Enzymic preparation and characterization of an α- l-β-methylaspartic acid
Charcoal-treated extracts of Clostridium tetanomorphum, incubated with mesaconate and an ammonium salt under suitable conditions, catalyze the formation of large amounts of a dicarboxylic amino acid which has been isolated and shown to be an α- l-β-methylaspartic acid. The compound has been tentativ...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1958-12, Vol.78 (2), p.468-476 |
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| container_end_page | 476 |
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| container_issue | 2 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 78 |
| creator | Barker, H.A. Smyth, R.D. Wawszkiewicz, E.J. Lee, Mary N. Wilson, R.Marilyn |
| description | Charcoal-treated extracts of
Clostridium tetanomorphum, incubated with mesaconate and an ammonium salt under suitable conditions, catalyze the formation of large amounts of a dicarboxylic amino acid which has been isolated and shown to be an α-
l-β-methylaspartic acid. The compound has been tentatively identified as the
l-
threo isomer. A simple enzymic method is given for preparing 15 g. of the pure amino acid. A spectrophotometric method for the quantitative determination of enzymic β-methylaspartic acid in amounts of 0.02-0.25 μmole is described. |
| doi_str_mv | 10.1016/0003-9861(58)90371-0 |
| format | Article |
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Clostridium tetanomorphum, incubated with mesaconate and an ammonium salt under suitable conditions, catalyze the formation of large amounts of a dicarboxylic amino acid which has been isolated and shown to be an α-
l-β-methylaspartic acid. The compound has been tentatively identified as the
l-
threo isomer. A simple enzymic method is given for preparing 15 g. of the pure amino acid. A spectrophotometric method for the quantitative determination of enzymic β-methylaspartic acid in amounts of 0.02-0.25 μmole is described.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(58)90371-0</identifier><identifier>PMID: 13618029</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aspartic Acid - analogs & derivatives ; Clostridium - metabolism ; Old Medline</subject><ispartof>Archives of biochemistry and biophysics, 1958-12, Vol.78 (2), p.468-476</ispartof><rights>1958</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c358t-bba9147562be822d1328c0a7cb981b7f56d2ec00b043577261bbe3cf0f0d4bc13</citedby><cites>FETCH-LOGICAL-c358t-bba9147562be822d1328c0a7cb981b7f56d2ec00b043577261bbe3cf0f0d4bc13</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(58)90371-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13618029$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Barker, H.A.</creatorcontrib><creatorcontrib>Smyth, R.D.</creatorcontrib><creatorcontrib>Wawszkiewicz, E.J.</creatorcontrib><creatorcontrib>Lee, Mary N.</creatorcontrib><creatorcontrib>Wilson, R.Marilyn</creatorcontrib><title>Enzymic preparation and characterization of an α- l-β-methylaspartic acid</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Charcoal-treated extracts of
Clostridium tetanomorphum, incubated with mesaconate and an ammonium salt under suitable conditions, catalyze the formation of large amounts of a dicarboxylic amino acid which has been isolated and shown to be an α-
l-β-methylaspartic acid. The compound has been tentatively identified as the
l-
threo isomer. A simple enzymic method is given for preparing 15 g. of the pure amino acid. A spectrophotometric method for the quantitative determination of enzymic β-methylaspartic acid in amounts of 0.02-0.25 μmole is described.</description><subject>Aspartic Acid - analogs & derivatives</subject><subject>Clostridium - metabolism</subject><subject>Old Medline</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1958</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKBDEQRYMoOj7-QKRXootoJelOpzeCiC8U3Og6JOlqjPRjTHqE8a_0Q_wmM86gO1dFinNvkUPIPoMTBkyeAoCglZLsqFDHFYiSUVgjEwaVpCBUvk4mv8gW2Y7xBYCxXPJNssWEZAp4NSF3l_37vPMumwacmmBGP_SZ6evMPaeXGzH49-VyaNI--_qgWUu_PmmH4_O8NTGFxhQ3zte7ZKMxbcS91dwhT1eXjxc39P7h-vbi_J46UaiRWmsqlpeF5BYV5zUTXDkwpbOVYrZsCllzdAAWclGUJZfMWhSugQbq3DomdsjhsncahtcZxlF3PjpsW9PjMIs6lcoq5yqB-RJ0YYgxYKOnwXcmzDUDvZCoF4b0wpAulP6RqCHFDlb9M9th_RdaWUvA2RLA9Ms3j0FH57F3WPuAbtT14P-_8A2bCIHm</recordid><startdate>195812</startdate><enddate>195812</enddate><creator>Barker, H.A.</creator><creator>Smyth, R.D.</creator><creator>Wawszkiewicz, E.J.</creator><creator>Lee, Mary N.</creator><creator>Wilson, R.Marilyn</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>195812</creationdate><title>Enzymic preparation and characterization of an α- l-β-methylaspartic acid</title><author>Barker, H.A. ; Smyth, R.D. ; Wawszkiewicz, E.J. ; Lee, Mary N. ; Wilson, R.Marilyn</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-bba9147562be822d1328c0a7cb981b7f56d2ec00b043577261bbe3cf0f0d4bc13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1958</creationdate><topic>Aspartic Acid - analogs & derivatives</topic><topic>Clostridium - metabolism</topic><topic>Old Medline</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barker, H.A.</creatorcontrib><creatorcontrib>Smyth, R.D.</creatorcontrib><creatorcontrib>Wawszkiewicz, E.J.</creatorcontrib><creatorcontrib>Lee, Mary N.</creatorcontrib><creatorcontrib>Wilson, R.Marilyn</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>Barker, H.A.</au><au>Smyth, R.D.</au><au>Wawszkiewicz, E.J.</au><au>Lee, Mary N.</au><au>Wilson, R.Marilyn</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymic preparation and characterization of an α- l-β-methylaspartic acid</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1958-12</date><risdate>1958</risdate><volume>78</volume><issue>2</issue><spage>468</spage><epage>476</epage><pages>468-476</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Charcoal-treated extracts of
Clostridium tetanomorphum, incubated with mesaconate and an ammonium salt under suitable conditions, catalyze the formation of large amounts of a dicarboxylic amino acid which has been isolated and shown to be an α-
l-β-methylaspartic acid. The compound has been tentatively identified as the
l-
threo isomer. A simple enzymic method is given for preparing 15 g. of the pure amino acid. A spectrophotometric method for the quantitative determination of enzymic β-methylaspartic acid in amounts of 0.02-0.25 μmole is described.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>13618029</pmid><doi>10.1016/0003-9861(58)90371-0</doi><tpages>9</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1958-12, Vol.78 (2), p.468-476 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Aspartic Acid - analogs & derivatives Clostridium - metabolism Old Medline |
| title | Enzymic preparation and characterization of an α- l-β-methylaspartic acid |
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