EC 4.1.99.19 - 2-iminoacetate synthase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 4.1.99.19

Names

Accepted name:
2-iminoacetate synthase
Other name:
thiH
Systematic name:
L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming)

Reaction

Cofactor

Comments:

Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce methionine and a 5-deoxyadenosin-5-yl radical that is crucial for the conversion of the substrate. Part of the pathway for thiamine biosynthesis. Formerly EC 1.3.99.n2.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0036355
UniProtKB/Swiss-Prot:

References

  1. Leonardi, R., Fairhurst, S. A., Kriek, M., Lowe, D. J., Roach, P. L.
    Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex.
    FEBS Lett. 539: 95-99 (2003). [PMID: 12650933]
  2. Kriek, M., Martins, F., Challand, M. R., Croft, A., Roach, P. L.
    Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine.
    Angew. Chem. Int. Ed. Engl. 46: 9223-9226 (2007). [PMID: 17969213]
  3. Kriek, M., Martins, F., Leonardi, R., Fairhurst, S. A., Lowe, D. J., Roach, P. L.
    Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro.
    J. Biol. Chem. 282: 17413-17423 (2007). [PMID: 17403671]
  4. Challand, M. R., Martins, F. T., Roach, P. L.
    Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli.
    J. Biol. Chem. 285: 5240-5248 (2010). [PMID: 19923213]

[EC 4.1.99.19 created 2011, modified 2014]