polyamine oxidase (propane-1,3-diamine-forming) 1.5.3.14

2013 ◽  
pp. 416-425
Author(s):  
Dietmar Schomburg ◽  
Ida Schomburg
Keyword(s):  
2016 ◽  
Vol 42 (5) ◽  
pp. 734 ◽  
Author(s):  
Tong-Zhen ZHANG ◽  
Yong-Sheng LI ◽  
Yue LI ◽  
Hai-Mei YAO ◽  
Juan ZHAO ◽  
...  

1995 ◽  
Vol 145 (5-6) ◽  
pp. 686-692 ◽  
Author(s):  
Riccardo Angelini ◽  
Rodolfo Federico ◽  
Paola Bonfante

Biochemistry ◽  
2004 ◽  
Vol 43 (12) ◽  
pp. 3426-3435 ◽  
Author(s):  
Alessandra Cona ◽  
Fabrizio Manetti ◽  
Rosalida Leone ◽  
Federico Corelli ◽  
Paraskevi Tavladoraki ◽  
...  

Author(s):  
Yoshinori Kobayashi ◽  
Toshihiko Higashi ◽  
Haruo Machida ◽  
Shinjiro Iwasaki ◽  
Koki Horikoshi

2007 ◽  
Vol 35 (2) ◽  
pp. 396-400 ◽  
Author(s):  
A. Lentini ◽  
P. Mattioli ◽  
B. Provenzano ◽  
A. Abbruzzese ◽  
M. Caraglia ◽  
...  

Protein-bound γ-glutamylpolyamines have highlighted a new pathway in polyamine metabolism. Human foreskin keratinocytes offer a suitable model for this study. Indeed, they develop polymerized envelopes, as they differentiate, rich in ϵ-(γ-glutamyl)lysine and N1,N8-bis(γ-glutamyl)spermidine cross-links. We have found that the selective oxidation of N1-(γ-glutamyl)spermidine and N-(γ-glutamyl)spermine by FAD-dependent polyamine oxidase (PAO) may be one of the cellular mechanisms regulating the preferential formation of a sterically defined bis(γ-glutamyl)spermidine cross-link. The significance of this finding is unknown, but it suggests that the target of this PAO-modulation is to achieve the biochemical prerequisite for production of a normal epidermal stratum corneum.


1995 ◽  
Vol 1244 (1) ◽  
pp. 198-202 ◽  
Author(s):  
Angela Sessa ◽  
Patrizia Tunici ◽  
Stanley W.B. Ewen ◽  
George Grant ◽  
Arpad Pusztai ◽  
...  

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