Divalent Metal Cation Requirement and Possible Classification of cGMP-Inhibited Phosphodiesterase as a Metallohydrolase
cGMP-inhibited phosphodiesterase (cGI-PDE) has been found to require a divalent metal cation for cAMP hydrolysis. The cGI-PDE isolated from human platelets exhibited significantly higher enzymatic activity when incubated with Mn2+, Mg2+, and Co2+. The addition of Zn2+, Cd2+, Ca2+, K+, or Na+to the e...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1995-10, Vol.323 (1), p.1-5 |
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| creator | Omburo, George A. Brickus, Tishara Ghazaleh, Faika A. Colman, Robert W. |
| description | cGMP-inhibited phosphodiesterase (cGI-PDE) has been found to require a divalent metal cation for cAMP hydrolysis. The cGI-PDE isolated from human platelets exhibited significantly higher enzymatic activity when incubated with Mn2+, Mg2+, and Co2+. The addition of Zn2+, Cd2+, Ca2+, K+, or Na+to the enzyme did not enhance the activity and, when present in high concentration (>1.0 μM), Zn2+and Cd2+inhibited the enzymatic activity of cGI-PDE. The inhibition by Zn2+(and Cd2+) was partially prevented by preincubation of the enzyme with Mn2+. The enzyme was also inhibited by metal chelators EDTA and 1,10-phenanthroline and not by their non-metal-chelating analogs. The partial protection against chelation (and inhibition) was afforded by AMP (the product of cAMP hydrolysis). |
| doi_str_mv | 10.1006/abbi.1995.0001 |
| format | Article |
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The cGI-PDE isolated from human platelets exhibited significantly higher enzymatic activity when incubated with Mn2+, Mg2+, and Co2+. The addition of Zn2+, Cd2+, Ca2+, K+, or Na+to the enzyme did not enhance the activity and, when present in high concentration (>1.0 μM), Zn2+and Cd2+inhibited the enzymatic activity of cGI-PDE. The inhibition by Zn2+(and Cd2+) was partially prevented by preincubation of the enzyme with Mn2+. The enzyme was also inhibited by metal chelators EDTA and 1,10-phenanthroline and not by their non-metal-chelating analogs. 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The partial protection against chelation (and inhibition) was afforded by AMP (the product of cAMP hydrolysis).</description><subject>3',5'-Cyclic-GMP Phosphodiesterases - classification</subject><subject>3',5'-Cyclic-GMP Phosphodiesterases - metabolism</subject><subject>Blood Platelets - enzymology</subject><subject>Cations, Divalent - metabolism</subject><subject>Cyclic AMP - metabolism</subject><subject>Humans</subject><subject>Metalloendopeptidases - classification</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtLAzEURoMotVa37oRZuZuazCMzWUrVKrRYRNchjxsamU7aZFrpvzfDFHeuEvKdfNx7ELoleEowpg9CSjsljJVTjDE5Q2OCGU1xXhfnaByf8pTVlFyiqxC-I0AKmo3QqCrqCpf5GP082YNooO2SJXSiSWais65NPmC3tx42fSBanaxcCFY2kMwaEW_GqoFzJlHz5Sp9a9dW2g4iuXZhu3baQujAiwCJCIkY2hu3PmrvYgVcowsjmgA3p3OCvl6eP2ev6eJ9_jZ7XKQqz1mXGqaUhKyspKkzUUuVScZEjWmpc0ZAGwqlwIZqYDmlumCKyQqTTGbSaJGZfILuh96td7t9nIlvbFDQNKIFtw-8qkpKcVlEcDqAysddPRi-9XYj_JETzHvTvDfNe9O8Nx0_3J2a93ID-g8_qY15PeQQ1ztY8DwoC60CHcWqjmtn_6v-Bajyj64</recordid><startdate>19951020</startdate><enddate>19951020</enddate><creator>Omburo, George A.</creator><creator>Brickus, Tishara</creator><creator>Ghazaleh, Faika A.</creator><creator>Colman, Robert W.</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>19951020</creationdate><title>Divalent Metal Cation Requirement and Possible Classification of cGMP-Inhibited Phosphodiesterase as a Metallohydrolase</title><author>Omburo, George A. ; Brickus, Tishara ; Ghazaleh, Faika A. ; Colman, Robert W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-f9ccbe257bf82a8bc2b99a8065d391edf6e5a0f6de9366d49c9b7012b2bfda2f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>3',5'-Cyclic-GMP Phosphodiesterases - classification</topic><topic>3',5'-Cyclic-GMP Phosphodiesterases - metabolism</topic><topic>Blood Platelets - enzymology</topic><topic>Cations, Divalent - metabolism</topic><topic>Cyclic AMP - metabolism</topic><topic>Humans</topic><topic>Metalloendopeptidases - classification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Omburo, George A.</creatorcontrib><creatorcontrib>Brickus, Tishara</creatorcontrib><creatorcontrib>Ghazaleh, Faika A.</creatorcontrib><creatorcontrib>Colman, Robert W.</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>Omburo, George A.</au><au>Brickus, Tishara</au><au>Ghazaleh, Faika A.</au><au>Colman, Robert W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Divalent Metal Cation Requirement and Possible Classification of cGMP-Inhibited Phosphodiesterase as a Metallohydrolase</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1995-10-20</date><risdate>1995</risdate><volume>323</volume><issue>1</issue><spage>1</spage><epage>5</epage><pages>1-5</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>cGMP-inhibited phosphodiesterase (cGI-PDE) has been found to require a divalent metal cation for cAMP hydrolysis. The cGI-PDE isolated from human platelets exhibited significantly higher enzymatic activity when incubated with Mn2+, Mg2+, and Co2+. The addition of Zn2+, Cd2+, Ca2+, K+, or Na+to the enzyme did not enhance the activity and, when present in high concentration (>1.0 μM), Zn2+and Cd2+inhibited the enzymatic activity of cGI-PDE. The inhibition by Zn2+(and Cd2+) was partially prevented by preincubation of the enzyme with Mn2+. The enzyme was also inhibited by metal chelators EDTA and 1,10-phenanthroline and not by their non-metal-chelating analogs. The partial protection against chelation (and inhibition) was afforded by AMP (the product of cAMP hydrolysis).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7487053</pmid><doi>10.1006/abbi.1995.0001</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1995-10, Vol.323 (1), p.1-5 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77566054 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | 3',5'-Cyclic-GMP Phosphodiesterases - classification 3',5'-Cyclic-GMP Phosphodiesterases - metabolism Blood Platelets - enzymology Cations, Divalent - metabolism Cyclic AMP - metabolism Humans Metalloendopeptidases - classification |
| title | Divalent Metal Cation Requirement and Possible Classification of cGMP-Inhibited Phosphodiesterase as a Metallohydrolase |
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