Kinetic analysis of differences in brain acetylcholinesterase from fish or mammalian sources
A kinetic analysis of the interactions of gold fish and rat brain AChE (acetylcholine acetylhydrolase, EC 3.1.1.7) with acetylthiocholine substrate and sulfonyl fluoride inhibitors revealed several differences between these enzymes. The fish brain AChE had a K m of 250 μM while the mammalian brain A...
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| Veröffentlicht in: | Biochemical pharmacology 1978, Vol.27 (23), p.2693-2698 |
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| container_title | Biochemical pharmacology |
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| creator | Moss, Donald E. Fahrney, David |
| description | A kinetic analysis of the interactions of gold fish and rat brain AChE (acetylcholine acetylhydrolase, EC 3.1.1.7) with acetylthiocholine substrate and sulfonyl fluoride inhibitors revealed several differences between these enzymes. The fish brain AChE had a
K
m
of 250 μM while the mammalian brain AChE had a
K
m
of 55 μM under the same assay conditions. In addition, the mammalian brain enzyme reacted with methanesulfonyl fluoride at more than three times the rate at which the fish enzyme reacted, and fish AChE did not react with phenylmethanesulfonyl fluoride at a measurable rate while mammalian AChE was found to react rapidly. Leptocurares were found to accelerate methanesulfonylation of both enzymes; however, they inhibited phenylmethanesulfonylation. These results suggest that fish and mammalian AChE may have topographic differences in the vicinity of the anionic portion of the active site. |
| doi_str_mv | 10.1016/0006-2952(78)90044-8 |
| format | Article |
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K
m
of 250 μM while the mammalian brain AChE had a
K
m
of 55 μM under the same assay conditions. In addition, the mammalian brain enzyme reacted with methanesulfonyl fluoride at more than three times the rate at which the fish enzyme reacted, and fish AChE did not react with phenylmethanesulfonyl fluoride at a measurable rate while mammalian AChE was found to react rapidly. Leptocurares were found to accelerate methanesulfonylation of both enzymes; however, they inhibited phenylmethanesulfonylation. These results suggest that fish and mammalian AChE may have topographic differences in the vicinity of the anionic portion of the active site.</description><identifier>ISSN: 0006-2952</identifier><identifier>EISSN: 1873-2968</identifier><identifier>DOI: 10.1016/0006-2952(78)90044-8</identifier><identifier>PMID: 215165</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Acetylcholinesterase - metabolism ; Animals ; Brain - enzymology ; Cholinesterase Inhibitors ; Fishes - metabolism ; In Vitro Techniques ; Kinetics ; Mesylates - pharmacology ; Neuromuscular Depolarizing Agents - pharmacology ; Neuromuscular Nondepolarizing Agents - pharmacology ; Rats ; Species Specificity ; Substrate Specificity</subject><ispartof>Biochemical pharmacology, 1978, Vol.27 (23), p.2693-2698</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-ed7c1592b6cec2221c3cfd4ed83fdc99deff71bc498e27dbe989428947b032443</citedby><cites>FETCH-LOGICAL-c356t-ed7c1592b6cec2221c3cfd4ed83fdc99deff71bc498e27dbe989428947b032443</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-2952(78)90044-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/215165$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moss, Donald E.</creatorcontrib><creatorcontrib>Fahrney, David</creatorcontrib><title>Kinetic analysis of differences in brain acetylcholinesterase from fish or mammalian sources</title><title>Biochemical pharmacology</title><addtitle>Biochem Pharmacol</addtitle><description>A kinetic analysis of the interactions of gold fish and rat brain AChE (acetylcholine acetylhydrolase, EC 3.1.1.7) with acetylthiocholine substrate and sulfonyl fluoride inhibitors revealed several differences between these enzymes. The fish brain AChE had a
K
m
of 250 μM while the mammalian brain AChE had a
K
m
