| IED ID | IndEnz0002002625 |
| Enzyme Type ID | protease002625 |
| Protein Name |
Succinyl-diaminopimelate desuccinylase SDAP desuccinylase EC 3.5.1.18 Aspartyl peptidase N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase |
| Gene Name | dapE STM2483 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MSCPVIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRGRGETLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLVGEPSSTEIVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA |
| Enzyme Length | 375 |
| Uniprot Accession Number | Q8ZN75 |
| Absorption | |
| Active Site | ACT_SITE 68; /evidence=ECO:0000250; ACT_SITE 133; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Mn(2+)-activated peptidase is inhibited by Mn(2+) at concentration above 1 mM and by increasing concnentrations of Co(2+). There is a competitive inhibitor effect between the substrates. Hydrolysis of Asp-Leu by Mn(2+)-activated DapE is inhibited by SDAP, and hydrolysis of SDAP by Co(2+)-activated DapE is inhibited by Asp-Ser. {ECO:0000269|PubMed:12896993}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608, ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609, ChEBI:CHEBI:58087; EC=3.5.1.18; |
| DNA Binding | |
| EC Number | 3.5.1.18 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. Can also hydrolyze all N-terminal Asp dipeptides except Asp-Pro. Asp-Ser is the best substrate, followed by Asp-Gly, Asp-Leu, and Asp-Cys. {ECO:0000269|PubMed:12896993}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6) |
| Keywords | Amino-acid biosynthesis;Cobalt;Diaminopimelate biosynthesis;Dipeptidase;Hydrolase;Lysine biosynthesis;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,578 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.63 mM for SDAP (in the presence of 1 mM Co(2+) {ECO:0000269|PubMed:12896993}; KM=0.66 mM for Asp-Ser (in the presence of 1 mM Mn(2+) {ECO:0000269|PubMed:12896993}; KM=3.3 mM for Asp-Leu (in the presence of 1 mM Mn(2+) {ECO:0000269|PubMed:12896993}; |
| Metal Binding | METAL 66; /note=Zinc 1; /evidence=ECO:0000250; METAL 99; /note=Zinc 1; /evidence=ECO:0000250; METAL 99; /note=Zinc 2; /evidence=ECO:0000250; METAL 134; /note=Zinc 2; /evidence=ECO:0000250; METAL 162; /note=Zinc 1; /evidence=ECO:0000250; METAL 348; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | RHEA:22608 |
| Cross Reference Brenda |