Regulation of phenylethanolamine N-methyl transferase
Phenylethanolamine N-methyl transferase (PNMT) catalyzes the methylation of norepinephrine, forming epinephrine in the adrenal medulla. In vitro, PNMT accepts a variety of phenylethanolamines and phenylethylenediamines as substrates. It is inhibited by phenethylamines and other compounds structurall...
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| Veröffentlicht in: | Advances in enzyme regulation 1974, Vol.12, p.311-341 |
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| creator | Fuller, Ray W. Roush, Betty W. Molloy, Bryan B. |
| description | Phenylethanolamine N-methyl transferase (PNMT) catalyzes the methylation of norepinephrine, forming epinephrine in the adrenal medulla.
In vitro, PNMT accepts a variety of phenylethanolamines and phenylethylenediamines as substrates. It is inhibited by phenethylamines and other compounds structurally similar to its substrates, as well as by agents that bind to sulfhydryl groups. Specific inhibitors of PNMT may be useful pharmacologic tools and potentially drugs. A group of benzylamines, including 2,3-dichloro-α-methylbenzylamine, are among the most potent inhibitors presently known.
In vivo, maintenance of PNMT levels in the adrenal medulla is dependent upon an adequate supply of glucocorticoids from the adrenal cortex. Neural input to the medulla may also influence the enzyme level. The possibility that product inhibition may influence PNMT activity
in vivo requires further study. |
| doi_str_mv | 10.1016/0065-2571(74)90019-3 |
| format | Article |
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In vitro, PNMT accepts a variety of phenylethanolamines and phenylethylenediamines as substrates. It is inhibited by phenethylamines and other compounds structurally similar to its substrates, as well as by agents that bind to sulfhydryl groups. Specific inhibitors of PNMT may be useful pharmacologic tools and potentially drugs. A group of benzylamines, including 2,3-dichloro-α-methylbenzylamine, are among the most potent inhibitors presently known.
In vivo, maintenance of PNMT levels in the adrenal medulla is dependent upon an adequate supply of glucocorticoids from the adrenal cortex. Neural input to the medulla may also influence the enzyme level. The possibility that product inhibition may influence PNMT activity
in vivo requires further study.</description><identifier>ISSN: 0065-2571</identifier><identifier>EISSN: 1873-2437</identifier><identifier>DOI: 10.1016/0065-2571(74)90019-3</identifier><identifier>PMID: 4462384</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Adrenal Medulla - enzymology ; Allosteric Regulation ; Amines - pharmacology ; Animals ; Benzyl Compounds - pharmacology ; Epinephrine - biosynthesis ; Glucocorticoids - metabolism ; Liver - enzymology ; Models, Chemical ; Norepinephrine - metabolism ; Phenethylamines - pharmacology ; Phenylethanolamine N-Methyltransferase - antagonists & inhibitors ; Phenylethanolamine N-Methyltransferase - metabolism ; Rabbits ; Rats</subject><ispartof>Advances in enzyme regulation, 1974, Vol.12, p.311-341</ispartof><rights>1974</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c272t-71de747b20f059e045a06b862310110ad946065f5f9a763f0f7827bc0e04a1993</citedby><cites>FETCH-LOGICAL-c272t-71de747b20f059e045a06b862310110ad946065f5f9a763f0f7827bc0e04a1993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0065-2571(74)90019-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,4022,27922,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4462384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fuller, Ray W.</creatorcontrib><creatorcontrib>Roush, Betty W.</creatorcontrib><creatorcontrib>Molloy, Bryan B.</creatorcontrib><title>Regulation of phenylethanolamine N-methyl transferase</title><title>Advances in enzyme regulation</title><addtitle>Adv Enzyme Regul</addtitle><description>Phenylethanolamine N-methyl transferase (PNMT) catalyzes the methylation of norepinephrine, forming epinephrine in the adrenal medulla.
In vitro, PNMT accepts a variety of phenylethanolamines and phenylethylenediamines as substrates. It is inhibited by phenethylamines and other compounds structurally similar to its substrates, as well as by agents that bind to sulfhydryl groups. Specific inhibitors of PNMT may be useful pharmacologic tools and potentially drugs. A group of benzylamines, including 2,3-dichloro-α-methylbenzylamine, are among the most potent inhibitors presently known.
