EC Number   |
General Information |
Reference |
|---|
   3.5.1.61 | malfunction |
mutational analysis of Mp mimosinase reveals that the disruption of a disulfide bond in the vicinity of the pyridoxal 5'-phosphate domain increases the enzyme's preference toward cystathionine |
754484 |
| 3.5.1.61 | metabolism |
molecular relationship between mimosinase and cystathionine beta-lyase (CBL, UniProt ID A0A0M3VI47, EC 4.4.1.13). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate |
754484 |
| 3.5.1.61 | metabolism |
the carbon-nitrogen lyase catalyzes the first step of mimosine degradation. Mimosine is a toxic nonprotein aromatic amino acid |
734969 |
| 3.5.1.61 | more |
homology modeling and molecular dynamics simulations of Mp mimosinase suggest a closer coordination of the residues that interact with mimosine at the active site compared with cystathionine, indicating a more compact pocket size for mimosine degradation, substrate docking study. Active site structure |
754484 |
| 3.5.1.61 | physiological function |
mimosinase is an important enzyme especially in the context of metabolic engineering of plant secondary metabolite as it catalyzes the degradation of mimosine, which is a toxic secondary metabolite found in all Leucaena and Mimosa species |
754627 |