of 55 μM under the same assay conditions. In addition, the mammalian brain enzyme reacted with methanesulfonyl fluoride at more than three times the rate at which the fish enzyme reacted, and fish AChE did not react with phenylmethanesulfonyl fluoride at a measurable rate while mammalian AChE was found to react rapidly. Leptocurares were found to accelerate methanesulfonylation of both enzymes; however, they inhibited phenylmethanesulfonylation. These results suggest that fish and mammalian AChE may have topographic differences in the vicinity of the anionic portion of the active site.</description><subject>Acetylcholinesterase - metabolism</subject><subject>Animals</subject><subject>Brain - enzymology</subject><subject>Cholinesterase Inhibitors</subject><subject>Fishes - metabolism</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Mesylates - pharmacology</subject><subject>Neuromuscular Depolarizing Agents - pharmacology</subject><subject>Neuromuscular Nondepolarizing Agents - pharmacology</subject><subject>Rats</subject><subject>Species Specificity</subject><subject>Substrate Specificity</subject><issn>0006-2952</issn><issn>1873-2968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtPxSAQhYnxdX38AxesjC6qQCmFjYkxvqKJG92ZEApDxLRFodfk_nup17h0MUyGOecEPoSOKDmjhIpzQoiomGrYSStPFSGcV3IDLahs63It5CZa_El20V7O7_MoBd1B24w2VDQL9PoQRpiCxWY0_SqHjKPHLngPCUYLGYcRd8mU01iYVr19i31x5AmSyYB9igP2Ib_hmPBghsH0wYw4x2Uq5gO05U2f4fC376OXm-vnq7vq8en2_urysbJ1I6YKXGtpo1gnLFjGGLW19Y6Dk7V3VikH3re0s1xJYK3rQEnFWam2IzXjvN5Hx-vcjxQ_l-VxegjZQt-bEeIy65YzxYQgRcjXQptizgm8_khhMGmlKdEzUz0T0jMw3Ur9w1TLYjv6zV92A7g_0xpiWV-s11D--BUg6WzDTM-FBHbSLob_878BK7aHbQ</recordid><startdate>1978</startdate><enddate>1978</enddate><creator>Moss, Donald E.</creator><creator>Fahrney, David</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>1978</creationdate><title>Kinetic analysis of differences in brain acetylcholinesterase from fish or mammalian sources</title><author>Moss, Donald E. ; Fahrney, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-ed7c1592b6cec2221c3cfd4ed83fdc99deff71bc498e27dbe989428947b032443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Acetylcholinesterase - metabolism</topic><topic>Animals</topic><topic>Brain - enzymology</topic><topic>Cholinesterase Inhibitors</topic><topic>Fishes - metabolism</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Mesylates - pharmacology</topic><topic>Neuromuscular Depolarizing Agents - pharmacology</topic><topic>Neuromuscular Nondepolarizing Agents - pharmacology</topic><topic>Rats</topic><topic>Species Specificity</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moss, Donald E.</creatorcontrib><creatorcontrib>Fahrney, David</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>Biochemical pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moss, Donald E.</au><au>Fahrney, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetic analysis of differences in brain acetylcholinesterase from fish or mammalian sources</atitle><jtitle>Biochemical pharmacology</jtitle><addtitle>Biochem Pharmacol</addtitle><date>1978</date><risdate>1978</risdate><volume>27</volume><issue>23</issue><spage>2693</spage><epage>2698</epage><pages>2693-2698</pages><issn>0006-2952</issn><eissn>1873-2968</eissn><abstract>A kinetic analysis of the interactions of gold fish and rat brain AChE (acetylcholine acetylhydrolase, EC 3.1.1.7) with acetylthiocholine substrate and sulfonyl fluoride inhibitors revealed several differences between these enzymes. The fish brain AChE had a
K
m
of 250 μM while the mammalian brain AChE had a
K
m
of 55 μM under the same assay conditions. In addition, the mammalian brain enzyme reacted with methanesulfonyl fluoride at more than three times the rate at which the fish enzyme reacted, and fish AChE did not react with phenylmethanesulfonyl fluoride at a measurable rate while mammalian AChE was found to react rapidly. Leptocurares were found to accelerate methanesulfonylation of both enzymes; however, they inhibited phenylmethanesulfonylation. These results suggest that fish and mammalian AChE may have topographic differences in the vicinity of the anionic portion of the active site.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>215165</pmid><doi>10.1016/0006-2952(78)90044-8</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical pharmacology, 1978, Vol.27 (23), p.2693-2698 |
| issn | 0006-2952 1873-2968 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Acetylcholinesterase - metabolism Animals Brain - enzymology Cholinesterase Inhibitors Fishes - metabolism In Vitro Techniques Kinetics Mesylates - pharmacology Neuromuscular Depolarizing Agents - pharmacology Neuromuscular Nondepolarizing Agents - pharmacology Rats Species Specificity Substrate Specificity |
| title | Kinetic analysis of differences in brain acetylcholinesterase from fish or mammalian sources |
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