InterPro : IPR005322

Name  Peptidase C69, dipeptidase A Short Name  Peptidase_C69
Type  Family Description  Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad or triad []. This group of peptidases, belong to MEROPS peptidase family C69 (dipeptidase, clan PB). They are mainly dipeptidases []and incude dipeptidase A from Lactobacillus helveticus. Comparative sequence and structural analysis, particularly to penicillin V acylase (MEROPS peptidase family C59) revealed a cysteine as the catalytic nucleophile as well as other conserved residues important for catalysis []. In general, C69 family is variable in sequence and exhibits great diversity in substrate specificity, to include enzymes such as choloyglycine hydrolases, acid ceramidases, isopenicillin N acyltransferases, and a subgroup of eukaryotic proteins with unclear function.
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3 Publications

First Author Title Year Journal Volume Pages
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33
Vesanto E Molecular characterization, over-expression and purification of a novel dipeptidase from Lactobacillus helveticus. 1996 Appl Microbiol Biotechnol 45 638-45
Pei J Peptidase family U34 belongs to the superfamily of N-terminal nucleophile hydrolases. 2003 Protein Sci 12 1131-5



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)