Succinyl-diaminopimelate desuccinylase, proteobacteria (IPR005941)

Short name: DapE_proteobac

Overlapping homologous superfamilies

Family relationships

  • Peptidase M20 (IPR002933)
    • Succinyl-diaminopimelate desuccinylase, proteobacteria (IPR005941)


This entry represents succinyl-diaminopimelate desuccinylase from proteobacteria (DapE, EC:, which hydrolyses N-succinyl-L,L-diaminopimelic acid to L,L-diaminopimelic acid (L,L-DAP) [PMID: 3276674]. L,L-DAP is required for the bacterial synthesis of lysine and meso-diaminopimelic acid.

This group of bacterial sequences belong to the MEROPS peptidase family M20 (clan MH), subfamily M20A (DapE peptidase); they are not strictly peptidases as they are aminohydrolases.

It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE [PMID: 7674922, PMID: 20138056, PMID: 14640610, PMID: 16421726, PMID: 9671518, PMID: 18712420, PMID: 19822427].

GO terms

Biological Process

GO:0009089 lysine biosynthetic process via diaminopimelate

Molecular Function

GO:0009014 succinyl-diaminopimelate desuccinylase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.