Deoxyribose-phosphate aldolase

Deoxyribose-phosphate aldolase
deoxyribose-phosphate aldolase
Identifiers
EC number 4.1.2.4
CAS number 9026-97-5
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

In enzymology, a deoxyribose-phosphate aldolase (EC 4.1.2.4) is an enzyme that catalyzes the chemical reaction

2-deoxy-D-ribose 5-phosphate \rightleftharpoons D-glyceraldehyde 3-phosphate + acetaldehyde

Hence, this enzyme has one substrate, 2-deoxy-D-ribose 5-phosphate, and two products, D-glyceraldehyde 3-phosphate and acetaldehyde.

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 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase (D-glyceraldehyde-3-phosphate-forming). Other names in common use include phosphodeoxyriboaldolase, deoxyriboaldolase, deoxyribose-5-phosphate aldolase, 2-deoxyribose-5-phosphate aldolase, and 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase. This enzyme participates in pentose phosphate pathway.

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1JCJ, 1JCL, 1KTN, 1MZH, 1N7K, 1O0Y, 1P1X, 1UB3, 1VCV, and 2A4A.

References

  • Hoffee PA (1968). "2-deoxyribose-5-phosphate aldolase of Salmonella typhimurium: purification and properties". Arch. Biochem. Biophys. 126 (3): 795–802. doi:10.1016/0003-9861(68)90473-6. PMID 4879701. 
  • Jedziniak JA, Lionetti FJ (1970). "Purification and properties of deoxyriboaldolase from human erythrocytes". Biochim. Biophys. Acta. 212 (3): 478–87. PMID 4989681. 
  • RACKER E (1952). "Enzymatic synthesis and breakdown of desoxyribose phosphate". J. Biol. Chem. 196 (1): 347–65. PMID 12980976. 
  • Hoffee P Rosen OM and Horecker BL (1965). "The mechanism of action of aldolases. VI. Crystallization of deoxyribose 5-phosphate aldolase and the number of active sites". J. Biol. Chem. 240: 1512–1516. 
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