EC |
2.4.2.59 |
Accepted name: |
sulfide-dependent adenosine diphosphate thiazole synthase |
Reaction: |
NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O |
Other name(s): |
Thi4 (ambiguous) |
Systematic name: |
NAD+:glycine ADP-D-ribosyltransferase (sulfide-adding) |
Comments: |
This iron dependent enzyme, found in most archaea, is involved in the biosynthesis of thiamine phosphate. The homologous enzyme from plants and fungi (EC 2.4.2.60, cysteine-dependent adenosine diphosphate thiazole synthase) uses an intrinsic cysteine as sulfur donor and, unlike the archaeal enzyme, is a single turn-over enzyme. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
References: |
1. |
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] |
2. |
Eser, B.E., Zhang, X., Chanani, P.K., Begley, T.P. and Ealick, S.E. From suicide enzyme to catalyst: the iron-dependent sulfide transfer in Methanococcus jannaschii thiamin thiazole biosynthesis. J. Am. Chem. Soc. 138 (2016) 3639–3642. [DOI] [PMID: 26928142] |
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[EC 2.4.2.59 created 2018] |
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