Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae
S-Adenosylmethionine decarboxylase from Saccharomyces cerevisiae has been purified to homogeneity. Acid hydrolysis of NaB3H4-reduced enzyme released 2.2 mol of tritiated lactate per mol of dimeric enzyme, indicating that a pyruvate moiety is present. Inhibition of enzymatic activity by NaBH4 reducti...
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| Veröffentlicht in: | The Journal of biological chemistry 1977-11, Vol.252 (22), p.8212-8216 |
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| container_end_page | 8216 |
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| container_issue | 22 |
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| container_title | The Journal of biological chemistry |
| container_volume | 252 |
| creator | Cohn, M S Tabor, C W Tabor, H |
| description | S-Adenosylmethionine decarboxylase from Saccharomyces cerevisiae has been purified to homogeneity. Acid hydrolysis of NaB3H4-reduced
enzyme released 2.2 mol of tritiated lactate per mol of dimeric enzyme, indicating that a pyruvate moiety is present. Inhibition
of enzymatic activity by NaBH4 reduction and by carbonyl-binding reagents indicates that this pyruvoyl residue is required
for the activity of the enzyme. This is the first example reported of a eukaryotic enzyme containing a covalently linked pyruvoyl
residue. |
| doi_str_mv | 10.1016/S0021-9258(17)40957-4 |
| format | Article |
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enzyme released 2.2 mol of tritiated lactate per mol of dimeric enzyme, indicating that a pyruvate moiety is present. Inhibition
of enzymatic activity by NaBH4 reduction and by carbonyl-binding reagents indicates that this pyruvoyl residue is required
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enzyme released 2.2 mol of tritiated lactate per mol of dimeric enzyme, indicating that a pyruvate moiety is present. Inhibition
of enzymatic activity by NaBH4 reduction and by carbonyl-binding reagents indicates that this pyruvoyl residue is required
for the activity of the enzyme. This is the first example reported of a eukaryotic enzyme containing a covalently linked pyruvoyl
residue.</description><subject>Adenosylmethionine Decarboxylase - metabolism</subject><subject>Borohydrides - pharmacology</subject><subject>Carboxy-Lyases - metabolism</subject><subject>Pyruvates - metabolism</subject><subject>Saccharomyces cerevisiae - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kM1q3TAQRkXp323aN2hBUAjtwq2lkSxrWULaBgJZ3BS6E7I0qlVs61ay0_jt4-SGzGYGvjMzcAj5wOovrGbN131dc1ZpLttPTH0WtZaqEs_IjtUtVCDZ7-dk94S8Jm9K-VtvJTR7RV4CCKXUjvQXHqc5hujsHNNEU6CWHta83KR1oBlL9AvSONF9ZTcylXUYce43NE5IPTqbu3S7DrYgDTmNdG-d6-02rQ4LdZjxJpZo8S15EexQ8N1jPyG_vp9fn_2sLq9-XJx9u6wcqHaumPSh8UGD9oxbrSS6ELrAGgCuHAhk3vtOevC-ERqkBfQ1-KZxgIC6hRNyerx7yOnfgmU2YywOh8FOmJZiFDRSaKE2UB5Bl1MpGYM55DjavBpWm3vB5kGwubdnmDIPgo3Y9t4_Pli6Ef3T1tHoFn88xn380_-PGU0Xk-txNFxyw7lpOeNwB0HVhSA</recordid><startdate>19771125</startdate><enddate>19771125</enddate><creator>Cohn, M S</creator><creator>Tabor, C W</creator><creator>Tabor, H</creator><general>American Society for Biochemistry and Molecular Biology</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>19771125</creationdate><title>Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae</title><author>Cohn, M S ; Tabor, C W ; Tabor, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-15df6df939d12a975ecffbf163327c34e1dddb5d3dd64935a3ed03d66c3e3e983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Adenosylmethionine Decarboxylase - metabolism</topic><topic>Borohydrides - pharmacology</topic><topic>Carboxy-Lyases - metabolism</topic><topic>Pyruvates - metabolism</topic><topic>Saccharomyces cerevisiae - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cohn, M S</creatorcontrib><creatorcontrib>Tabor, C W</creatorcontrib><creatorcontrib>Tabor, H</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cohn, M S</au><au>Tabor, C W</au><au>Tabor, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1977-11-25</date><risdate>1977</risdate><volume>252</volume><issue>22</issue><spage>8212</spage><epage>8216</epage><pages>8212-8216</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>S-Adenosylmethionine decarboxylase from Saccharomyces cerevisiae has been purified to homogeneity. Acid hydrolysis of NaB3H4-reduced
enzyme released 2.2 mol of tritiated lactate per mol of dimeric enzyme, indicating that a pyruvate moiety is present. Inhibition
of enzymatic activity by NaBH4 reduction and by carbonyl-binding reagents indicates that this pyruvoyl residue is required
for the activity of the enzyme. This is the first example reported of a eukaryotic enzyme containing a covalently linked pyruvoyl
residue.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>334777</pmid><doi>10.1016/S0021-9258(17)40957-4</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1977-11, Vol.252 (22), p.8212-8216 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73654947 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Adenosylmethionine Decarboxylase - metabolism Borohydrides - pharmacology Carboxy-Lyases - metabolism Pyruvates - metabolism Saccharomyces cerevisiae - enzymology |
| title | Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae |
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