Phosphoketolase

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Phosphoketolase
Identifiers
EC number4.1.2.9
CAS number9031-75-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, phosphoketolase is an enzyme that catalyzes the chemical reactions

D-xylulose 5-phosphate + phosphate acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O (EC 4.1.2.9) [1]
D-fructose 6-phosphate + phosphate acetyl phosphate + D-erythrose 4-phosphate + H2O (EC 4.1.2.22)[2]
D-sedoheptulose 7-phosphate + phosphate acetyl phosphate + D-ribose 5-phosphate + H2O[3]

Phosphoketolase is considered a promiscuous enzyme as it was demonstrated to use 3 different sugar phosphates as substrates. In a recent genetic study, more than 150 putative phosphoketolase genes exhibiting varying catalytic properties were found in 650 analyzed bacterial genomes.[4]

This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. It participates in 3 metabolic pathways: pentose phosphate pathway, methane metabolism, and carbon fixation. It employs one cofactor, thiamin diphosphate. Phosphoketolase was previously used for biotechnological purposes[5][6][7] as it enables the construction of synthetic pathways that allow complete carbon conservation without the generation of reducing power.[8]

References[edit]

  1. ^ Glenn, Katie; Smith, Kerry S. (2015-01-20). "Allosteric Regulation of Lactobacillus plantarum Xylulose 5-Phosphate/Fructose 6-Phosphate Phosphoketolase (Xfp)". Journal of Bacteriology. 197 (7): 1157–1163. doi:10.1128/jb.02380-14. ISSN 0021-9193.
  2. ^ Racker, E. (1962), "[29d] Fructose-6-phosphate phosphoketolase from Acetobacter xylinum", Methods in Enzymology, Elsevier, pp. 276–280, ISBN 9780121818050, retrieved 2019-04-10
  3. ^ Krüsemann, Jan L.; Lindner, Steffen N.; Dempfle, Marian; Widmer, Julian; Arrivault, Stephanie; Debacker, Marine; He, Hai; Kubis, Armin; Chayot, Romain (2018). "Artificial pathway emergence in central metabolism from three recursive phosphoketolase reactions". The FEBS Journal. 285 (23): 4367–4377. doi:10.1111/febs.14682. ISSN 1742-4658.
  4. ^ Sánchez, Borja; Zúñiga, Manuel; González-Candelas, Fernando; de los Reyes-Gavilán, Clara G.; Margolles, Abelardo (2010). "Bacterial and Eukaryotic Phosphoketolases: Phylogeny, Distribution and Evolution". Journal of Molecular Microbiology and Biotechnology. 18 (1): 37–51. doi:10.1159/000274310. ISSN 1464-1801.
  5. ^ Sonderegger, M.; Schumperli, M.; Sauer, U. (2004-05-01). "Metabolic Engineering of a Phosphoketolase Pathway for Pentose Catabolism in Saccharomyces cerevisiae". Applied and Environmental Microbiology. 70 (5): 2892–2897. doi:10.1128/aem.70.5.2892-2897.2004. ISSN 0099-2240.
  6. ^ Anfelt, Josefine; Kaczmarzyk, Danuta; Shabestary, Kiyan; Renberg, Björn; Rockberg, Johan; Nielsen, Jens; Uhlén, Mathias; Hudson, Elton P. (2015-10-16). "Genetic and nutrient modulation of acetyl-CoA levels in Synechocystis for n-butanol production". Microbial Cell Factories. 14 (1). doi:10.1186/s12934-015-0355-9. ISSN 1475-2859.
  7. ^ Meadows, Adam L.; Hawkins, Kristy M.; Tsegaye, Yoseph; Antipov, Eugene; Kim, Youngnyun; Raetz, Lauren; Dahl, Robert H.; Tai, Anna; Mahatdejkul-Meadows, Tina (September 2016). "Rewriting yeast central carbon metabolism for industrial isoprenoid production". Nature. 537 (7622): 694–697. doi:10.1038/nature19769. ISSN 0028-0836.
  8. ^ Bogorad, Igor W.; Lin, Tzu-Shyang; Liao, James C. (2013-09-29). "Synthetic non-oxidative glycolysis enables complete carbon conservation". Nature. 502 (7473): 693–697. doi:10.1038/nature12575. ISSN 0028-0836.
  • 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, Racker E (1958). "Phospholytic cleavage of fructose-6-phosphate by fructose-6-phosphate phosphoketolase from Acetobacter xylinum". J. Biol. Chem. 233: 1283–1288.