Overexpression of biotin synthase and biotin ligase is required for efficient generation of sulfur-35 labeled biotin in <Emphasis Type="Italic">E. coli</Emphasis> |
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Authors: | Teegan A Delli-Bovi Maroya D Spalding Sean T Prigge |
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Institution: | (1) Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, 21205 Baltimore, MD, USA;(2) Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, 21205 Baltimore, MD, USA |
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Abstract: | Background Biotin is an essential enzyme cofactor that acts as a CO2 carrier in carboxylation and decarboxylation reactions. The E. coli genome encodes a biosynthetic pathway that produces biotin from pimeloyl-CoA in four enzymatic steps. The final step, insertion
of sulfur into desthiobiotin to form biotin, is catalyzed by the biotin synthase, BioB. A dedicated biotin ligase (BirA) catalyzes
the covalent attachment of biotin to biotin-dependent enzymes. Isotopic labeling has been a valuable tool for probing the
details of the biosynthetic process and assaying the activity of biotin-dependent enzymes, however there is currently no established
method for 35S labeling of biotin. |
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Keywords: | |
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