2-iminoacetate synthase
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| 2-iminoacetate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.99.19 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-iminoacetate synthase (EC 4.1.99.19, thiH (gene)) is an enzyme with systematic name L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- L-tyrosine + S-adenosyl-L-methionine + reduced acceptor 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+
This enzyme binds a 4Fe-4S cluster.
References
- ^ Leonardi R, Fairhurst SA, Kriek M, Lowe DJ, Roach PL (March 2003). "Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex". FEBS Letters. 539 (1–3): 95–9. doi:10.1016/s0014-5793(03)00204-7. PMID 12650933.
- ^ Kriek M, Martins F, Challand MR, Croft A, Roach PL (2007). "Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine". Angewandte Chemie. 46 (48): 9223–6. doi:10.1002/anie.200702554. PMID 17969213.
- ^ Kriek M, Martins F, Leonardi R, Fairhurst SA, Lowe DJ, Roach PL (June 2007). "Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro". The Journal of Biological Chemistry. 282 (24): 17413–23. doi:10.1074/jbc.M700782200. PMID 17403671.
External links
- 2-iminoacetate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
