Overproduction, Purification, and Characterization of Recombinant Aspartate Semialdehyde Dehydrogenase from Arabidopsis thaliana
In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. In this study, we report the first cDNA cloning, purification, and characterization of a plant ASDH. The Arabidopsis thaliana ASDH is...
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| Veröffentlicht in: | Protein expression and purification 2002-02, Vol.24 (1), p.99-104 |
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| creator | Paris, Stephane Wessel, Peter M. Dumas, Renaud |
| description | In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. In this study, we report the first cDNA cloning, purification, and characterization of a plant ASDH. The Arabidopsis thaliana ASDH is an homodimeric enzyme composed of subunits of 36 kDa. The plant enzyme exhibited a specific activity of 26 μmol NADPH oxidized min−1 mg−1 of protein with a KM value for NADPH of 92 μM. ASDH showed cooperative behavior for aspartyl phosphate with a K0.5 value of 37 μM. |
| doi_str_mv | 10.1006/prep.2001.1538 |
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ASDH showed cooperative behavior for aspartyl phosphate with a K0.5 value of 37 μM.</description><identifier>ISSN: 1046-5928</identifier><identifier>EISSN: 1096-0279</identifier><identifier>DOI: 10.1006/prep.2001.1538</identifier><identifier>PMID: 11812229</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis thaliana ; ASADH ; ASDH ; Aspartate-Semialdehyde Dehydrogenase - chemistry ; Aspartate-Semialdehyde Dehydrogenase - genetics ; Aspartate-Semialdehyde Dehydrogenase - isolation & purification ; Cloning, Molecular ; DNA, Complementary ; Escherichia coli - genetics ; Gene Expression ; Kinetics ; Molecular Sequence Data ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Solutions</subject><ispartof>Protein expression and purification, 2002-02, Vol.24 (1), p.99-104</ispartof><rights>2002 Elsevier Science (USA)</rights><rights>Copyright 2002 Elsevier Science (USA).</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-9b883e60262e973386e61e6f341b2e4a9aa7f99e983b683b8bd063b4f08532b3</citedby><cites>FETCH-LOGICAL-c406t-9b883e60262e973386e61e6f341b2e4a9aa7f99e983b683b8bd063b4f08532b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/prep.2001.1538$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11812229$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Paris, Stephane</creatorcontrib><creatorcontrib>Wessel, Peter M.</creatorcontrib><creatorcontrib>Dumas, Renaud</creatorcontrib><title>Overproduction, Purification, and Characterization of Recombinant Aspartate Semialdehyde Dehydrogenase from Arabidopsis thaliana</title><title>Protein expression and purification</title><addtitle>Protein Expr Purif</addtitle><description>In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. 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ASDH showed cooperative behavior for aspartyl phosphate with a K0.5 value of 37 μM.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis thaliana</subject><subject>ASADH</subject><subject>ASDH</subject><subject>Aspartate-Semialdehyde Dehydrogenase - chemistry</subject><subject>Aspartate-Semialdehyde Dehydrogenase - genetics</subject><subject>Aspartate-Semialdehyde Dehydrogenase - isolation & purification</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary</subject><subject>Escherichia coli - genetics</subject><subject>Gene Expression</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Analysis, Protein</subject><subject>Sequence Homology, Amino Acid</subject><subject>Solutions</subject><issn>1046-5928</issn><issn>1096-0279</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAQhi0EoqVw5Yh84tRs_ZF17ONqoRSpUhH0bo2dCWuUxMF2KrUnfjoJu1JPHKzxjJ55pXkIec_ZhjOmrqaE00Ywxjd8K_ULcs6ZURUTjXm5_mtVbY3QZ-RNzr8Wiiu2fU3OONdcCGHOyZ-7B0xTiu3sS4jjJf02p9AFD8cOxpbuD5DAF0zh6d-Uxo5-Rx8HF0YYC93lCVKBgvQHDgH6Fg-PLdJPa0nxJ46QkXYpDnSXwIU2TjlkWg7QBxjhLXnVQZ_x3alekPvrz_f7m-r27svX_e628jVTpTJOa4mKCSXQNFJqhYqj6mTNncAaDEDTGYNGS6eWp13LlHR1x_RWCicvyMdj7HLr7xlzsUPIHvseRoxztg2vmdENX8DNEfQp5pyws1MKA6RHy5ldldtVuV2V21X5svDhlDy7Adtn_OR4AfQRwOW8h4DJZh9w9NiGhL7YNob_Zf8FA_eSrw</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>Paris, Stephane</creator><creator>Wessel, Peter M.</creator><creator>Dumas, Renaud</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>20020201</creationdate><title>Overproduction, Purification, and Characterization of Recombinant Aspartate Semialdehyde Dehydrogenase from Arabidopsis thaliana</title><author>Paris, Stephane ; Wessel, Peter M. ; Dumas, Renaud</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-9b883e60262e973386e61e6f341b2e4a9aa7f99e983b683b8bd063b4f08532b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis thaliana</topic><topic>ASADH</topic><topic>ASDH</topic><topic>Aspartate-Semialdehyde Dehydrogenase - chemistry</topic><topic>Aspartate-Semialdehyde Dehydrogenase - genetics</topic><topic>Aspartate-Semialdehyde Dehydrogenase - isolation & purification</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary</topic><topic>Escherichia coli - genetics</topic><topic>Gene Expression</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Analysis, Protein</topic><topic>Sequence Homology, Amino Acid</topic><topic>Solutions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Paris, Stephane</creatorcontrib><creatorcontrib>Wessel, Peter M.</creatorcontrib><creatorcontrib>Dumas, Renaud</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>Protein expression and purification</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Paris, Stephane</au><au>Wessel, Peter M.</au><au>Dumas, Renaud</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overproduction, Purification, and Characterization of Recombinant Aspartate Semialdehyde Dehydrogenase from Arabidopsis thaliana</atitle><jtitle>Protein expression and purification</jtitle><addtitle>Protein Expr Purif</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>24</volume><issue>1</issue><spage>99</spage><epage>104</epage><pages>99-104</pages><issn>1046-5928</issn><eissn>1096-0279</eissn><abstract>In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. In this study, we report the first cDNA cloning, purification, and characterization of a plant ASDH. The Arabidopsis thaliana ASDH is an homodimeric enzyme composed of subunits of 36 kDa. The plant enzyme exhibited a specific activity of 26 μmol NADPH oxidized min−1 mg−1 of protein with a KM value for NADPH of 92 μM. ASDH showed cooperative behavior for aspartyl phosphate with a K0.5 value of 37 μM.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11812229</pmid><doi>10.1006/prep.2001.1538</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis thaliana ASADH ASDH Aspartate-Semialdehyde Dehydrogenase - chemistry Aspartate-Semialdehyde Dehydrogenase - genetics Aspartate-Semialdehyde Dehydrogenase - isolation & purification Cloning, Molecular DNA, Complementary Escherichia coli - genetics Gene Expression Kinetics Molecular Sequence Data Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Analysis, Protein Sequence Homology, Amino Acid Solutions |
| title | Overproduction, Purification, and Characterization of Recombinant Aspartate Semialdehyde Dehydrogenase from Arabidopsis thaliana |
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