InterPro : IPR011356

Name  Leucine aminopeptidase/peptidase B Short Name  Leucine_aapep/pepB
Type  Family Description  The majority of members of this family are zinc-dependent exopeptidases belonging to MEROPS peptidase family M17 (leucyl aminopeptidase, clan MF).Leucyl aminopeptidase (LAP; ) selectively release N-terminal amino acid residues from polypeptides and proteins; in general they are involved in the processing, catabolism and degradation of intracellular proteins [, , ]. Leucyl aminopeptidase forms a homohexamer containing two trimers stacked on top of one another []. Each monomer binds two zinc ions. The zinc-binding and catalytic sites are located within the C-terminal catalytic domain []. Leucine aminopeptidase has been shown to be identical with prolyl aminopeptidase () in mammals []. Interestingly, members of this group are also implicated in transcriptional regulation and are thought to combine catalytic and regulatory properties []. The N-terminal domain of these proteins has been shown in Escherichia coliPepA to function as a DNA-binding protein in Xer site-specific recombination and in transcriptional control of the carAB operon [, ]. It is not well conserved and in some members can be found only by PSI-BLAST (after 4-6 iterations). It is not clear if the DNA binding function is preserved in all or even in most of the members.For additional information please see [, , , ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR008330 Peptidase M17, peptidase B Pept_M17_PepB Family
IPR023042 Peptidase M17, leucine aminopeptidase Peptidase_M17_leu_NH2_pept Family

2 Contains

Id Name Short Name Type
IPR000819 Peptidase M17, leucyl aminopeptidase, C-terminal Peptidase_M17_C Domain
IPR008283 Peptidase M17, leucyl aminopeptidase, N-terminal Peptidase_M17_N Domain

0 Found In

0 Parent Features

10 Publications

First Author Title Year Journal Volume Pages
Rawlings ND Evolutionary families of metallopeptidases. 1995 Methods Enzymol 248 183-228
Rawlings ND Evolutionary families of peptidases. 1993 Biochem J 290 ( Pt 1) 205-18
Bartling D Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants. 1992 Eur J Biochem 205 425-31
Burley SK Molecular structure of leucine aminopeptidase at 2.7-A resolution. 1990 Proc Natl Acad Sci U S A 87 6878-82
Gonzales T Bacterial aminopeptidases: properties and functions. 1996 FEMS Microbiol Rev 18 319-44
Sträter N X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination. 1999 EMBO J 18 4513-22
Charlier D Mutational analysis of Escherichia coli PepA, a multifunctional DNA-binding aminopeptidase. 2000 J Mol Biol 302 411-26
Kim H Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography. 1993 Proc Natl Acad Sci U S A 90 5006-10
Matsushima M Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase. 1991 Biochem Biophys Res Commun 178 1459-64
Stirling CJ xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. 1989 EMBO J 8 1623-7

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)