The enzymology of sulfur activation during thiamin and biotin biosynthesis. Academic Article

abstract

• The thiamin and biotin biosynthetic pathways utilize elaborate strategies for the transfer of sulfur from cysteine to cofactor precursors. For thiamin, the sulfur atom of cysteine is transferred to a 66-amino-acid peptide (ThiS) to form a carboxy-terminal thiocarboxylate group. This sulfur transfer requires three enzymes and proceeds via a ThiS-acyladenylate intermediate. The biotin synthase Fe-S cluster functions as the immediate sulfur donor for biotin formation. C-S bond formation proceeds via radical intermediates that are generated by hydrogen atom transfer from dethiobiotin to the adenosyl radical. This radical is formed by the reductive cleavage of S-adenosylmethionine by the reduced Fe-S cluster of biotin synthase.

authors

• Begley, Tadhg

published proceedings

• Curr Opin Chem Biol

author list (cited authors)

• Begley, T. P., Xi, J., Kinsland, C., Taylor, S., & McLafferty, F.

citation count

• 100

complete list of authors

• Begley, TP||Xi, J||Kinsland, C||Taylor, S||McLafferty, F

publication date

• January 1999

publisher

• Elsevier  Publisher

published in

• Current Opinion in Chemical Biology  Journal

keywords

• Biotin
• Cysteine
• Models, Chemical
• Phosphotransferases (Alcohol Group Acceptor)
• Sulfur
• Sulfurtransferases
• Thiamine

PubMed Central ID

• 10508664

Digital Object Identifier (DOI)

• 10.1016/s1367-5931(99)00018-6

start page

• 623

end page

• 629

volume

• 3

issue

• 5

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fs1367-5931%2899%2900018-6