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Phosphoketolase

From Wikipedia, the free encyclopedia

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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]

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