Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous
A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including Drosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequenc...
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| Veröffentlicht in: | Journal of molecular evolution 1990-10, Vol.31 (4), p.325-329 |
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| container_title | Journal of molecular evolution |
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| creator | JACKSON, F. R |
| description | A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including Drosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases. |
| doi_str_mv | 10.1007/BF02101126 |
| format | Article |
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Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</description><identifier>ISSN: 0022-2844</identifier><identifier>EISSN: 1432-1432</identifier><identifier>DOI: 10.1007/BF02101126</identifier><identifier>PMID: 2124279</identifier><identifier>CODEN: JMEVAU</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Biological Evolution ; Carboxy-Lyases - chemistry ; Carboxy-Lyases - genetics ; Coenzymes ; Drosophila - enzymology ; Enterobacteriaceae - enzymology ; Fundamental and applied biological sciences. Psychology ; Genetics of eukaryotes. 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R</creatorcontrib><title>Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title><title>Journal of molecular evolution</title><addtitle>J Mol Evol</addtitle><description>A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including Drosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biological Evolution</subject><subject>Carboxy-Lyases - chemistry</subject><subject>Carboxy-Lyases - genetics</subject><subject>Coenzymes</subject><subject>Drosophila - enzymology</subject><subject>Enterobacteriaceae - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics of eukaryotes. Biological and molecular evolution</subject><subject>Molecular Sequence Data</subject><subject>Pyridoxal Phosphate - physiology</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0022-2844</issn><issn>1432-1432</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EKqWwsCNlgQEp4M84HqGigFQJBpijS2xDIImLnUjtv8cVUTuynHW-R6_uHoTOCb4hGMvb-wWmBBNCswM0JZzRdFsO0RRjSlOac36MTkL4wphIodgETSihnEo1RctX777Bb1xfVwl0OjHDrl1tfK3dGppUm5XptOn6RJsKfOnWmwaCCQl4k3y61jXuww3hFB1ZaII5G98Zel88vM2f0uXL4_P8bplWTKo-tTwHaVimspKIDJQQ1pZCcaatxIpaTYnNOQFZKml5BlIZiDcQZeMXlJrN0NVf7sq7n8GEvmjrUJmmgc7ENYo83smkyP4FiZBSRhMRvP4DK-9C8MYWK1-3UURBcLF1XOwdR_hiTB3K1ugdOkqN88txDqGCxnroqjrsExUTjOWE_QIJZIP1</recordid><startdate>199010</startdate><enddate>199010</enddate><creator>JACKSON, F. 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R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</atitle><jtitle>Journal of molecular evolution</jtitle><addtitle>J Mol Evol</addtitle><date>1990-10</date><risdate>1990</risdate><volume>31</volume><issue>4</issue><spage>325</spage><epage>329</epage><pages>325-329</pages><issn>0022-2844</issn><eissn>1432-1432</eissn><coden>JMEVAU</coden><abstract>A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including Drosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</abstract><cop>New York, NY</cop><pub>Springer</pub><pmid>2124279</pmid><doi>10.1007/BF02101126</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of molecular evolution, 1990-10, Vol.31 (4), p.325-329 |
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| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Animals Biological and medical sciences Biological Evolution Carboxy-Lyases - chemistry Carboxy-Lyases - genetics Coenzymes Drosophila - enzymology Enterobacteriaceae - enzymology Fundamental and applied biological sciences. Psychology Genetics of eukaryotes. Biological and molecular evolution Molecular Sequence Data Pyridoxal Phosphate - physiology Sequence Homology, Nucleic Acid |
| title | Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous |
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