| IED ID | IndEnz0018000300 |
| Enzyme Type ID | peroxidase000300 |
| Protein Name |
L-Ala-D/L-Glu epimerase AE epimerase AEE EC 5.1.1.20 |
| Gene Name | ycjG ycjH b1325 JW1318 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MRTVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREELQKILPAGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLISERMVAIRTAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKALKGRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQVSFADLDGPTWLAVDVEPALQFTTGELHL |
| Enzyme Length | 321 |
| Uniprot Accession Number | P51981 |
| Absorption | |
| Active Site | ACT_SITE 151; /note=Proton acceptor; specific for (R)-substrate epimerization; /evidence=ECO:0000250; ACT_SITE 247; /note=Proton acceptor; specific for (S)-substrate epimerization; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 124; /note=Substrate; /evidence=ECO:0000250; BINDING 149; /note=Substrate; /evidence=ECO:0000250; BINDING 275; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250; BINDING 297; /note=Substrate; /evidence=ECO:0000250; BINDING 299; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=L-alanyl-L-glutamate = L-alanyl-D-glutamate; Xref=Rhea:RHEA:28394, ChEBI:CHEBI:61395, ChEBI:CHEBI:61396; EC=5.1.1.20; Evidence={ECO:0000269|PubMed:11747447}; |
| DNA Binding | |
| EC Number | 5.1.1.20 |
| Enzyme Function | FUNCTION: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala. {ECO:0000269|PubMed:11747447, ECO:0000269|PubMed:18535144}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan recycling. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (15); Binding site (5); Chain (1); Erroneous termination (1); Frameshift (1); Helix (17); Metal binding (3); Sequence conflict (5); Turn (1) |
| Keywords | 3D-structure;Cell wall biogenesis/degradation;Isomerase;Magnesium;Metal-binding;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1JPD; |
| Mapped Pubmed ID | 16606699; 18020459; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,674 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for L-Ala-D-Glu (at pH 8.5) {ECO:0000269|PubMed:11747447}; KM=0.19 mM for L-Ala-D-Asp (at pH 8.5) {ECO:0000269|PubMed:11747447}; KM=0.69 mM for L-Ala-D-Met (at pH 8.5) {ECO:0000269|PubMed:11747447}; KM=1.8 mM for L-Ala-D-Gln (at pH 8.5) {ECO:0000269|PubMed:11747447}; |
| Metal Binding | METAL 176; /note=Magnesium; /evidence=ECO:0000250; METAL 202; /note=Magnesium; /evidence=ECO:0000250; METAL 225; /note=Magnesium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:28394 |
| Cross Reference Brenda | 5.1.1.20; |