ExplorEnz: EC 2.4.2.60

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2.4.2.60

Accepted name:

cysteine-dependent adenosine diphosphate thiazole synthase

Reaction:

NAD⁺ + glycine + [ADP-thiazole synthase]-L-cysteine = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + [ADP-thiazole synthase]-dehydroalanine + 3 H₂O

Other name(s):

THI4 (gene name) (ambiguous); THI1 (gene name); ADP-thiazole synthase

Systematic name:

NAD⁺:glycine ADP-D-ribosyltransferase (dehydroalanine-producing)

Comments:

This iron dependent enzyme, found in fungi, plants, and some archaea, is involved in the thiamine phosphate biosynthesis pathway. It is a single turn-over enzyme since the cysteine residue is not regenerated in vivo [3]. The homologous enzyme in archaea (EC 2.4.2.59, sulfide-dependent adenosine diphosphate thiazole synthase) uses sulfide as sulfur donor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Godoi, P.H., Galhardo, R.S., Luche, D.D., Van Sluys, M.A., Menck, C.F. and Oliva, G. Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana. J. Biol. Chem. 281 (2006) 30957–30966. [DOI] [PMID: 16912043]
2.	Chatterjee, A., Abeydeera, N.D., Bale, S., Pai, P.J., Dorrestein, P.C., Russell, D.H., Ealick, S.E. and Begley, T.P. Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase. Nature 478 (2011) 542–546. [DOI] [PMID: 22031445]
3.	Zhang, X., Eser, B.E., Chanani, P.K., Begley, T.P. and Ealick, S.E. Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases. Biochemistry 55 (2016) 1826–1838. [DOI] [PMID: 26919468]
4.	Hwang, S., Cordova, B., Chavarria, N., Elbanna, D., McHugh, S., Rojas, J., Pfeiffer, F. and Maupin-Furlow, J.A. Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii. BMC Microbiol. 14:260 (2014). [PMID: 25348237]

[EC 2.4.2.60 created 2018]