enzyme additionally catalyzes the reduction of quinones, reaction of EC 188.8.131.52. The enzyme shows a low level of activity with cinnamaldehyde and no activity with 2-cyclohexen-1-one and 15-ketoprostaglandin E2. No activity is detected with nonanal and 2-nonene
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to 1.85 A resolution. The overall structure displays the typical medium-chain dehydrogenase fold with two domains: the catalytic domain, residues 1-128 and 271-329, and the coenzyme-binding domain, residues 129-270, which are separated by a deep cleft that binds the cofactor NADP+ and the substrate