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Literature summary extracted from

  • Sund, C.J.; Liu, S.; Germane, K.L.; Servinsky, M.D.; Gerlach, E.S.; Hurley, M.M.
    Phosphoketolase flux in Clostridium acetobutylicum during growth on L-arabinose (2015), Microbiology, 161, 430-440 .
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.9 Clostridium acetobutylicum Q97JE3
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.9 D-Fructose 6-phosphate + phosphate the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate Clostridium acetobutylicum Acetyl phosphate + D-erythrose 4-phosphate + H2O
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4.1.2.9 D-Xylulose 5-phosphate + phosphate the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate Clostridium acetobutylicum Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
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Synonyms

EC Number Synonyms Comment Organism
4.1.2.9 xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
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Clostridium acetobutylicum

General Information

EC Number General Information Comment Organism
4.1.2.9 metabolism mutation of the gene encoding phosphoketolase almost completely abolishes flux through the pentose phosphoketolase pathway during growth on arabinose and results in decreased acetate/butyrate ratios Clostridium acetobutylicum
4.1.2.9 metabolism the enzyme is involved in pentose phosphoketolase pathway. This pathway has a primary role in arabinose metabolism of Clostridium acetobutylicum Clostridium acetobutylicum