24431-54-7Relevant articles and documents
Oxidation of acetylpolyamines by maize polyamine oxidase
Federico, Rodolfo,Ercolini, Luca,Laurenzi, Maria,Angelini, Riccardo
, p. 339 - 341 (2007/10/03)
The oxidation of acetylpolyamines by celt wall polyamine oxidase from maize shoots was investigated. The purified enzyme catalysed the oxidation of N1-acetylspermine, N1-acetylspermidine, and N8-acetylspermidine at the same optimal pH (6.5), but with lower relative velocities and higher K(m) than those found for spermine and spermidine oxidation. The enzyme cleaved N1-acetylspermine and N8-acetylspermidine, at the same positions as in spermine and spermidine oxidation, with the production of H2O2, 1,3- diaminopropane and the corresponding aminoaldehydes. Polyamine oxidase was quickly inactivated by catalysis, and the aminoaldehyde derived from N1- acetylspermine behaved as a competitive inhibitor of the enzyme (K(m) = 20 μM). These findings suggest that cell wait polyamine oxidase from maize shoots does not effect the interconversion pathway of acetylpolyamines found in vertebrates.
Novel Amide-Directed Hydrocarbonylation and Double Carbonylation of N-Allylamides
Ojima, Iwao,Zhang, Zhaoda
, p. 4422 - 4425 (2007/10/02)
The rhodium-catalyzed hydroformylation and palladium-catalyzed hydroesteryfication of N-allylamides give isoaldehyde (1) and isoester (5), respectively, with good regioselectivity through chelation control while the rhodium- and Co2Rh2(CO)12-catalyzed reactions of an N-methallylamide give a novel double carbonylation product (10) and a pyrrolidine (11), respectively, with exellent selectivity.
