(Redirected from
ATP:(ThiS) adenylyltransferase)
| Sulfur carrier protein ThiS adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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] diphosphate + adenylyl-[ThiS]
This enzyme binds Zn2+. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
- ^ Taylor SV, Kelleher NL, Kinsland C, Chiu HJ, Costello CA, Backstrom AD, McLafferty FW, Begley TP (June 1998). "Thiamin biosynthesis in Escherichia coli. Identification of ThiS thiocarboxylate as the immediate sulfur donor in the thiazole formation". The Journal of Biological Chemistry. 273 (26): 16555–60. doi: 10.1074/jbc.273.26.16555. PMID 9632726.
- ^ Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP (July 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". Proceedings of the National Academy of Sciences of the United States of America. 98 (15): 8513–8. doi: 10.1073/pnas.141226698. PMC 37467. PMID 11438688.
- ^ Duda DM, Walden H, Sfondouris J, Schulman BA (June 2005). "Structural analysis of Escherichia coli ThiF". Journal of Molecular Biology. 349 (4): 774–86. doi: 10.1016/j.jmb.2005.04.011. PMID 15896804.
- ^ Lehmann C, Begley TP, Ealick SE (January 2006). "Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis". Biochemistry. 45 (1): 11–9. doi: 10.1021/bi051502y. PMC 2566941. PMID 16388576.
- Sulfur+carrier+protein+ThiS+adenylyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
(Redirected from
ATP:(ThiS) adenylyltransferase)
| Sulfur carrier protein ThiS adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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] diphosphate + adenylyl-[ThiS]
This enzyme binds Zn2+. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
- ^ Taylor SV, Kelleher NL, Kinsland C, Chiu HJ, Costello CA, Backstrom AD, McLafferty FW, Begley TP (June 1998). "Thiamin biosynthesis in Escherichia coli. Identification of ThiS thiocarboxylate as the immediate sulfur donor in the thiazole formation". The Journal of Biological Chemistry. 273 (26): 16555–60. doi: 10.1074/jbc.273.26.16555. PMID 9632726.
- ^ Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP (July 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". Proceedings of the National Academy of Sciences of the United States of America. 98 (15): 8513–8. doi: 10.1073/pnas.141226698. PMC 37467. PMID 11438688.
- ^ Duda DM, Walden H, Sfondouris J, Schulman BA (June 2005). "Structural analysis of Escherichia coli ThiF". Journal of Molecular Biology. 349 (4): 774–86. doi: 10.1016/j.jmb.2005.04.011. PMID 15896804.
- ^ Lehmann C, Begley TP, Ealick SE (January 2006). "Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis". Biochemistry. 45 (1): 11–9. doi: 10.1021/bi051502y. PMC 2566941. PMID 16388576.
- Sulfur+carrier+protein+ThiS+adenylyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)