Family

Deoxyribose-phosphate aldolase (IPR011343)

Short name: DeoC

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.
TIGRFAMs
PANTHER
CDD
PIRSF