Enzymes
| UniProtKB help_outline | 1,738 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
[ADP-thiazole synthase]-L-cysteine
Identifier
RHEA-COMP:14264
Reactive part
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- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 123 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycine Identifier CHEBI:57305 Charge 0 Formula C2H5NO2 InChIKeyhelp_outline DHMQDGOQFOQNFH-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 135 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[ADP-thiazole synthase]-dehydroalanine
Identifier
RHEA-COMP:14265
Reactive part
help_outline
- Name help_outline dehydroalanine residue Identifier CHEBI:90873 Charge 0 Formula C3H3NO SMILEShelp_outline O=C(*)C(N*)=C 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP-5-ethyl-4-methylthiazole-2-carboxylate Identifier CHEBI:139151 Charge -3 Formula C17H19N6O12P2S InChIKeyhelp_outline VGXBGQACJQRWLV-LKGUXBDMSA-K SMILEShelp_outline C1(=NC(=C(S1)CCOP(OP(OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=NC=4C3=NC=NC4N)O)O)(=O)[O-])(=O)[O-])C)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nicotinamide Identifier CHEBI:17154 (Beilstein: 383619; CAS: 98-92-0) help_outline Charge 0 Formula C6H6N2O InChIKeyhelp_outline DFPAKSUCGFBDDF-UHFFFAOYSA-N SMILEShelp_outline NC(=O)c1cccnc1 2D coordinates Mol file for the small molecule Search links Involved in 60 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:55708 | RHEA:55709 | RHEA:55710 | RHEA:55711 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases.
Zhang X., Eser B.E., Chanani P.K., Begley T.P., Ealick S.E.
Thiamin diphosphate is an essential cofactor in all forms of life and plays a key role in amino acid and carbohydrate metabolism. Its biosynthesis involves separate syntheses of the pyrimidine and thiazole moieties, which are then coupled to form thiamin monophosphate. A final phosphorylation prod ... >> More
Thiamin diphosphate is an essential cofactor in all forms of life and plays a key role in amino acid and carbohydrate metabolism. Its biosynthesis involves separate syntheses of the pyrimidine and thiazole moieties, which are then coupled to form thiamin monophosphate. A final phosphorylation produces the active form of the cofactor. In most bacteria, six gene products are required for biosynthesis of the thiamin thiazole. In yeast and fungi only one gene product, Thi4, is required for thiazole biosynthesis. Methanococcus jannaschii expresses a putative Thi4 ortholog that was previously reported to be a ribulose 1,5-bisphosphate synthase [Finn, M. W. and Tabita, F. R. (2004) J. Bacteriol., 186, 6360-6366]. Our structural studies show that the Thi4 orthologs from M. jannaschii and Methanococcus igneus are structurally similar to Thi4 from Saccharomyces cerevisiae. In addition, all active site residues are conserved except for a key cysteine residue, which in S. cerevisiae is the source of the thiazole sulfur atom. Our recent biochemical studies showed that the archael Thi4 orthologs use nicotinamide adenine dinucleotide, glycine, and free sulfide to form the thiamin thiazole in an iron-dependent reaction [Eser, B., Zhang, X., Chanani, P. K., Begley, T. P., and Ealick, S. E. (2016) J. Am. Chem. Soc. , DOI: 10.1021/jacs.6b00445]. Here we report X-ray crystal structures of Thi4 from M. jannaschii complexed with ADP-ribulose, the C205S variant of Thi4 from S. cerevisiae with a bound glycine imine intermediate, and Thi4 from M. igneus with bound glycine imine intermediate and iron. These studies reveal the structural basis for the iron-dependent mechanism of sulfur transfer in archael and yeast thiazole synthases. << Less
Biochemistry 55:1826-1838(2016) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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From suicide enzyme to catalyst: The iron-dependent sulfide transfer in Methanococcus jannaschii thiamin thiazole biosynthesis.
Eser B.E., Zhang X., Chanani P.K., Begley T.P., Ealick S.E.
Bacteria and yeast utilize different strategies for sulfur incorporation in the biosynthesis of the thiamin thiazole. Bacteria use thiocarboxylated proteins. In contrast, Saccharomyces cerevisiae thiazole synthase (THI4p) uses an active site cysteine as the sulfide source and is inactivated after ... >> More
Bacteria and yeast utilize different strategies for sulfur incorporation in the biosynthesis of the thiamin thiazole. Bacteria use thiocarboxylated proteins. In contrast, Saccharomyces cerevisiae thiazole synthase (THI4p) uses an active site cysteine as the sulfide source and is inactivated after a single turnover. Here, we demonstrate that the Thi4 ortholog from Methanococcus jannaschii uses exogenous sulfide and is catalytic. Structural and biochemical studies on this enzyme elucidate the mechanistic details of the sulfide transfer reactions. << Less
J. Am. Chem. Soc. 138:3639-3642(2016) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.