Family C59

Family

Summary Holotypes Alignment Tree Genomes Structure Literature

Summary for family C59

Family type peptidaseC59.001 - penicillin V acylase precursor (Lysinibacillus sphaericus), MEROPS Accession MER0020029 (peptidase unit: 4-338)
Content of familyPeptidase family C59 contains Cys-dependent Ntn-hydrolases.
History Identifier created: MEROPS 6.4 (24 September 2003)
Cys-dependent Ntn-hydrolases are only classified as peptidases by virtue of their self-processing activity. The autolysis step produces a mature amidase with Cys1 as the nucleophile. All peptidase activity is lost on conversion to the mature peptidase.
Catalytic typeCysteine
Active site residuesC4 
Active siteThe catalytic Cys becomes the new N-terminus following autolysis (see the Alignment).
Activities and specificitiesThe only known peptidase activity is the autolytic cleavage of the penicillin V acylase precursor protein (C59.001).
Molecular structureThe mature peptidase is a homotetramer and has a fold that is similar to that of the proteasome (XT01-001). There are two anti-parallel beta sheets sandwiched between two pairs of anti-parallel alpha helices. There are extensions from one of the pairs of alpha helices and also at the C-terminus, which interact with other monomers in the tetramer and provide stability (Suresh et al., 1999).
ClanPB
SubclanPB(C)
Distribution of family Bacteria details  
Archaea details  
Protozoa -  
Fungi details  
Plants details  
Animals details  
Viruses details  
Biological functions
Pharmaceutical and biotech relevancePenicillin V acylase has an important industrial role in the production of penicillins.
Statistics for family C59Sequences:2011
Identifiers:2
Identifiers with PDB entries:2
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Peptidases and Homologues MEROPS ID Structure
penicillin V acylase precursorC59.001Yes
choloylglycine hydrolaseC59.951Yes
family C59 non-peptidase homologuesnon-peptidase homologue-
family C59 unassigned peptidasesunassigned-