ExplorEnz: EC 4.1.99.19

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4.1.99.19

Accepted name:

2-iminoacetate synthase

Reaction:

L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5′-deoxyadenosine + L-methionine + NADP⁺ + H⁺

For diagram of thiamine diphosphate biosynthesis, click here

Glossary:

4-methylphenol = 4-cresol = p-cresol

Other name(s):

thiH (gene name)

Systematic name:

L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming)

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. The reductant is assumed to be NADPH, which is provided by a flavoprotein:NADPH oxidoreductase system [4]. Part of the pathway for thiamine biosynthesis.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

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

[EC 4.1.99.19 created 2011, modified 2014]