Reconstitution of Escherichia coli membrane vesicles with D-amino acid dehydrogenase

Biochemistry ◽  
1981 ◽  
Vol 20 (21) ◽  
pp. 6272-6279 ◽  
Author(s):  
Paula J. Olsiewski ◽  
Gregory J. Kaczorowski ◽  
Christopher Walsh ◽  
H. Ronald Kaback
RSC Advances ◽  
2016 ◽  
Vol 6 (84) ◽  
pp. 80557-80563 ◽  
Author(s):  
Jun Cheng ◽  
Guochao Xu ◽  
Ruizhi Han ◽  
Jinjun Dong ◽  
Ye Ni

An amino acid dehydrogenase from Bacillus clausii (BcAADH) was identified and overexpressed in Escherichia coli BL21(DE3) for the preparation of l-phenylglycine from benzoylformic acid.


2002 ◽  
Vol 277 (15) ◽  
pp. 12861-12867 ◽  
Author(s):  
Takenori Satomura ◽  
Ryushi Kawakami ◽  
Haruhiko Sakuraba ◽  
Toshihisa Ohshima

2013 ◽  
Vol 59 (9) ◽  
pp. 598-603 ◽  
Author(s):  
Kathryn E. Oliver ◽  
Laura Silo-Suh

Chronic Pseudomonas aeruginosa infections remain the leading cause of lung dysfunction and mortality for cystic fibrosis (CF) patients. Many other bacteria inhabit the CF lung, but P. aeruginosa utilizes novel strategies that allow it to colonize this environment as the predominant bacterial pathogen. d-Amino acid dehydrogenase encoded by dadA is highly expressed by P. aeruginosa within the CF lung, and it is required for optimal production of hydrogen cyanide by some CF-adapted isolates. To better understand the increased significance of d-amino acid dehydrogenase in P. aeruginosa physiology, we characterized the contribution of the dad operon to virulence factor production. In this study, we determined that DadA is required for optimal production of pyocyanin, pyoverdine, and rhamnolipid by CF-adapted and non-CF-adapted isolates of P. aeruginosa. In addition, DadA is required for optimal production of alginate, biofilm formation, and virulence of a CF-adapted isolated of P. aeruginosa in an alfalfa seedling model of infection. Taken together, the results indicate that DadA plays a pleiotropic role in the production of important virulence factors by P. aeruginosa.


1936 ◽  
Vol 30 (9) ◽  
pp. 1617-1621 ◽  
Author(s):  
Nalin Bandhu Das

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