In vivo, maintenance of PNMT levels in the adrenal medulla is dependent upon an adequate supply of glucocorticoids from the adrenal cortex. Neural input to the medulla may also influence the enzyme level. The possibility that product inhibition may influence PNMT activity
in vivo requires further study.</description><subject>Adrenal Medulla - enzymology</subject><subject>Allosteric Regulation</subject><subject>Amines - pharmacology</subject><subject>Animals</subject><subject>Benzyl Compounds - pharmacology</subject><subject>Epinephrine - biosynthesis</subject><subject>Glucocorticoids - metabolism</subject><subject>Liver - enzymology</subject><subject>Models, Chemical</subject><subject>Norepinephrine - metabolism</subject><subject>Phenethylamines - pharmacology</subject><subject>Phenylethanolamine N-Methyltransferase - antagonists & inhibitors</subject><subject>Phenylethanolamine N-Methyltransferase - metabolism</subject><subject>Rabbits</subject><subject>Rats</subject><issn>0065-2571</issn><issn>1873-2437</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAQgIMo67r6DxR6Ej1UJ2matBdhWXzBoiB6Dmk7cSN9rEkr7L83dZc9ehqG-eb1EXJO4YYCFbcAIo1ZKumV5Nc5AM3j5IBMaSaTmPFEHpLpHjkmJ95_BYZJISdkwrlgScanJH3Dz6HWve3aqDPReoXtpsZ-pduu1o1tMXqJm5Bv6qh3uvUGnfZ4So6Mrj2e7eKMfDzcvy-e4uXr4_NivoxLJlkfS1qh5LJgYCDNEXiqQRRZWB0eoKCrnItwoUlNrqVIDBiZMVmUEFBN8zyZkcvt3LXrvgf0vWqsL7GudYvd4FWgQVCeBJBvwdJ13js0au1so91GUVCjLTWqUKMKJbn6s6XGtovd_KFosNo37fSE-t22juHJH4tO-dJiW2JlHZa9qjr7_4JfCHx3Xw</recordid><startdate>1974</startdate><enddate>1974</enddate><creator>Fuller, Ray W.</creator><creator>Roush, Betty W.</creator><creator>Molloy, Bryan B.</creator><general>Elsevier 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>1974</creationdate><title>Regulation of phenylethanolamine N-methyl transferase</title><author>Fuller, Ray W. ; Roush, Betty W. ; Molloy, Bryan B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c272t-71de747b20f059e045a06b862310110ad946065f5f9a763f0f7827bc0e04a1993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Adrenal Medulla - enzymology</topic><topic>Allosteric Regulation</topic><topic>Amines - pharmacology</topic><topic>Animals</topic><topic>Benzyl Compounds - pharmacology</topic><topic>Epinephrine - biosynthesis</topic><topic>Glucocorticoids - metabolism</topic><topic>Liver - enzymology</topic><topic>Models, Chemical</topic><topic>Norepinephrine - metabolism</topic><topic>Phenethylamines - pharmacology</topic><topic>Phenylethanolamine N-Methyltransferase - antagonists & inhibitors</topic><topic>Phenylethanolamine N-Methyltransferase - metabolism</topic><topic>Rabbits</topic><topic>Rats</topic><toplevel>online_resources</toplevel><creatorcontrib>Fuller, Ray W.</creatorcontrib><creatorcontrib>Roush, Betty W.</creatorcontrib><creatorcontrib>Molloy, Bryan B.</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>Advances in enzyme regulation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fuller, Ray W.</au><au>Roush, Betty W.</au><au>Molloy, Bryan B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of phenylethanolamine N-methyl transferase</atitle><jtitle>Advances in enzyme regulation</jtitle><addtitle>Adv Enzyme Regul</addtitle><date>1974</date><risdate>1974</risdate><volume>12</volume><spage>311</spage><epage>341</epage><pages>311-341</pages><issn>0065-2571</issn><eissn>1873-2437</eissn><abstract>Phenylethanolamine N-methyl transferase (PNMT) catalyzes the methylation of norepinephrine, forming epinephrine in the adrenal medulla.
In vitro, PNMT accepts a variety of phenylethanolamines and phenylethylenediamines as substrates. It is inhibited by phenethylamines and other compounds structurally similar to its substrates, as well as by agents that bind to sulfhydryl groups. Specific inhibitors of PNMT may be useful pharmacologic tools and potentially drugs. A group of benzylamines, including 2,3-dichloro-α-methylbenzylamine, are among the most potent inhibitors presently known.
In vivo, maintenance of PNMT levels in the adrenal medulla is dependent upon an adequate supply of glucocorticoids from the adrenal cortex. Neural input to the medulla may also influence the enzyme level. The possibility that product inhibition may influence PNMT activity
in vivo requires further study.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>4462384</pmid><doi>10.1016/0065-2571(74)90019-3</doi><tpages>31</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0065-2571 |
| ispartof | Advances in enzyme regulation, 1974, Vol.12, p.311-341 |
| issn | 0065-2571 1873-2437 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Adrenal Medulla - enzymology Allosteric Regulation Amines - pharmacology Animals Benzyl Compounds - pharmacology Epinephrine - biosynthesis Glucocorticoids - metabolism Liver - enzymology Models, Chemical Norepinephrine - metabolism Phenethylamines - pharmacology Phenylethanolamine N-Methyltransferase - antagonists & inhibitors Phenylethanolamine N-Methyltransferase - metabolism Rabbits Rats |
| title | Regulation of phenylethanolamine N-methyl transferase |
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