| IED ID | IndEnz0002010761 |
| Enzyme Type ID | protease010761 |
| Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | pip |
| Organism | Weizmannia coagulans (Bacillus coagulans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Weizmannia Weizmannia coagulans (Bacillus coagulans) |
| Enzyme Sequence | MYTEGFIDVTGGRVSFQKFDENGGGTPVIVLHGGPGSSCYSLLGLKALAKDRPVILYDQLGCGKSDRPMDTTLWRLDRFVEELAQIRQALNLDEVHILGHSWGTTLAAAYCLTKPSGVKSVIFSSPCLSAPLWEQDQKRNLKKLPLDVQETINRCEENGTTDSEEFAAAIEVFGKHFVNRLEKQPEWLEQKPSGYRNADIYNIMWGPSEFTVLGNLKNFDCTTQLKEITCPSLYTCGRFDEATPETTEYYSSLTPKSKFHVFEKSAHMPYIEEPEEYLAVIGDFLNSI |
| Enzyme Length | 288 |
| Uniprot Accession Number | P46541 |
| Absorption | |
| Active Site | ACT_SITE 101; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 240; /evidence=ECO:0000250; ACT_SITE 267; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by p-chloromercuribenzoate (PCMB) and heavy metal salts. Partially inhibited by proline and proline derivatives with proline as the amino terminus. Enzyme inactivated by PCMB is reactivated by incubation with 2-mercaptoethanol. {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}. |
| 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:1459939, ECO:0000269|PubMed:4030733, ECO:0000269|PubMed:7896753}; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates including at least dipeptides Pro-Pro, Pro-Gln, Pro-Trp and Pro-Tyr. Acts also on amides (Pro-beta NA) and oligopeptides including Pro-Leu-GlyNH2, Pro-Leu-Gly, Pro-Phe-Gly-Lys, Pro-Pro-Ala-OBut and Pro-Pro-Gly-(Pro-Pro-Gly)(4). Higher activity toward small peptides (up to three residues), but very low activity for longer peptides. Has no activity against p-nitrophenyl acetate, poly_L-proline, Met-Pro or amino acyl amides other than Pro-betaNA (Pyr-betaNA, Phe-betaNA, Cys-betaNA, Met-betaNA, Leu-betaNA, Ala-betaNA and Z-Gly-Pro-betaNA). {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Maximum activity at 40 degrees Celsius. Stable at temperatures up to 38 degrees Celsius. {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Stable at pH 5.5-7.5. Most active at 7.3 with Pro-beta-naphthylamide (Pro-2-NNap) as the substrate. More than 85% of the activity remains between pH 6.5 and 7.5 after incubation for 15 minutes at 30 degrees Celsius and it retains 50% of the original activity after incubation at pH 7.0 and at 30 degrees Celsius for 30 minutes. 50% of the activity remains after 15 minutes preincubations at pH 8.0. {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Mutagenesis (2) |
| Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,357 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.08 mM for Pro-Ala {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=1.16 mM for Pro-Asp {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=1.06 mM for Pro-Gly {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=0.91 mM for Pro-Lys {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=7.70 mM for Pro-Leu {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=1.50 mM for Pro-Phe {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=1.27 mM for Pro-Trp {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=0.95 mM for Pro-Tyr {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=0.26 mM for Pro-2-NNap {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=0.26 mM for Pro-pNA {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=27.0 mM for Pro-D-Ala {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=2.51 mM for Pro-D-Phe {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; KM=6.35 mM for Pro-Leu-Gly-NH(2) {ECO:0000269|PubMed:1459939, ECO:0000269|PubMed:4030733}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |