EC Number   |
General Information |
Reference |
|---|
    5.4.3.3 | evolution |
the enzyme belongs to the class III dAdoCbl-dependent isomerase family |
727644 |
| 5.4.3.3 | malfunction |
the D298N, D298A, K370Q, and K370A variants of the alpha-subunits abolish the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid |
747510 |
| 5.4.3.3 | metabolism |
lysine 5,6-aminomutase is essential for the metabolism of L- or D-lysine in anaerobic bacteria |
705339 |
| 5.4.3.3 | metabolism |
lysine 5,6-aminomutase participates in the fermentation of L- or D-lysine as carbon and nitrogen sources in anaerobic bacteria |
702340 |
| 5.4.3.3 | metabolism |
the enzyme participates in the second step of the fermentation pathway of lysine in which lysine is converted to acetic acid, ammonia and butyric acid |
727644 |
| 5.4.3.3 | more |
a large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. The recombinant enzyme (KamDE) containing only E1 is active, but is subjected to suicide inactivation with the substrate |
727644 |
| 5.4.3.3 | more |
active site structure, overview. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. The recombinant enzyme (KamDE) containing only E1 is active, but is subjected to suicide inactivation with the substrate. Modeling of the closed conformation of the enzyme, domain motions, overview |
727644 |
| 5.4.3.3 | more |
both Asp298alpha and Lys370alpha are functionally important residues in enzyme 5,6-LAM |
747510 |
| 5.4.3.3 | more |
lysine 5,6-aminomutase (5,6-LAM) from Clostridium sticklandii is an adenosylcobalamin (AdoCbl) and pyridoxal 5'-phosphate (PLP)-dependent enzyme |
747193 |
| 5.4.3.3 | more |
the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine |
-, 727695 |
