| IED ID | IndEnz0002004965 |
| Enzyme Type ID | protease004965 |
| Protein Name |
Murein peptide amidase A EC 3.4.17.- Gamma-D-Glu-Dap amidase Zinc metallocarboxypeptidase MpaA |
| Gene Name | mpaA ycjI b1326 JW1319 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTVTRPRAERGAFPPGTEHYGRSLLGAPLIWFPAPAASRESGLILAGTHGDENSSVVTLSCALRTLTPSLRRHHVVLCVNPDGCQLGLRANANGVDLNRNFPAANWKEGETVYRWNSAAEERDVVLLTGDKPGSEPETQALCQLIHRIQPAWVVSFHDPLACIEDPRHSELGEWLAQAFELPLVTSVGYETPGSFGSWCADLNLHCITAEFPPISSDEASEKYLFAMANLLRWHPKDAIRPS |
| Enzyme Length | 242 |
| Uniprot Accession Number | P0ACV6 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:22970852}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791, ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:12511517, ECO:0000269|PubMed:22970852}; |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap (PubMed:12511517, PubMed:22970852). Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap (PubMed:22970852). Cannot hydrolyze murein tetrapeptide (PubMed:22970852). {ECO:0000269|PubMed:12511517, ECO:0000269|PubMed:22970852}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22970852}; |
| Pathway | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:22970852}. |
| nucleotide Binding | |
| Features | Chain (1); Erroneous initiation (1); Metal binding (3) |
| Keywords | Carboxypeptidase;Cell wall biogenesis/degradation;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:12511517}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,558 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.41 mM for L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid {ECO:0000269|PubMed:22970852}; Note=kcat is 38.3 sec(-1). {ECO:0000269|PubMed:22970852}; |
| Metal Binding | METAL 49; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000250|UniProtKB:A7N805, ECO:0000255|HAMAP-Rule:MF_02211"; METAL 52; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:A7N805, ECO:0000255|HAMAP-Rule:MF_02211"; METAL 157; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000250|UniProtKB:A7N805, ECO:0000255|HAMAP-Rule:MF_02211" |
| Rhea ID | RHEA:28398 |
| Cross Reference Brenda |