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- W2004642738 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 Nε-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." @default.
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- W2004642738 date "2006-04-01" @default.
- W2004642738 modified "2023-10-13" @default.
- W2004642738 title "The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate" @default.
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- W2004642738 doi "https://doi.org/10.1016/j.ab.2006.01.023" @default.
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