjjXy3LohR6fX2j4WJN1W-x0qvJ_zD7DQaNf6JP-vZGMS4pLSf4eYZokr4PY-ymxv571hNkfZI5</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>74285835</pqid></control><display><type>article</type><title>Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase</title><source>American Chemical Society</source><creator>Alvear, Marysol ; Jabalquinto, Ana Maria ; Eyzaguirre, Jaime ; Cardemil, Emilio</creator><creatorcontrib>Alvear, Marysol ; Jabalquinto, Ana Maria ; Eyzaguirre, Jaime ; Cardemil, Emilio</creatorcontrib><description>Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85400 +/- 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5'-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00262a020</identifier><identifier>PMID: 6814481</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Carboxy-Lyases - isolation &amp; purification ; Carboxy-Lyases - metabolism ; Cations, Divalent ; Chickens ; Edetic Acid - pharmacology ; Kinetics ; Liver - enzymology ; Molecular Weight</subject><ispartof>Biochemistry (Easton), 1982-09, Vol.21 (19), p.4646-4650</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a439t-a89ce14c010db43998aaa3d622e1d756d7683537d6e3fe962d5019ce1aab01823</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00262a020$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00262a020$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,27045,27905,27906,56747,56797</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6814481$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alvear, Marysol</creatorcontrib><creatorcontrib>Jabalquinto, Ana Maria</creatorcontrib><creatorcontrib>Eyzaguirre, Jaime</creatorcontrib><creatorcontrib>Cardemil, Emilio</creatorcontrib><title>Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85400 +/- 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5'-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.</description><subject>Animals</subject><subject>Carboxy-Lyases - isolation &amp; purification</subject><subject>Carboxy-Lyases - metabolism</subject><subject>Cations, Divalent</subject><subject>Chickens</subject><subject>Edetic Acid - pharmacology</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Molecular Weight</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><recordid>eNptkEFr3DAQRkVpSTebnnorFHxqD8XtSJZk-VhCNw0EmpLNIScxluSuUq_lSPaS7a-PFy8hh57EzHv6GD5C3lP4SoHRb7UHYJIhMHhFFlQwyHlViddkAQAyZ5WEt-Q0pftp5FDyE3IiFeVc0QW5ux6jb7zBwYcuw85mZoMRzeCi_zcvQ5PhzmOXtX7nYrZ1O2xDh4PLRd7vY-g3IfWbac6sMxjr8LhvMbkz8qbBNrl3x3dJblc_1uc_86tfF5fn369y5EU15Kgq4yg3QMHW06ZSiFhYyZijthTSllIVoiitdEXjKsmsAHr4glgDVaxYkk9zbh_Dw-jSoLc-Gde22LkwJl1ypsQhYkm-zKKJIaXoGt1Hv8W41xT0oUj9osjJ_niMHeuts8_usbmJ5zP3aXCPzxjjXy3LohR6fX2j4WJN1W-x0qvJ_zD7DQaNf6JP-vZGMS4pLSf4eYZokr4PY-ymxv571hNkfZI5</recordid><startdate>19820914</startdate><enddate>19820914</enddate><creator>Alvear, Marysol</creator><creator>Jabalquinto, Ana Maria</creator><creator>Eyzaguirre, Jaime</creator><creator>Cardemil, Emilio</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19820914</creationdate><title>Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase</title><author>Alvear, Marysol ; Jabalquinto, Ana Maria ; Eyzaguirre, Jaime ; Cardemil, Emilio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a439t-a89ce14c010db43998aaa3d622e1d756d7683537d6e3fe962d5019ce1aab01823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Carboxy-Lyases - isolation &amp; purification</topic><topic>Carboxy-Lyases - metabolism</topic><topic>Cations, Divalent</topic><topic>Chickens</topic><topic>Edetic Acid - pharmacology</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Molecular Weight</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alvear, Marysol</creatorcontrib><creatorcontrib>Jabalquinto, Ana Maria</creatorcontrib><creatorcontrib>Eyzaguirre, Jaime</creatorcontrib><creatorcontrib>Cardemil, Emilio</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alvear, Marysol</au><au>Jabalquinto, Ana Maria</au><au>Eyzaguirre, Jaime</au><au>Cardemil, Emilio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1982-09-14</date><risdate>1982</risdate><volume>21</volume><issue>19</issue><spage>4646</spage><epage>4650</epage><pages>4646-4650</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85400 +/- 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5'-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>6814481</pmid><doi>10.1021/bi00262a020</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2960
ispartof Biochemistry (Easton), 1982-09, Vol.21 (19), p.4646-4650
issn 0006-2960
1520-4995
language eng
recordid cdi_proquest_miscellaneous_74285835
source American Chemical Society
subjects Animals
Carboxy-Lyases - isolation & purification
Carboxy-Lyases - metabolism
Cations, Divalent
Chickens
Edetic Acid - pharmacology
Kinetics
Liver - enzymology
Molecular Weight
title Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T21%3A00%3A54IST&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=Purification%20and%20characterization%20of%20avian%20liver%20mevalonate-5-pyrophosphate%20decarboxylase&rft.jtitle=Biochemistry%20(Easton)&rft.au=Alvear,%20Marysol&rft.date=1982-09-14&rft.volume=21&rft.issue=19&rft.spage=4646&rft.epage=4650&rft.pages=4646-4650&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00262a020&rft_dat=%3Cproquest_cross%3E74285835%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a439t-a89ce14c010db43998aaa3d622e1d756d7683537d6e3fe962d5019ce1aab01823%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=74285835&rft_id=info:pmid/6814481&rfr_iscdi=true