phosphoketolase | |||||||||
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Identifiers | |||||||||
EC number | 4.1.2.9 | ||||||||
CAS number | 9031-75-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
In enzymology, a phosphoketolase (EC 4.1.2.9) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are D-xylulose 5-phosphate and phosphate, whereas its 3 products are acetyl phosphate, D-glyceraldehyde 3-phosphate, and H2O.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (adding phosphate; acetyl-phosphate-forming). Other names in common use include D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase, and (phosphate-acetylating). This enzyme participates in 3 metabolic pathways: pentose phosphate pathway, methane metabolism, and carbon fixation. It employs one cofactor, thiamin diphosphate.