Summary for peptidase M24.003: Xaa-Pro dipeptidase (bacteria-type)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Inhibitors Pharma

 

Names
MEROPS NameXaa-Pro dipeptidase (bacteria-type)
Other namesimidodipeptidase, gamma peptidase, pepQ (Escherichia coli), prolidase, proline dipeptidase, prolytase, X-Pro dipeptidase
Domain architecture
MEROPS Classification
Classification Clan MG >> Subclan (none) >> Family M24 >> Subfamily B >> M24.003
HolotypeXaa-Pro dipeptidase (bacteria-type) (Escherichia coli), Uniprot accession P21165 (peptidase unit: 157-443), MERNUM MER0001250
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00238
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.13 (Dipeptidases) >> Peptidase 3.4.13.9
EnzymologyBRENDA database
PhysiologyDegrades proline-containing peptides, e.g. from collagen.
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/-Scissile bondP/-/-/- (based on 13 cleavages)
weblogo
Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 0 0 1 0 0 0 0
Pro 0 0 0 1 13 0 0 0
Ala 0 0 0 1 0 0 0 0
Val 0 0 0 1 0 0 0 0
Leu 0 0 0 1 0 0 0 0
Ile 0 0 0 1 0 0 0 0
Met 0 0 0 1 0 0 0 0
Phe 0 0 0 1 0 0 0 0
Tyr 0 0 0 1 0 0 0 0
Trp 0 0 0 0 0 0 0 0
Ser 0 0 0 1 0 0 0 0
Thr 0 0 0 0 0 0 0 0
Cys 0 0 0 0 0 0 0 0
Asn 0 0 0 0 0 0 0 0
Gln 0 0 0 0 0 0 0 0
Asp 0 0 0 0 0 0 0 0
Glu 0 0 0 0 0 0 0 0
Lys 0 0 0 1 0 0 0 0
Arg 0 0 0 1 0 0 0 0
His 0 0 0 1 0 0 0 0