| IED ID | IndEnz0002000194 |
| Enzyme Type ID | protease000194 |
| Protein Name |
Cytosol non-specific dipeptidase EC 3.4.13.18 Aminoacyl-histidine dipeptidase Beta-alanyl-histidine dipeptidase Carnosinase Cysteinylglycinase Peptidase D Xaa-His dipeptidase X-His dipeptidase |
| Gene Name | pepD pepH b0237 JW0227 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSELSQLSPQPLWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVGNILIRKPATAGMENRKPVVLQAHLDMVPQKNNDTVHDFTKDPIQPYIDGEWVKARGTTLGADNGIGMASALAVLADENVVHGPLEVLLTMTEEAGMDGAFGLQGNWLQADILINTDSEEEGEIYMGCAGGIDFTSNLHLDREAVPAGFETFKLTLKGLKGGHSGGEIHVGLGNANKLLVRFLAGHAEELDLRLIDFNGGTLRNAIPREAFATIAVAADKVDVLKSLVNTYQEILKNELAEKEKNLALLLDSVANDKAALIAKSRDTFIRLLNATPNGVIRNSDVAKGVVETSLNVGVVTMTDNNVEIHCLIRSLIDSGKDYVVSMLDSLGKLAGAKTEAKGAYPGWQPDANSPVMHLVRETYQRLFNKTPNIQIIHAGLECGLFKKPYPEMDMVSIGPTITGPHSPDEQVHIESVGHYWTLLTELLKEIPAK |
| Enzyme Length | 485 |
| Uniprot Accession Number | P15288 |
| Absorption | |
| Active Site | ACT_SITE 78; /evidence=ECO:0000250; ACT_SITE 145; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by metal chelators. {ECO:0000269|PubMed:7988883}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.; EC=3.4.13.18; Evidence={ECO:0000269|PubMed:355237, ECO:0000269|PubMed:7988883}; |
| DNA Binding | |
| EC Number | 3.4.13.18 |
| Enzyme Function | FUNCTION: Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source. {ECO:0000269|PubMed:11157967, ECO:0000269|PubMed:20067529, ECO:0000269|PubMed:355237, ECO:0000269|PubMed:7988883}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:7988883}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:7988883}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Initiator methionine (1); Metal binding (6); Modified residue (1) |
| Keywords | Acetylation;Cobalt;Dipeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | P60560; P15034 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 296; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15690043; 16606699; 16858726; 1938933; 21905274; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,915 |
| Kinetics | |
| Metal Binding | METAL 76; /note=Zinc 2; /evidence=ECO:0000250; METAL 115; /note=Zinc 1; /evidence=ECO:0000250; METAL 115; /note=Zinc 2; /evidence=ECO:0000250; METAL 146; /note=Zinc 1; /evidence=ECO:0000250; METAL 169; /note=Zinc 2; /evidence=ECO:0000250; METAL 457; /note=Zinc 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |