Pseudomonas putida PydR, a RutR-like transcriptional regulator, represses the dihydropyrimidine dehydrogenase gene in the pyrimidine reductive catabolic pathway

2012 ◽  
Vol 152 (4) ◽  
pp. 341-346 ◽  
Author(s):  
R. Hidese ◽  
H. Mihara ◽  
T. Kurihara ◽  
N. Esaki
2021 ◽  
Author(s):  
Brendan T. Keenan ◽  
Raymond J. Galante ◽  
Jie Lian ◽  
Lin Zhang ◽  
Xiaofeng Guo ◽  
...  

1986 ◽  
Vol 64 (12) ◽  
pp. 1288-1293 ◽  
Author(s):  
Josefa M. Alonso ◽  
Amando Garrido-Pertierra

5-Carboxymethyl-2-hydroxymuconic semialdehyde (CHMSA) dehydrogenase in the 4-hydroxyphenylacetate meta-cleavage pathway was purified from Pseudomonas putida by gel filtration, anion-exchange, and affinity chromatographies. Sodium dodecyl sulfate – polyacrylamide gel electrophoresis analysis suggested an approximate tetrameric molecular weight of 200 000. The purified enzyme showed a pH optimum at 7.8. The temperature–activity relationship for the enzyme from 27 to 45 °C showed broken Arrhenius plots with an inflexion at 36–37 °C. Under standard assay conditions, the enzyme acted preferentially with NAD. It could also catalyze the reduction with NADP (which had a higher Km), at 18% of the rate observed for NAD. The following kinetic parameters were found: Km(NAD) = 20.0 ± 3.6 μM, Km(CHMSA) = 8.5 ± 1.8 μM, and Kd(enzyme–NAD complex) = 7.8 ± 2.0 μM. The product NADH acted as a competitive inhibitor against NAD.


2020 ◽  
Vol 239 ◽  
pp. 126550
Author(s):  
Dharmendra Nath Bhatt ◽  
Sekhu Ansari ◽  
Anil Kumar ◽  
Sumit Ghosh ◽  
Alka Narula ◽  
...  

Author(s):  
André B.P. van Kuilenburg ◽  
Judith Meijer ◽  
Michael W.T. Tanck ◽  
Doreen Dobritzsch ◽  
Lida Zoetekouw ◽  
...  

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