EC Number   |
Reaction |
Reference |
|---|
    5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
catalytic mechanism, overview |
727644 |
| 5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
catalytic mechanism, 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 |
| 5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
in the first step of the proposed catalytic cycle the enzyme accepts the substrate in the open state. Substrate interactions with the active site residues initiate an external aldimine formation with PLP breaking the pyridoxal 5'-phosphate-lys144beta internal aldimine, which results in two simultaneous events: (1) the domain motion brings dAdoCbl close to the pyridoxal 5'-phosphate-substrate adduct and locks the enzyme in the catalytically active closed state and (2) cleavage of the Co-C bond of dAdoCbl generates the 5'-deoxyadenosyl radical and cob(II)alamin. Hydrogen abstraction by 5'-deoxyadenosyl radical from the substrate generates deoxyadenosine and the substrate related radical that undergoes radical isomerization via a hypothetical azacyclopropylcarbinyl radical to afford the product related radical. Hydrogen abstraction by the product related radical from deoxyadenosine generates the product-pyridoxal 5'-phosphate adduct and 5'-deoxyadenosyl radical. Finally, transition from the closed state to open state occurs, which allows the release of the product and reformation of dAdoCbl and the internal aldimine |
747510 |
| 5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
radical catalytic mechanism |
727339 |
| 5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase, role of Tyr263alpha. The enzyme utilizes free radical intermediates to mediate 1,2-amino group rearrangement, during which an elusive high-energy aziridincarbinyl radical is proposed to be central in the mechanism of action. The aziridincarbinyl radical acts either as a spin-relay device or serves as an anchor for the pyridine ring of pyridoxal-5' -phosphate through aromatic PI-stacking interactions during spin transfer, detailed overview |
727664 |
| 5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
reaction mechanism, detailed overview |
746577 |
| 5.4.3.3 | (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate |
steric course and mechanistic aspects |
3399 |
| 5.4.3.3 | D-lysine = (2R,5S)-2,5-diaminohexanoate |
catalytic mechanism, overview |
727644 |
| 5.4.3.3 | D-lysine = (2R,5S)-2,5-diaminohexanoate |
catalytic mechanism, 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 |
| 5.4.3.3 | D-lysine = (2R,5S)-2,5-diaminohexanoate |
radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase, role of Tyr263alpha. The enzyme utilizes free radical intermediates to mediate 1,2-amino group rearrangement, during which an elusive high-energy aziridincarbinyl radical is proposed to be central in the mechanism of action. The aziridincarbinyl radical acts either as a spin-relay device or serves as an anchor for the pyridine ring of pyridoxal-5' -phosphate through aromatic PI-stacking interactions during spin transfer, detailed overview |
727664 |
