Enzymes
| UniProtKB help_outline | 15,406 proteins |
Reaction participants Show >> << Hide
- Name help_outline Fe3+ Identifier CHEBI:29034 (CAS: 20074-52-6) help_outline Charge 3 Formula Fe InChIKeyhelp_outline VTLYFUHAOXGGBS-UHFFFAOYSA-N SMILEShelp_outline [Fe+3] 2D coordinates Mol file for the small molecule Search links Involved in 248 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
L-histidyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
Identifier
RHEA-COMP:16894
Reactive part
help_outline
- Name help_outline L-histidine residue Identifier CHEBI:29979 Charge 0 Formula C6H7N3O SMILEShelp_outline C(*)(=O)[C@@H](N*)CC=1N=CNC1 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
N6-(pyridoxal phosphate)-L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
Identifier
RHEA-COMP:16892
Reactive part
help_outline
- Name help_outline N6-(pyridoxal phosphate)-L-lysine residue Identifier CHEBI:143915 Charge -2 Formula C14H18N3O6P SMILEShelp_outline N=1C=C(C(=C(C1C)O)/C=N/CCCC[C@H](N*)C(=O)*)COP([O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
(2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
Identifier
RHEA-COMP:16895
Reactive part
help_outline
- Name help_outline (2S)-2-amino-5-hydroxy-4-oxopentanoate residue Identifier CHEBI:157692 Charge 0 Formula C5H7NO3 SMILEShelp_outline OCC(C[C@@H](C(*)=O)N*)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-oxopropanoate Identifier CHEBI:33190 Charge -1 Formula C3H3O3 InChIKeyhelp_outline OAKURXIZZOAYBC-UHFFFAOYSA-M SMILEShelp_outline [H]C(=O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 20 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine Identifier CHEBI:58354 Charge -2 Formula C6H8N3O4P InChIKeyhelp_outline PKYFHKIYHBRTPI-UHFFFAOYSA-L SMILEShelp_outline Cc1ncc(COP([O-])([O-])=O)c(N)n1 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline Fe2+ Identifier CHEBI:29033 (CAS: 15438-31-0) help_outline Charge 2 Formula Fe InChIKeyhelp_outline CWYNVVGOOAEACU-UHFFFAOYSA-N SMILEShelp_outline [Fe++] 2D coordinates Mol file for the small molecule Search links Involved in 263 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
Identifier
RHEA-COMP:16893
Reactive part
help_outline
- Name help_outline L-lysine residue Identifier CHEBI:29969 Charge 1 Formula C6H13N2O SMILEShelp_outline C([C@@H](C(*)=O)N*)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 136 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:65756 | RHEA:65757 | RHEA:65758 | RHEA:65759 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
The last piece in the vitamin B1 biosynthesis puzzle: structural and functional insight into yeast 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase.
Coquille S., Roux C., Fitzpatrick T.B., Thore S.
Vitamin B(1) is essential for all organisms being well recognized as a necessary cofactor for key metabolic pathways such as glycolysis, and was more recently implicated in DNA damage responses. Little is known about the enzyme responsible for the formation of the pyrimidine moiety (4-amino-5-hydr ... >> More
Vitamin B(1) is essential for all organisms being well recognized as a necessary cofactor for key metabolic pathways such as glycolysis, and was more recently implicated in DNA damage responses. Little is known about the enzyme responsible for the formation of the pyrimidine moiety (4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase). We report a structure-function study of the HMP-P synthase from yeast, THI5p. Our crystallographic structure shows that THI5p is a mix between periplasmic binding proteins and pyridoxal 5'-phosphate-dependent enzymes. Mutational and yeast complementation studies identify the key residues for HMP-P biosynthesis as well as the use of pyridoxal 5'-phosphate as a substrate rather than as a cofactor. Furthermore, we could show that iron binding to HMP-P synthase is essential for the reaction. << Less
-
Thiamin pyrimidine biosynthesis in Candida albicans: a remarkable reaction between histidine and pyridoxal phosphate.
Lai R.Y., Huang S., Fenwick M.K., Hazra A., Zhang Y., Rajashankar K., Philmus B., Kinsland C., Sanders J.M., Ealick S.E., Begley T.P.
In Saccharomyces cerevisiae , thiamin pyrimidine is formed from histidine and pyridoxal phosphate (PLP). The origin of all of the pyrimidine atoms has been previously determined using labeling studies and suggests that the pyrimidine is formed using remarkable chemistry that is without chemical or ... >> More
In Saccharomyces cerevisiae , thiamin pyrimidine is formed from histidine and pyridoxal phosphate (PLP). The origin of all of the pyrimidine atoms has been previously determined using labeling studies and suggests that the pyrimidine is formed using remarkable chemistry that is without chemical or biochemical precedent. Here we report the overexpression of the closely related Candida albicans pyrimidine synthase (THI5p) and the reconstitution and preliminary characterization of the enzymatic activity. A structure of the C. albicans THI5p shows PLP bound at the active site via an imine with Lys62 and His66 in close proximity to the PLP. Our data suggest that His66 of the THI5 protein is the histidine source for pyrimidine formation and that the pyrimidine synthase is a single-turnover enzyme. << Less
Comments
The histidine residue being consumed during this reaction is an integral part of the enzyme itself. The enzyme is thus a single turn-over (or suicide) enzyme.