Young Sil Min

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About

Young Sil Min has made significant contributions to structural enzymology, with a particular focus on vitamin B12 metabolism and the mechanistic understanding of coenzyme B12 biosynthesis. Her landmark work includes the determination of the crystal structure of a PduO-type ATP:cobalamin adenosyltransferase from *Burkholderia thailandensis*, an enzyme that catalyzes the conversion of cobalamin to adenosylcobalamin—the biologically active coenzyme B12. This study, published in 2008, provided critical insights into how the enzyme transfers a 5′-deoxyadenosyl moiety from ATP to the cobalt atom of cobalamin, revealing the structural basis for this essential radical-generating step in bacterial metabolism. Though her most-cited paper has accumulated 5 citations, its impact lies in its foundational contribution to the field of B12 enzymology, offering a detailed molecular framework for understanding adenosyltransferase function. Min’s work has implications for both microbial physiology and potential therapeutic applications, as coenzyme B12 is vital for DNA synthesis and energy metabolism. Her research exemplifies the power of structural biology in unraveling complex enzymatic mechanisms, making her a respected figure in the study of vitamin B12-dependent processes.