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
| 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 | ||||||||
| |||||||||
- 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
edit- ^ 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 12650933.1–3&rft.pages=95-9&rft.date=2003-03&rft_id=info:doi/10.1016/s0014-5793(03)00204-7&rft_id=info:pmid/12650933&rft.aulast=Leonardi&rft.aufirst=R&rft.au=Fairhurst, SA&rft.au=Kriek, M&rft.au=Lowe, DJ&rft.au=Roach, PL&rft_id=https://doi.org/10.1016%2Fs0014-5793%2803%2900204-7&rfr_id=info:sid/en.wikipedia.org:2-iminoacetate synthase" class="Z3988">
- ^ 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 17969213.9223-6&rft.date=2007&rft_id=info:doi/10.1002/anie.200702554&rft_id=info:pmid/17969213&rft.aulast=Kriek&rft.aufirst=M&rft.au=Martins, F&rft.au=Challand, MR&rft.au=Croft, A&rft.au=Roach, PL&rft_id=https://zenodo.org/record/2642082&rfr_id=info:sid/en.wikipedia.org:2-iminoacetate synthase" class="Z3988">
- ^ 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 17403671.17413-23&rft.date=2007-06&rft_id=info:doi/10.1074/jbc.M700782200&rft_id=info:pmid/17403671&rft.aulast=Kriek&rft.aufirst=M&rft.au=Martins, F&rft.au=Leonardi, R&rft.au=Fairhurst, SA&rft.au=Lowe, DJ&rft.au=Roach, PL&rft_id=https://doi.org/10.1074%2Fjbc.M700782200&rfr_id=info:sid/en.wikipedia.org:2-iminoacetate synthase" class="Z3988">
External links
edit- 2-iminoacetate synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
