EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.5.1.28 | (GlcNAc-MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala)2 + H2O |
- |
Homo sapiens |
? |
- |
? |
| 3.5.1.28 | 1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP + H2O |
- |
Citrobacter freundii |
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP |
- |
? |
| 3.5.1.28 | 1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O |
- |
Citrobacter freundii |
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala |
- |
? |
| 3.5.1.28 | 1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O |
- |
Escherichia coli |
? |
- |
? |
| 3.5.1.28 | 1,6-anhydro-N-acetylmuramic-acid-L-Ala-gamma-D-Glu-L-Lys + H2O |
- |
Escherichia coli |
1,6-anhydro-N-acetylmuramate + L-Ala-gamma-D-Glu-L-Lys |
- |
? |
| 3.5.1.28 | 1,6-anhydromuropeptide + H2O |
AmpD has a strict specificity for 1,6-anhydromuropeptides, three-dimensional structure, active site structure, catalytic mechanism, Lys-162 and Tyr-63 are probably involved in substrate binding |
Citrobacter freundii |
? |
- |
? |
| 3.5.1.28 | 4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O |
the substrate is likely not turned over in vitro by AmpD |
Citrobacter freundii |
? |
- |
? |
| 3.5.1.28 | 7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O |
- |
Staphylococcus epidermidis |
? |
- |
? |
| 3.5.1.28 | 7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O |
- |
Staphylococcus epidermidis |
? |
- |
? |
| 3.5.1.28 | bacterial peptidoglycan + H2O |
- |
Citrobacter freundii |
? |
- |
? |
