The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate
The protein lipoyl synthase (LipA) is essential for lipoic acid biosynthesis via sulfur insertions into a protein-bound octanoyl group. We have developed an in vitro assay for LipA using a synthetic tetrapeptide substrate, containing an N ε-octanoyl lysine residue, corresponding in sequence to the l...
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| Veröffentlicht in: | Analytical biochemistry 2006-04, Vol.351 (1), p.44-49 |
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| container_title | Analytical biochemistry |
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| creator | Bryant, Penny Kriek, Marco Wood, Robert J. Roach, Peter L. |
| description | The protein lipoyl synthase (LipA) is essential for lipoic acid biosynthesis via sulfur insertions into a protein-bound octanoyl group. We have developed an in vitro assay for LipA using a synthetic tetrapeptide substrate, containing an N
ε-octanoyl lysine residue, corresponding in sequence to the lipoyl binding domain of the E2 subunit of pyruvate dehydrogenase. A putative LipA from the hypothermophilic archaea
Sulfolobus solfataricus was expressed in
Escherichia coli and purified, and the activity was measured using this novel assay. The optimal temperature for the
S. solfataricus LipA-dependent formation of the lipoyl group was found to be 60
°C. |
| doi_str_mv | 10.1016/j.ab.2006.01.023 |
| format | Article |
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ε-octanoyl lysine residue, corresponding in sequence to the lipoyl binding domain of the E2 subunit of pyruvate dehydrogenase. A putative LipA from the hypothermophilic archaea
Sulfolobus solfataricus was expressed in
Escherichia coli and purified, and the activity was measured using this novel assay. The optimal temperature for the
S. solfataricus LipA-dependent formation of the lipoyl group was found to be 60
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ε-octanoyl lysine residue, corresponding in sequence to the lipoyl binding domain of the E2 subunit of pyruvate dehydrogenase. A putative LipA from the hypothermophilic archaea
Sulfolobus solfataricus was expressed in
Escherichia coli and purified, and the activity was measured using this novel assay. The optimal temperature for the
S. solfataricus LipA-dependent formation of the lipoyl group was found to be 60
°C.</description><subject>Base Sequence</subject><subject>Caprylates - metabolism</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cofactor biosynthesis</subject><subject>DNA Primers</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Ligases - metabolism</subject><subject>Lipoyl synthase</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Mass Spectrometry</subject><subject>Radical sam</subject><subject>Substrate Specificity</subject><subject>Sulfolobus solfataricus</subject><subject>Sulfolobus solfataricus - enzymology</subject><subject>Sulfur insertion</subject><subject>Temperature</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFr3DAQRkVoaTZp7zkVnXqzO5Js2e6thDYpBHpoehZjecRqkVdbSU7Zf18nu5BTT2LgvQf6GLsRUAsQ-vOuxrGWALoGUYNUF2wjYNAVKBjesA0AqErqobtkVznvAIRoWv2OXQrdrpKQGxYft8TRFv_ky5FHx5GXLaU55oJjIB78IR4Dz8d92WIm7lKc-a8luBjiuGSeY3BYMHm7Hn992a6BF5iKtzzagvsXfxlzSVjoPXvrMGT6cH6v2e_v3x5v76uHn3c_br8-VFY1fakGVCBQTi2ibZXCvuukalspR-j6cZrITrbpQckWpesH14kWOt3owckeBWp1zT6duocU_yyUi5l9thQC7iku2eiu06IRcgXhBNoUc07kzCH5GdPRCDDPI5udwdE8j2xAmHXkVfl4bi_jTNOrcF51Bb6cAFp_-OQpmWw97S1NPpEtZor-__V__rWNpw</recordid><startdate>20060401</startdate><enddate>20060401</enddate><creator>Bryant, Penny</creator><creator>Kriek, Marco</creator><creator>Wood, Robert J.</creator><creator>Roach, Peter L.</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>20060401</creationdate><title>The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate</title><author>Bryant, Penny ; Kriek, Marco ; Wood, Robert J. ; Roach, Peter L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c348t-9a301a2d5aac533a877235522b078bddecdc480325a2f89f715076469f28a1a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Base Sequence</topic><topic>Caprylates - metabolism</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cofactor biosynthesis</topic><topic>DNA Primers</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Stability</topic><topic>Ligases - metabolism</topic><topic>Lipoyl synthase</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Mass Spectrometry</topic><topic>Radical sam</topic><topic>Substrate Specificity</topic><topic>Sulfolobus solfataricus</topic><topic>Sulfolobus solfataricus - enzymology</topic><topic>Sulfur insertion</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bryant, Penny</creatorcontrib><creatorcontrib>Kriek, Marco</creatorcontrib><creatorcontrib>Wood, Robert J.</creatorcontrib><creatorcontrib>Roach, Peter L.</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>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bryant, Penny</au><au>Kriek, Marco</au><au>Wood, Robert J.</au><au>Roach, Peter L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>2006-04-01</date><risdate>2006</risdate><volume>351</volume><issue>1</issue><spage>44</spage><epage>49</epage><pages>44-49</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>The protein lipoyl synthase (LipA) is essential for lipoic acid biosynthesis via sulfur insertions into a protein-bound octanoyl group. We have developed an in vitro assay for LipA using a synthetic tetrapeptide substrate, containing an N
ε-octanoyl lysine residue, corresponding in sequence to the lipoyl binding domain of the E2 subunit of pyruvate dehydrogenase. A putative LipA from the hypothermophilic archaea
Sulfolobus solfataricus was expressed in
Escherichia coli and purified, and the activity was measured using this novel assay. The optimal temperature for the
S. solfataricus LipA-dependent formation of the lipoyl group was found to be 60
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| fulltext | fulltext |
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| ispartof | Analytical biochemistry, 2006-04, Vol.351 (1), p.44-49 |
| issn | 0003-2697 1096-0309 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Base Sequence Caprylates - metabolism Chromatography, High Pressure Liquid Cofactor biosynthesis DNA Primers Electrophoresis, Polyacrylamide Gel Enzyme Stability Ligases - metabolism Lipoyl synthase Magnetic Resonance Spectroscopy Mass Spectrometry Radical sam Substrate Specificity Sulfolobus solfataricus Sulfolobus solfataricus - enzymology Sulfur insertion Temperature |
| title | The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate |
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