The single-crystal X-ray diffraction of a novel alkaloid, stellettamine (15), together with long-range lH-13C coupling constants obtained by inverse detection methods, and metal chelation studies have shown that the previously reported regiochemistry of the thiazole moiety of dercitin (1) and four other related alkaloids 2-5 has to be revised. The corrected structures 10-14 are related to, and in one case identical to, those of the kuanoniamines 6-9; A new alcohol dehydrogenase from Pseudomonas sp. strain PED has been isolated and characterized. The enzyme exhibits a broad substrate specificity, accepting aromatic, cyclic, and aliphatic compounds as substrates. The K, values were determined as 525 HM for NAD and 75 pM for 2-propanol with a specific activity of 36 U/mg. The kinetic mechanism is ordered bi-bi with the cofactor binding first and releasing last. The enzyme transfers the pro-R hydride of NADH to the si face of carbonyl compounds to yield (R) alcohols. Synthetic-scale reductions of a number of representative compounds were carried out in high enantiomeric excess with in situ regeneration of NADH using 2-propanol as the hydride source and the same enzyme as catalyst.