Detail Information for IndEnz0010000790
IED ID IndEnz0010000790
Enzyme Type ID esterase000790
Protein Name Xaa-Pro dipeptidyl-peptidase
EC 3.4.14.11
X-Pro dipeptidyl-peptidase
X-prolyl-dipeptidyl aminopeptidase
X-PDAP
Gene Name pepX
Organism Lactobacillus helveticus (Lactobacillus suntoryeus)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus helveticus (Lactobacillus suntoryeus)
Enzyme Sequence MKYNQYAYVETDFQQQVKELIDINFLPKNYQVWDFSSLLAKLVKNAIAEAKTDAAKNAKLAEFAVSDHQTLADFLKEKPTEIGTKQFYNVALQLLGYHVHYDYDFADPTGFMQRNALPFLQDISDNQKLISAFYRLLNTRAKNGQILLDVMAGKGYFTQFWGQNKFKFFNGKSIPVFDTNKVIREVVYVETDLDTDHDGKSDLIQVTVFRPEETNKGLKVPALYTASPYFGGIIANEKRNHNVDENLSDSTEWNDPQYVHSPIVKAEKPDGSSRPATEEAVHKSSYPLNEYMLARGFASVFAGAIGTRGSDGVRITGAPEETESAAAVIEWLHGDRVAYTDRTRTVQTTADWCNGNIGMTGRSYLGTLQIAIATTGVKGLKTVVSEAAISSWYDYYREHGLVIAPEACQGEDLDLLAETCQSNLWDAGSYLKIKPEYDKMQKQLREKEDRNTGQYSDFWEARNYRHHADGIKCSWISVHGLNDWNVKPKNVYKIWQLVKKMPMKHHLFLHQGPHYNMNNLVSIDFTDLMNLWFVHELLGIENNAYNQWPTVMIQDNLQADKWHEEPDWSNDLGQEKIYYPTDEGELFQDGNGKAQKSFTDVGGIEFKKAGISESDWQYKFICGDEKWAKPSLRFETDEFTHPTTIVGRPEVKVRVSASLPKGEISVALVELGERQRLTATPKFLMHGGQELGYRFGTDTLQEFVPDKKTKAKLITKAHMNLQNFKDMKKPEAIDADKFYDLDFLLQPTYYTIPSGSKLALIIYSTDQGMTKRPLEDETYTIDLANTEIKFYEK
Enzyme Length 793
Uniprot Accession Number Q59485
Absorption
Active Site ACT_SITE 363; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 483; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 514; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
DNA Binding
EC Number 3.4.14.11
Enzyme Function FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (31); Chain (1); Helix (32); Sequence conflict (8); Turn (5)
Keywords 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Protease;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 6NFF;
Mapped Pubmed ID 31584010;
Motif
Gene Encoded By
Mass 90,487
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda