| IED ID | IndEnz0002016720 |
| Enzyme Type ID | protease016720 |
| Protein Name |
D-alanyl-D-alanine-carboxypeptidase/endopeptidase AmpH EC 3.4.-.- DD-alanine-endopeptidase DD-carboxypeptidase Penicillin-binding protein AmpH |
| Gene Name | ampH yaiH b0376 JW5052 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKRSLLFSAVLCAASLTSVHAAQPITEPEFASDIVDRYADHIFYGSGATGMALVVIDGNQRVFRSYGETRPGNNVRPQLDSVVRIASLTKLMTSEMLVKLLDQGTVKLNDPLSKYAPPGARVPTYNGTPITLVNLATHTSALPREQPGGAAHRPVFVWPTREQRWKYLSTAKLKAAPGSQAAYSNLAFDLLADALANASGKPYTQLFEEQITRPLGMKDTTYTPSPDQCRRLMVAERGASPCNNTLAAIGSGGVYSTPGDMMRWMQQYLSSDFYQRSNQADRMQTLIYQRAQFTKVIGMDVPGKADALGLGWVYMAPKEGRPGIIQKTGGGGGFITYMAMIPQKNIGAFVVVTRSPLTRFKNMSDGINDLVTELSGNKPLVIPAS |
| Enzyme Length | 385 |
| Uniprot Accession Number | P0AD70 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cefmetazole. {ECO:0000269|PubMed:22001512}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Hydrolyzes the cross-linked dimers tetrapentapeptide (D45) and tetratetrapeptide (D44). Removes the terminal D-alanine from muropeptides and disaccharide pentapeptide M5 with a C-terminal D-Ala-D-Ala dipeptide. Associated with recycling and remodeling of peptidoglycan (PG). Also displays a low beta-lactamase activity. {ECO:0000269|PubMed:22001512}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Erroneous initiation (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:22001512}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:22001512 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,849 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=102 uM for D45 (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:22001512}; KM=134 uM for D44 (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:22001512}; KM=225 uM for M5 (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:22001512}; Vmax=4.98 nmol/min/ug enzyme with M5 as substrate (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:22001512}; Vmax=162 nmol/min/ug enzyme with D44 as substrate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:22001512}; Vmax=174 nmol/min/ug enzyme with D45 as substrate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:22001512}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |