<p>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: <reaction> 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde</reaction>While the physiological role of this enzyme remains unknown in eukaryotes, in prokaroytes it is thought to function in the catabolism of deoxyribonucleotides [<cite idref="PUB00000628"/>, <cite idref="PUB00028044"/>].</p><p>In all studied structures, the deoxyribose-phophate aldolase subunits adopt the classical eight-bladed TIM barrel fold [<cite idref="PUB00021873"/>, <cite idref="PUB00016149"/>, <cite idref="PUB00027586"/>]. The oligomerisation state of the enzyme appears to depend on the living temperature of the organism - the <taxon tax_id="562">Escherichia coli</taxon> enzyme (<db_xref db="SWISSPROT" dbkey="P0A6L0"/>) is a homodimer, while the enzymes from the thermophilic microorganisms <taxon tax_id="274">Thermus thermophilus</taxon> and <taxon tax_id="56636">Aeropyrum pernix</taxon> (<db_xref db="SWISSPROT" dbkey="Q9Y948"/>) are homotetramers. The degree of oligomerisation does not, however, appear to affect catalysis.</p><p>This entry represents the type 1 subfamily.</p> Deoxyribose-phosphate aldolase, type 1