2-iminoacetate synthase
2-iminoacetate synthase | |||||||||
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Identifiers | |||||||||
EC number | 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 | ||||||||
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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, S.A.; Kriek, M.; Lowe, D.J.; Roach, P.L. (2003). "Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex". FEBS Lett. 539 (1-3): 95–99. doi:10.1016/s0014-5793(03)00204-7. PMID 12650933.
- ↑ Kriek, M.; Martins, F.; Challand, M.R.; Croft, A.; Roach, P.L. (2007). "Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine". Angew. Chem. Int. Ed. Engl. 46: 9223–9226. doi:10.1002/anie.200702554. PMID 17969213.
- ↑ Kriek, M.; Martins, F.; Leonardi, R.; Fairhurst, S.A.; Lowe, D.J.; Roach, P.L. (2007). "Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro". J. Biol. Chem. 282: 17413–17423. doi:10.1074/jbc.M700782200. PMID 17403671.
External links
- 2-iminoacetate synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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