// Workers AI · dad joke modeWhat did formaldehyde transketolase say? I'm bonded to my work.
| Formaldehyde transketolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.2.1.3 | ||||||||
| CAS no. | 76774-46-4 | ||||||||
| 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 | ||||||||
| |||||||||
Formaldehyde transketolase (EC 2.2.1.3) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are D-xylulose 5-phosphoric acid and formaldehyde. Its products are glyceraldehyde 3-phosphate and dihydroxyacetone. The enzyme was characterised from the yeast Candida boidinii [1][2][3]
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is D-xylulose-5-phosphate:formaldehyde glycolaldehydetransferase. This enzyme is also called dihydroxyacetone synthase. It uses thiamin diphosphate as a cofactor.[4]
References
[edit]- ↑ Bystrykh, L. V.; A. P. Sokolov; Iu. A. Trotsenko (1981). "Separation of transketolase and dihydroxyacetone synthase from methylotrophic yeasts" [Separation of transketolase and dihydroxyacetone synthase from methylotrophic yeasts]. Doklady Akademii Nauk SSSR (in Russian). 258 (2): 499–501. PMID 7249920.
- ↑ Kato N, Higuchi T, Sakazawa C, Nishizawa T, Tani Y, Yamada H (1982). "Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilizing yeast, candida boidinii (Kloeckera sp.) No. 2201". Biochim. Biophys. Acta. 715 (2): 143–50. doi:10.1016/0304-4165(82)90352-x. PMID 7074134.
- ↑ Waites MJ, Quayle JR (1981). "The interrelation transketolase and dihydroxyacetone synthase activities in the methylotrophic yeast Candida boidinii". J. Gen. Microbiol. 124 (2): 309–16. doi:10.1099/00221287-124-2-309. PMID 6276498.
- ↑ Enzyme 2.2.1.3 at KEGG Pathway Database.
