scholarly journals Enhanced Bacterial Growth and Gene Expression of D-Amino Acid Dehydrogenase With D-Glutamate as the Sole Carbon Source

2018 ◽  
Vol 9 ◽  
Author(s):  
Takeshi Naganuma ◽  
Yoshiakira Iinuma ◽  
Hitomi Nishiwaki ◽  
Ryota Murase ◽  
Kazuo Masaki ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Carbon Source ◽  
Bacterial Growth ◽  
Sole Carbon Source ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase

scholarly journals Dye-linked d-Proline Dehydrogenase from Hyperthermophilic ArchaeonPyrobaculum islandicumIs a Novel FAD-dependent Amino Acid Dehydrogenase

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

Impact ofd-amino acid dehydrogenase on virulence factor production by aPseudomonas aeruginosa

2013 ◽  
Vol 59 (9) ◽  
pp. 598-603 ◽  
Author(s):  
Kathryn E. Oliver ◽  
Laura Silo-Suh
Keyword(s):  
Amino Acid ◽  
Virulence Factor ◽  
Bacterial Pathogen ◽  
Optimal Production ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase ◽  
Factor Production ◽  
Lung Dysfunction ◽  
Production Of Hydrogen ◽  
Virulence Factor Production

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.

scholarly journals Studies on amino-acid dehydrogenase

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

α-Amino acid dehydrogenase models. Reduction of an imine and of iminium salts of α-keto esters by 1,4-dihydropyridines (Preliminary communication)

2010 ◽  
Vol 97 (5) ◽  
pp. 149-150 ◽  
Author(s):  
Upendra K. Pandit ◽  
Margreet J. de Nie-Sarink ◽  
Alida M. van der Burg ◽  
Jan B. Steevens ◽  
Ronald F. M. van Dokkum
Keyword(s):  
Amino Acid ◽  
Keto Esters ◽  
Iminium Salts ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase ◽  
Preliminary Communication

D-Amino acid dehydrogenase

1993 ◽  
pp. 899-904
Author(s):  
Dietmar Schomburg ◽  
Margit Salzmann ◽  
Dörte Stephan
Keyword(s):  
Amino Acid ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase

scholarly journals Purification of Helicobacter pylori NCTC 11637 Cytochrome bc1 and Respiration with d-Proline as a Substrate

2009 ◽  
Vol 192 (5) ◽  
pp. 1410-1415 ◽  
Author(s):  
Minoru Tanigawa ◽  
Tomomitsu Shinohara ◽  
Katsushi Nishimura ◽  
Kumiko Nagata ◽  
Morio Ishizuka ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Amino Acid ◽  
Electron Transport ◽  
Electron Transport Chain ◽  
Electron Flow ◽  
Gene Clusters ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase ◽  
Transport Chain ◽  
H Pylori

ABSTRACT Helicobacter pylori is a microaerophilic bacterium associated with gastric inflammation and peptic ulcers. Knowledge of how pathogenic organisms produce energy is important from a therapeutic point of view. We found d-amino acid dehydrogenase-mediated electron transport from d-proline or d-alanine to oxygen via the respiratory chain in H. pylori. Coupling of the electron transport to ATP synthesis was confirmed by using uncoupler reagents. We reconstituted the electron transport chain to demonstrate the electron flow from the d-amino acids to oxygen using the recombinant cytochrome bc 1 complex, cytochrome c-553, and the terminal oxidase cytochrome cbb 3 complex. Upon addition of the recombinant d-amino acid dehydrogenase and d-proline or d-alanine to the reconstituted electron transport system, reduction of cytochrome cbb 3 and oxygen consumption was revealed spectrophotometrically and polarographically, respectively. Among the constituents of H. pylori's electron transport chain, only the cytochrome bc 1 complex had been remained unpurified. Therefore, we cloned and sequenced the H. pylori NCTC 11637 cytochrome bc 1 gene clusters encoding Rieske Fe-S protein, cytochrome b, and cytochrome c 1, with calculated molecular masses of 18 kDa, 47 kDa, and 32 kDa, respectively, and purified the recombinant monomeric protein complex with a molecular mass of 110 kDa by gel filtration. The absorption spectrum of the recombinant cytochrome bc 1 complex showed an α peak at 561 nm with a shoulder at 552 nm.

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