EC Number   |
Reaction |
Reference |
|---|
    5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
conversion of glutamate to methylaspartate catalyzed by glutamate mutase is investigated by quantum mechanical/molecular mechanical simulations based on coupled cluster and density functional calculations, overview. Binding of the Glu substrate induces a homolytic cleavage of the cobalt-carbon bond of the cofactor, which yields a 5'-deoxyadenosyl radical and cob(II)alamin, atom tunneling mechanism |
728191 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
hydrogen transfer occurs directly between coenzyme and product and provides no evidence for the formation of a protein radical |
3454 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
kinetic study of deuterium effects, an isotopically insensitive step is partially rate-determining |
661188 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
kinetic study of tritium effects, reaction has a late transition state |
661116 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
mechanism |
3448, 3453, 3456 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
motions of the 5-hydrogen atoms are coupled in the transition state to the motion of the hydrogen undergoing transfer, in a reaction that involves a large degree of quantum tunneling |
678315 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
no significant activation of coenzyme adenosylcobalamin in absence of substrate |
661930 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
radical mechanism of the conversion of glutamate to methylaspartate catalyzed by glutamate mutase by quantum mechanical/molecular mechanical simulations based on density functional theory, crystal structure analysis |
727661 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
requires Co(II) for coordiation of the acrylate, in order to enable the addition of the radical fragment to the alpha-carbon of this intermediate, leading to the branched product |
3457 |
| 5.4.99.1 | L-threo-3-methylaspartate = L-glutamate |
study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals |
661176 |
