Family

Deoxyribose-phosphate aldolase (IPR011343)

Short name: DeoC

Overlapping homologous superfamilies

Family relationships

Description

Aldolases play important roles in essential metabolic pathways, such as gluconeogenesis and glycolysis. They are classified with respect to their catalytic mechanism into two classes: class I adolases are are characterised by formation of covalent Schiff base intermediates, while class II aldolases are metallodependent enzymes and use a divalent transition metal ion to polarize the substrate ketose [PMID: 16843441, PMID: 13950007, PMID: 5972827, PMID: 5793710, PMID: 5816380].

Deoxyribose-phosphate aldolase (DERA) belongs to the class I aldolases. It is 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 (P0A6L0) is a homodimer, while the enzymes from the thermophilic microorganisms Thermus thermophilus and Aeropyrum pernix (Q9Y948) are homotetramers. The degree of oligomerisation does not, however, appear to affect catalysis.

Deoxyribose-phophate aldolase is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction [PMID: 12467706, PMID: 12529358].

GO terms

Biological Process

GO:0009264 deoxyribonucleotide catabolic process

Molecular Function

GO:0004139 deoxyribose-phosphate aldolase activity

Cellular Component

GO:0005737 cytoplasm

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
CDD
PIRSF
PANTHER
TIGRFAMs