PMID:26928142

Eser BE, Zhang X, Chanani PK, Begley TP, Ealick SE

From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis.

J Am Chem Soc 138:3639-42 (2016)
DOI:10.1021/jacs.6b00445

[mja:MJ_0601]

PMID:25348237

Hwang S, Cordova B, Chavarria N, Elbanna D, McHugh S, Rojas J, Pfeiffer F, Maupin-Furlow JA

Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii.

BMC Microbiol 14:260 (2014)
DOI:10.1186/s12866-014-0260-0

[hvo:HVO_0665]

Transferases;
Glycosyltransferases;
Pentosyltransferases
BRITE hierarchy

NAD+:glycine ADP-D-ribosyltransferase (sulfide-adding)

NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O [RN:R12026]

R12026
Reaction

NAD+ [CPD:C00003];
glycine [CPD:C00037];
sulfide [CPD:C00283]

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.

EC 2.4.2.59 created 2018

1  [PMID:26919468]

Zhang X, Eser BE, Chanani PK, Begley TP, Ealick SE

Structural Basis for Iron-Mediated Sulfur Transfer in Archael and Yeast Thiazole  Synthases.

Biochemistry 55:1826-38 (2016)
DOI:10.1021/acs.biochem.6b00030

[mja:MJ_0601] [mig:Metig_0735]

2  [PMID:26928142]

Eser BE, Zhang X, Chanani PK, Begley TP, Ealick SE

From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis.

J Am Chem Soc 138:3639-42 (2016)
DOI:10.1021/jacs.6b00445

[mja:MJ_0601]