Phosphoketolase
In enzymology, a phosphoketolase (EC 4.1.2.9) is an enzyme that catalyzes the chemical reaction
- D-xylulose 5-phosphate + phosphate acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
Thus, the two substrates of this enzyme are D-xylulose 5-phosphate and phosphate, whereas its 3 products are acetyl phosphate, D-glyceraldehyde 3-phosphate, and H2O.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (adding phosphate; acetyl-phosphate-forming). Other names in common use include D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase, and (phosphate-acetylating). This enzyme participates in 3 metabolic pathways: pentose phosphate pathway, methane metabolism, and carbon fixation. It employs one cofactor, thiamin diphosphate.
References
- HEATH EC, HURWITZ J, HORECKER BL, GINSBURG A (1958). "Pentose fermentation by Lactobacillus plantarum. I. The cleavage of xylulose 5-phosphate by phosphoketolase". J. Biol. Chem. 231 (2): 1009–29. PMID 13539033.
- Schramm M, Klybas V and Racker E (1958). "Phospholytic cleavage of fructose-6-phosphate by fructose-6-phosphate phosphoketolase from Acetobacter xylinum". J. Biol. Chem. 233: 1283–1288.
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