Recombinant Oryza sativa subsp. japonica Lipoyl Synthase 2, chloroplastic (LIP1P-2) is a recombinant protein derived from the Japanese rice subspecies. This enzyme plays a crucial role in the biosynthesis of lipoic acid, a vital cofactor for several key metabolic enzymes. LIP1P-2 is specifically localized to the chloroplasts, where it catalyzes the radical-mediated insertion of two sulfur atoms into the octanoyl moiety of lipoate-dependent enzymes, converting them into lipoylated derivatives .
Function: LIP1P-2 is involved in the synthesis of lipoic acid, which is essential for the proper functioning of enzymes like pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase.
Localization: Chloroplastic, indicating its role in plant metabolism within the chloroplasts.
Expression System: Produced in E. coli, which is a common host for recombinant protein production due to its well-understood genetics and high yield .
The sequence of LIP1P-2 includes a specific arrangement of amino acids that facilitate its enzymatic activity. The full-length mature protein sequence is crucial for its function in converting octanoylated domains into lipoylated derivatives .
LIP1P-2 interacts with other proteins involved in metabolic pathways. Predicted functional partners include lipoate-protein ligase B and other lipoyl synthases, suggesting a complex network of interactions within the chloroplast .
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