IED ID | IndEnz0002011833 |
Enzyme Type ID | protease011833 |
Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
Gene Name | pip pepI |
Organism | Lactobacillus delbrueckii subsp. lactis |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus delbrueckii Lactobacillus delbrueckii subsp. lactis |
Enzyme Sequence | MQITEKYLPFGNWQTYCRIVGEATDRAPLLLLHGGPGSSHNYFEVLDQVAEKSGRQVIMYDQLGCGNSSIPDDQAETAYTAQTWVKELENVREQLGLDQIHLLGQSWGGMLALIYLCDYQPKGVKSLILSSTLASAKLWSQELHRLIKYLPKGEQAAIKEAETTGNYDSPAYQAANAHFMDQHAINVTPDLPEPVLRKKKGGNLAYLTGWGPNEYTPIGNLHGYEYTDRLKDLDLPALITSGTDDLCTPLVAKSMYDHLPNARWELFAGCGHMPFVQENAKYQELLSDWLISQD |
Enzyme Length | 294 |
Uniprot Accession Number | P46542 |
Absorption | |
Active Site | ACT_SITE 106; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 245; /evidence=ECO:0000250; ACT_SITE 272; /note=Proton donor; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by 3,4-DCI, but no significant effect on enzyme activity by pepstatin A, E-64, 1,10-phenanthroline or EDTA. {ECO:0000269|PubMed:8025678}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000269|PubMed:8025678}; |
DNA Binding | |
EC Number | 3.4.11.5 |
Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates. Cleaves Pro-betaNA (L-prolyl-beta-naphthylamide) effectively. {ECO:0000269|PubMed:8025678}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Domain (1) |
Keywords | Aminopeptidase;Hydrolase;Protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell envelope {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 32,879 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |