Detail Information for IndEnz0002001309
IED ID IndEnz0002001309
Enzyme Type ID protease001309
Protein Name Xaa-Pro dipeptidyl-peptidase
EC 3.4.14.11
X-Pro dipeptidyl-peptidase
X-prolyl-dipeptidyl aminopeptidase
X-PDAP
Gene Name pepX Ldb1455
Organism Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus delbrueckii Lactobacillus delbrueckii subsp. bulgaricus Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14)
Enzyme Sequence MKYNQYAYVETSPEKATEELLAINFLPENYSSLSFSELLAVLTGNVLAEATTRQAKDAKLAEFAVDDQTDLAAFLLDTPTAITASQFANVALQLLGYHPNYDYSLTDPLTCGEKHALPAFKDLTSKEELIFAFYRLLNTRSKNGQILLDVMAGKGYFTQFWGEGKFMLFNGKSLPVFDTSQVIREVVYVQSDLDTDGDGKGDLLPVTVFRPVESQDQLKVPALYTASPYFGGIIDNVKTNHNVDENLTDATTWTNPKYVAKPLVKSPAPSGQDVPATELATGQSSYGLNEYLLARGFASVFSGAIGNRHGDGIRITGSPEETISQKEVIEWLTGDRVAYTDRTRRFETKAGWCSGNVGMTGRSYLGTLQIAIATTGVKGLKTVVSEAAISSWYDYYREHGLVIAPSECQGEDMDKLAEVCQSNLWDGGNFTAKKAYEAEQAELLAAQDRATGQYSDFWESRNYRHHADGIKCSWISVHGLNDWNVKPKNVYKIWQKVKQLPVESHLFLHQGPHYNMNNLVSIDFTDLMNLWFVHELLEVENGAYEQWPKVMIQDNLEADKWHAESDWANDLGQASLYSPTADGYLSTVENGTGQLTFTDLGGTEFKKAGISETDWEYQFISGEKKWAKASLRFESEEFLHPTTLVGRPKVQVRVAANKTVGQLSVALVDLGTRQRLTATPKIFARGNQPFGYRFEADSLQEFVPDKATKAKLITKAHMNLQNYQDMKQPSKLEAGQFVDLEFELQPTYYTLPAGAKLCLIIYSTDQGMTKRPLETEDYTVDLAGTALLLYRK
Enzyme Length 792
Uniprot Accession Number Q1G9E8
Absorption
Active Site ACT_SITE 363; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 482; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 513; /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. {ECO:0000255|HAMAP-Rule:MF_00698}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Protease;Reference proteome;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
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 88,410
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda