Class I aldolases catalyse carbon-carbon bond formation using a 'Schiff base' mechanism. This entry represents deoxyribose-phosphate aldolase, a widely distributed enzyme, which catalyses the following reversible reaction: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde While the physiological role of this enzyme remains unknown in eukaryotes, in prokaroytes it is thought to function in the catabolism of deoxyribonucleotides [PMID:1730028, PMID:4923156].

In all studied structures, the deoxyribose-phophate aldolase subunits adopt the classical eight-bladed TIM barrel fold [PMID:15388928, PMID:11598300, PMID:12529358]. The oligomerisation state of the enzyme appears to depend on the living temperature of the organism - the Escherichia coli enzyme (SWISSPROT: P0A6L0) is a homodimer, while the enzymes from the thermophilic microorganisms Thermus thermophilus and Aeropyrum pernix (SWISSPROT: Q9Y948) are homotetramers. The degree of oligomerisation does not, however, appear to affect catalysis.