Literature summary for 4.1.2.9 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 .

Search for more literature for 4.1.2.9

Organism

Organism	UniProt	Comment	Textmining
Clostridium acetobutylicum	Q97JE3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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	-	?

Synonyms

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

General Information

General Information	Comment	Organism
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
metabolism	the enzyme is involved in pentose phosphoketolase pathway. This pathway has a primary role in arabinose metabolism of Clostridium acetobutylicum	Clostridium acetobutylicum

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Release 2023.1 (January 2023)