1. 1,5-ethano-2,3,4,5-tetrahydro-1H-3-benzazepines
L A Walter, W K Chang J Med Chem. 1975 Feb;18(2):206-8.doi: 10.1021/jm00236a022.
1,5-Ethano-2,3,4,5-tetrahydro-1H-3-benzazepine, from the LiA1H4 reduction of 2-benzyloxy-1,5-ethano-4-oxo-2,3,4,5-tetrahydro-1H-3-benzazepine, was converted to N-alkyl, aralkyl, cycloalkyl, and alkenyl derivatives which were inactive as morphine type analgetics in mice. The LiA1H4 reduction of 2-benzyloxy-1,5-etheno-4-oxo-2,3,4,5-tetrahydro-1H-3-benzazepine gave unstable products from which only the skeletally rearranged dihydro- and tetrahydrobenzo[e]isoindolines, were isolated.
2. Enzymes responsible for the conversion of N alpha-[(Benzyloxy)carbonyl]-D-lysine to N alpha-[(Benzyloxy)carbonyl]-D-aminoadipic acid by Rhodococcus sp. AIU Z-35-1
Kimiyasu Isobe, Nahoko Fukuda, Shouko Nagasawa, Kaoru Saitou Chem Biodivers. 2010 Jun;7(6):1549-54.doi: 10.1002/cbdv.200900251.
The enzymes responsible for the conversion of N(alpha)-[(benzyloxy)carbonyl]-D-lysine (N(alpha)-Z-D-lysine) to N(alpha)-Z-D-aminoadipic acid (N(alpha)-Z-D-AAA) by Rhodococcus sp. AIU Z-35-1 were identified. N(alpha)-Z-D-Lysine was first converted to N(alpha)-Z-D-aminoadipic delta-semialdehyde (N(alpha)-Z-D-AASA) by D-specific amino acid deaminase, whereas N(alpha)-Z-L-lysine was converted to N(alpha)-Z-L-AASA by L-specific amino acid oxidase. The resulting N(alpha)-Z-D-AASA was then converted to N(alpha)-Z-D-AAA by the same aldehyde dehydrogenase that is responsible for N(alpha)-Z-L-AASA oxidation. The product amount of the D-specific amino acid deaminase reached the maximum at one day of cultivation in the L-lysine medium. The aldehyde dehydrogenase reached the maximum at three days of cultivation.