| IED ID | IndEnz0002007360 |
| Enzyme Type ID | protease007360 |
| Protein Name |
Beta-Ala-Xaa dipeptidase EC 3.4.13.- Beta-Ala-His dipeptidase Peptidase V |
| Gene Name | pepV |
| 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 | MDLNFKELAEAKKDAILKDLEELIAIDSSEDLENATEEYPVGKGPVDAMTKFLSFAKRDGFDTENFANYAGRVNFGAGDKRLGIIGHMDVVPAGEGWTRDPFKMEIDEEGRIYGRGSADDKGPSLTAYYGMLLLKEAGFKPKKKIDFVLGTNEETNWVGIDYYLKHEPTPDIVFSPDAEYPIINGEQGIFTLEFSFKNDDTKGDYVLDKFKAGIATNVTPQVTRATISGPDLEAVKLAYESFLADKELDGSFEINDESADIVLIGQGAHASAPQVGKNSATFLALFLDQYAFAGRDKNFLHFLAEVEHEDFYGKKLGIFHHDDLMGDLASSPSMFDYEHAGKASLLNNVRYPQGTDPDTMIKQVLDKFSGILDVTYNGFEEPHYVPGSDPMVQTLLKVYEKQTGKPGHEVVIGGGTYGRLFERGVAFGAQPENGPMVMHAANEFMMLDDLILSIAIYAEAIYELTKDEEL |
| Enzyme Length | 470 |
| Uniprot Accession Number | P45494 |
| Absorption | |
| Active Site | ACT_SITE 89; /evidence=ECO:0000250; ACT_SITE 153; /note=Proton acceptor; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Fully inhibited by 1,10-phenanthroline or EDTA. {ECO:0000269|PubMed:7528082}. |
| Binding Site | BINDING 350; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.13.- |
| Enzyme Function | FUNCTION: Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides. {ECO:0000269|PubMed:7528082}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (18); Binding site (1); Chain (1); Helix (14); Metal binding (6); Turn (6) |
| Keywords | 3D-structure;Cytoplasm;Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7528082}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1LFW; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,990 |
| Kinetics | |
| Metal Binding | METAL 87; /note=Zinc 2; /evidence=ECO:0000269|PubMed:12176387; METAL 119; /note=Zinc 1; /evidence=ECO:0000269|PubMed:12176387; METAL 119; /note=Zinc 2; /evidence=ECO:0000269|PubMed:12176387; METAL 154; /note=Zinc 1; /evidence=ECO:0000269|PubMed:12176387; METAL 177; /note=Zinc 2; /evidence=ECO:0000269|PubMed:12176387; METAL 439; /note=Zinc 1; /evidence=ECO:0000269|PubMed:12176387 |
| Rhea ID | |
| Cross Reference Brenda |