EC Number   |
Reaction |
Reference |
|---|
   5.4.3.6 | L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate |
mechanism |
3406 |
| 5.4.3.6 | L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate |
MIO (3,5-dihydro-5-methylidene-4H-imidazol-4-one)-dependent aminomutases begin their reactions by adding the amino group of the substrate to the methylidene carbon of the MIO prosthesis. The enzyme removes the NH2/H pair from the substrate, yielding an NH2-MIO adduct, a tightly bound acrylate intermediate, and protonated catalytic Tyr |
747104 |
| 5.4.3.6 | L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate |
pH-dependent stereochemic mechanism, detailed overview. The enzyme uses a retention-of-configuration mechanism at the amino migration terminus |
727685 |
| 5.4.3.6 | L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate |
the 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) group in the enzyme's active site N-alkylates the NH2 of the alpha-amino acid substrates and promotes the removal of an intermediary NH2-MIO adduct. Concomitant removal of a beta-proton from the substrate (NH2-MIO adduct) by a catalytic tyrosine yields an acrylate intermediate. The aminomutase reaction continues by vicinal reprotonation and reamination at the alpha- and beta-carbons, respectively, of the acrylate to produce the beta-amino acid. Mechanism of MIO-dependent aminomutase, overview |
747148 |
