The ability of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate (HOPDA) hydrolase (BphD) of Burkholderia cepacia LB400 to hydrolyze polychlorinated biphenyl (PCB) metabolites was assessed by determining its specificity for monochlorinated HOPDAs. The relative specificities of BphD for HOPDAs bearing chlorine substituents on the phenyl moiety were 0.28, 0.38, and 1.1 for 8-Cl, 9-Cl, and 10-Cl HOPDA, respectively, versus HOPDA (100 mM phosphate, pH 7.5, 25°C). In contrast, HOPDAs bearing chlorine substituents on the dienoate moiety were poor substrates for BphD, which hydro-

High-resolution crystal structures of Staphylococcus aureus methionine aminopeptidase I in complex with various keto heterocycles and aminoketones were determined, and the intermolecular ligand interactions with the enzyme are reported. The compounds are effective inhibitors of the S. aureus enzyme because of the formation of an uncleavable tetrahedral intermediate upon binding. The electron densities unequivocally show the enzyme-catalyzed transition-state analogue mimicking that for amide bond hydrolysis of substrates.

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Chem. 2002, 67, 3637-3642) suggested that structures attributed by us to 4a, 4d, 7a, and 7d are incorrect. Our own re-investigation led us to conclude that compounds 4a, 4d, 7a, and 7d have aza-bicyclo[3.2.2]nonane structures as depicted in the accompanying graphic. These revised structures have been confirmed by NMR and X-ray analysis.

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S u b s t i t u t e d 2 -( C y a n o m e t h y l -a m i n o ) -a c e t a m i d e sAbstract: A novel three-component, one-pot reaction between primary (S)-amino acid amides, aldehydes and isocyanides in the presence of acetic acid yielding substituted 2-(cyanomethylamino)-acetamides 4 in good yields, is described. First efforts to investigate the mechanism of this reaction were undertaken.

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