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Coomassie αLA LipS in vitro activity. Recombinant LipS was purified and assayed in the presence of protein substrate and cofactor S-adenosylmethionine.

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Presentation on theme: "Coomassie αLA LipS in vitro activity. Recombinant LipS was purified and assayed in the presence of protein substrate and cofactor S-adenosylmethionine."— Presentation transcript:

1 Coomassie αLA LipS in vitro activity. Recombinant LipS was purified and assayed in the presence of protein substrate and cofactor S-adenosylmethionine (SAM). The product of SAM cleavage (5’ dA) was monitored over the course of LipS reaction. E1 αKGDH E2 PDHC LipS E3 αKGDH and PDHC E2 αKGDH H Protein Malaria LipS binds to the 3 lipoate-dependent enzyme complexes found in E. coli. The labeled bands were identified by amino acid sequencing and/or anti-lipoate Western blot. Tight LipS/substrate complexes will now be used to stabilize LipS, and to characterize the mechanism guiding substrate specificity.


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