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Published in 2019 at "ACS Catalysis"
DOI: 10.1021/acscatal.9b00780
Abstract: The enzyme 4-oxalocrotonate tautomerase (4-OT) exploits an N-terminal proline as main catalytic residue to facilitate several promiscuous C–C bond-forming reactions via enzyme-bound enamine intermediates. Here we show that the active site of this enzyme can…
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Keywords:
unsaturated aldehydes;
enzyme bound;
enzyme;
asymmetric michael ... See more keywords