In enzymology, an acetoin-ribose-5-phosphate transaldolase (EC 2.2.1.4) is an enzyme that catalyzes the chemical reaction
acetoin-ribose-5-phosphate transaldolase | |||||||||
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Identifiers | |||||||||
EC no. | 2.2.1.4 | ||||||||
CAS no. | 87843-76-3 | ||||||||
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 / QuickGO | ||||||||
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- 3-hydroxybutan-2-one + D-ribose 5-phosphate acetaldehyde + 1-deoxy-D-altro-heptulose 7-phosphate
Thus, the two substrates of this enzyme are 3-hydroxybutan-2-one and D-ribose 5-phosphate, whereas its two products are acetaldehyde and 1-deoxy-D-altro-heptulose 7-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase. Other names in common use include 1-deoxy-D-altro-heptulose-7-phosphate synthetase, 1-deoxy-D-altro-heptulose-7-phosphate synthase, 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase [wrong, and substrate name]. It employs one cofactor, thiamin diphosphate.
References
edit- Yokota A, Sasajima K (1983). "Enzymatic formation of a new monosaccharide, 1-deoxy-D-altro-heptulose phosphate, from DL-acetoin and D-ribose 5-phosphate by a transketolase mutant of Bacillus pumilus". Agric. Biol. Chem. 47 (7): 1545–1553. doi:10.1271/bbb1961.47.1545.