Selective inhibition of bovine plasma amine oxidase by homopropargylamine, a new inactivator motif

C Qiao, HB Jeon, LM Sayre

Index: Qiao, Chunhua; Jeon, Heung-Bae; Sayre, Lawrence M. Journal of the American Chemical Society, 2004 , vol. 126, # 25 p. 8038 - 8045

Full Text: HTML

Citation Number: 23

Abstract

Propargylic and activated allylic amines are known to inactivate the quinone-dependent plasma amine oxidases, possibly through active-site modification by the α, β-unsaturated aldehyde turnover products. Although homopropargylamine (1-amino-3-butyne, 1) is a nonobvious candidate as a mechanism-based inhibitor, 1 was found to be an unusually potent time-and concentration-dependent irreversible inactivator of bovine plasma amine ...

Related Articles:

General synthetic access to α-allenyl amines and α-allenyl-α-aminoacids as potential enzyme activated irreversible inhibitors of PLP dependent enzymes

[Casara, Patrick; Jund, Karin; Bey, Philippe Tetrahedron Letters, 1984 , vol. 25, # 18 p. 1891 - 1894]

N-(2, 3-Butadienyl)-1, 4-butanediamine derivatives: potent irreversible inactivators of mammalian polyamine oxidase

[Bey, Philippe; Bolkenius, Frank N.; Seiler, Nikolaus; Casara, Patrick Journal of Medicinal Chemistry, 1985 , vol. 28, # 1 p. 1 - 2]

More Articles...