Thiamine-phosphate diphosphorylase
| thiamin-phosphate diphosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.3 | ||||||||
| CAS no. | 9030-30-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a thiamine-phosphate diphosphorylase ( or, thiamine-phosphate pyrophosphorylase ) (EC 2.5.1.3) is an enzyme that catalyzes the chemical reaction
- 4-Amino-5-hydroxymethyl-2-methylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole diphosphate + thiamine monophosphate
The two substrates of this enzyme are 4-Amino-5-hydroxymethyl-2-methylpyrimidine diphosphate and 4-methyl-5-(2-phosphono-oxyethyl)thiazole; its two products are diphosphate and thiamine monophosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. This enzyme is on the biosynthetic pathway to thiamine.[1][2]
Nomenclature
The systematic name of this enzyme class is 2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2 -phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase. Other names in common use include
- thiamine phosphate synthase,
- thiamine phosphate pyrophosphorylase,
- thiamine monophosphate pyrophosphorylase, and
- TMP-PPase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1G4E, PDB: 1G4P, PDB: 1G4S, PDB: 1G4T, PDB: 1G67, PDB: 1G69, PDB: 1G6C, PDB: 1XI3, and PDB: 2TPS.
There are two main structural/evolutional families of proteins that exhibit this activity, both singular protein domains. ThiE (InterPro: IPR034291) is found in most bacteria, some protozoans, plants, and fungi. ThiN (InterPro: IPR019293) is found in archaea and some thermophilic bacteria.[3] The latter also has noncatalytic versions that acts as a thiamine sensor.[4]
References
- ↑ Caspi R (2011-09-14). "Pathway: superpathway of thiamine diphosphate biosynthesis I". MetaCyc Metabolic Pathway Database. Retrieved 2022-02-01.
- ↑ Ajjawi I, Tsegaye Y, Shintani D (March 2007). "Determination of the genetic, molecular, and biochemical basis of the Arabidopsis thaliana thiamin auxotroph th1". Archives of Biochemistry and Biophysics. 459 (1): 107–114. Bibcode:2007ArBB..459..107A. doi:10.1016/j.abb.2006.11.011. PMID 17174261.
- ↑ Hayashi, Maria; Kobayashi, Kazuya; Esaki, Hiroyoshi; Konno, Hiroyuki; Akaji, Kenichi; Tazuya, Keiko; Yamada, Kazuko; Nakabayashi, Toshikatsu; Nosaka, Kazuto (April 2014). "Enzymatic and structural characterization of an archaeal thiamin phosphate synthase". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844 (4): 803–809. doi:10.1016/j.bbapap.2014.02.017. PMID 24583237.
- ↑ Hwang, S; Cordova, B; Abdo, M; Pfeiffer, F; Maupin-Furlow, JA (1 April 2017). "ThiN as a Versatile Domain of Transcriptional Repressors and Catalytic Enzymes of Thiamine Biosynthesis". Journal of Bacteriology. 199 (7). doi:10.1128/JB.00810-16. PMC 5350279. PMID 28115546.
Further reading
- Camiener GW, Brown GM (August 1960). "The biosynthesis of thiamine. 2. Fractionation of enzyme system and identification of thiazole monophosphate and thiamine monophosphate as intermediates". The Journal of Biological Chemistry. 235: 2411–2417. doi:10.1016/S0021-9258(18)64636-8. PMID 13807175.
- Leder IG (November 1961). "The enzymatic synthesis of thiamine monophosphate". The Journal of Biological Chemistry. 236 (11): 3066–3071. doi:10.1016/S0021-9258(19)76430-8. PMID 14463407.