Phosphoketolase

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Phosphoketolase
Identifiers
EC no. 4.1.2.9
CAS no. 9031-75-8
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MetaCyc metabolic pathway
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The enzyme phosphoketolase(EC 4.1.2.9) 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 because 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]

Related Research Articles

A tetrose is a monosaccharide with 4 carbon atoms. They have either an aldehyde functional group in position 1 (aldotetroses) or a ketone functional group in position 2 (ketotetroses).

<span class="mw-page-title-main">Pentose phosphate pathway</span> Series of interconnected biochemical reactions

The pentose phosphate pathway is a metabolic pathway parallel to glycolysis. It generates NADPH and pentoses as well as ribose 5-phosphate, a precursor for the synthesis of nucleotides. While the pentose phosphate pathway does involve oxidation of glucose, its primary role is anabolic rather than catabolic. The pathway is especially important in red blood cells (erythrocytes). The reactions of the pathway were elucidated in the early 1950s by Bernard Horecker and co-workers.

<span class="mw-page-title-main">Xylulose 5-phosphate</span> Chemical compound

D-Xylulose 5-phosphate (D-xylulose-5-P) is an intermediate in the pentose phosphate pathway. It is a ketose sugar formed from ribulose-5-phosphate by ribulose-5-phosphate epimerase. In the non-oxidative branch of the pentose phosphate pathway, xylulose-5-phosphate acts as a donor of two-carbon ketone groups in transketolase reactions.

<span class="mw-page-title-main">Phosphopentose epimerase</span>

Phosphopentose epimerase encoded by the RPE gene is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.

<span class="mw-page-title-main">Xylose metabolism</span>

D-Xylose is a five-carbon aldose that can be catabolized or metabolized into useful products by a variety of organisms.

<span class="mw-page-title-main">D-xylulose reductase</span>

In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that is classified as an Oxidoreductase (EC 1) specifically acting on the CH-OH group of donors (EC 1.1.1) that uses NAD+ or NADP+ as an acceptor (EC 1.1.1.9). This enzyme participates in pentose and glucuronate interconversions; a set of metabolic pathways that involve converting pentose sugars and glucuronate into other compounds.

<span class="mw-page-title-main">L-ribulose-5-phosphate 4-epimerase</span>

In enzymology, a L-ribulose-5-phosphate 4-epimerase is an enzyme that catalyzes the interconversion of ribulose 5-phosphate and xylulose 5-phosphate in the oxidative phase of the Pentose phosphate pathway.

The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction

The enzyme fructose-6-phosphate phosphoketolase (EC 4.1.2.22) catalyzes the chemical reaction

The enzyme L-fuculose-phosphate aldolase (EC 4.1.2.17) catalyzes the chemical reaction

The enzyme rhamnulose-1-phosphate aldolase (EC 4.1.2.19) catalyzes the chemical reaction

The enzyme 1,5-anhydro-D-fructose dehydratase (EC 4.2.1.111) catalyzes the chemical reaction

The enzyme gluconate dehydratase (EC 4.2.1.39) catalyzes the chemical reaction

The enzyme mannonate dehydratase (EC 4.2.1.8) catalyzes the chemical reaction

The enzyme mannitol-1-phosphatase (EC 3.1.3.22) catalyzes the reaction

<span class="mw-page-title-main">Glucosamine-6-phosphate deaminase</span>

In enzymology, a glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1-deoxy-d-xylulose-5-phosphate synthase (EC 2.2.1.7) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction

<span class="mw-page-title-main">N-acetylneuraminate synthase</span>

In enzymology, a N-acetylneuraminate synthase (EC 2.5.1.56) is an enzyme that catalyzes the chemical reaction

In enzymology, a rhamnulokinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Ribulokinase</span>

In enzymology, a ribulokinase is an enzyme that catalyzes the chemical reaction

References

  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. PMC   4352667 . PMID   25605308.
  2. ↑ Racker, E. (1962), [29d] Fructose-6-phosphate phosphoketolase from Acetobacter xylinum, Methods in Enzymology, vol. 5, Elsevier, pp. 276–280, doi:10.1016/s0076-6879(62)05219-2, ISBN   9780121818050
  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. PMID   30347514.
  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. PMC   404438 . PMID   15128548.
  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): 167. doi: 10.1186/s12934-015-0355-9 . ISSN   1475-2859. PMC   4609045 . PMID   26474754.
  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. PMID   27654918.
  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. PMID   24077099.


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