Sulfur carrier protein ThiS adenylyltransferase

Sulfur carrier protein ThiS adenylyltransferase
Identifiers
EC number 2.7.7.73
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Sulfur carrier protein ThiS adenylyltransferase (EC 2.7.7.73, thiF (gene)) is an enzyme with systematic name ATP:(ThiS) adenylyltransferase.[1][2][3][4] This enzyme catalyses the following chemical reaction

ATP + [ThiS] \rightleftharpoons diphosphate + adenylyl-[ThiS]

This enzyme binds Zn2+. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.

References

  1. Taylor, S.V., Kelleher, N.L., Kinsland, C., Chiu, H.J., Costello, C.A., Backstrom, A.D., McLafferty, F.W. and Begley, T.P. (1998). "Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation". J. Biol. Chem. 273 (26): 16555–16560. doi:10.1074/jbc.273.26.16555. PMID 9632726.
  2. Xi, J., Ge, Y., Kinsland, C., McLafferty, F.W. and Begley, T.P. (2001). "Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein-protein conjugate that is functionally analogous to the ubiquitin/E1 complex". Proc. Natl. Acad. Sci. USA 98 (15): 8513–8518. doi:10.1073/pnas.141226698. PMC 37467. PMID 11438688.
  3. Duda, D.M., Walden, H., Sfondouris, J. and Schulman, B.A. (2005). "Structural analysis of Escherichia coli ThiF". J. Mol. Biol. 349 (4): 774–786. doi:10.1016/j.jmb.2005.04.011. PMID 15896804.
  4. Lehmann, C., Begley, T.P. and Ealick, S.E. (2006). "Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis". Biochemistry 45 (1): 11–19. doi:10.1021/bi051502y. PMC 2566941. PMID 16388576.

External links

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