Increment of antioxidase activity of transgenic tobacco with betaine aldehyde dehydrogenase

2001 ◽  
Vol 46 (6) ◽  
pp. 492-495
Author(s):  
Ailing Luo ◽  
Jaoyao Liu ◽  
Deqin Ma ◽  
Xuechen Wang ◽  
Zheng Liang
Keyword(s):  
Transgenic Tobacco ◽  
Aldehyde Dehydrogenase ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde ◽  
Antioxidase Activity

Effect of the drug cyclophosphamide on the activity of porcine kidney betaine aldehyde dehydrogenase

2021 ◽  
Author(s):  
Ramses Cruz-Valencia ◽  
Aldo A. Arvizu-Flores ◽  
Jesús A. Rosas-Rodríguez ◽  
Elisa M. Valenzuela-Soto
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Betaine Aldehyde Dehydrogenase ◽  
Porcine Kidney ◽  
Betaine Aldehyde

scholarly journals THE OXIDATION OF BETAINE ALDEHYDE BY BETAINE ALDEHYDE DEHYDROGENASE

1954 ◽  
Vol 209 (2) ◽  
pp. 511-523 ◽  
Author(s):  
H.A. Rothschild ◽  
E.S. Guzman Barron
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde

scholarly journals Production of the Escherichia coli betaine-aldehyde dehydrogenase, an enzyme required for the synthesis of the osmoprotectant glycine betaine, in transgenic plants

1994 ◽  
Vol 6 (5) ◽  
pp. 749-758 ◽  
Author(s):  
Kjell-Ove Holmstrom ◽  
Bjorn Welin ◽  
Abul Mandal ◽  
Ingileif Kristiansdottir ◽  
Teemu H. Teeri ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Transgenic Plants ◽  
Aldehyde Dehydrogenase ◽  
Glycine Betaine ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde

scholarly journals Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa

2000 ◽  
Vol 352 (3) ◽  
pp. 675-683 ◽  
Author(s):  
Roberto VELASCO-GARCÍA ◽  
Lilian GONZÁLEZ-SEGURA ◽  
Rosario A. MUÑOZ-CLARES
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Steady State ◽  
Aldehyde Dehydrogenase ◽  
Substrate Inhibition ◽  
Kinetic Mechanism ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde ◽  
Metabolic Role ◽  
Steady State Kinetic ◽  
State Kinetic

Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)+ to NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. The kinetic mechanisms of the NAD+- and NADP+-dependent reactions were examined by steady-state kinetic methods and by dinucleotide binding experiments. The double-reciprocal patterns obtained for initial velocity with NAD(P)+ and for product and dead-end inhibition establish that both mechanisms are steady-state random. However, quantitative analysis of the inhibitions, and comparison with binding data, suggest a preferred route of addition of substrates and release of products in which NAD(P)+ binds first and NAD(P)H leaves last, particularly in the NADP+-dependent reaction. Abortive binding of the dinucleotides, or their analogue ADP, in the betaine aldehyde site was inferred from total substrate inhibition by the dinucleotides, and parabolic inhibition by NADH and ADP. A weak partial uncompetitive substrate inhibition by the aldehyde was observed only in the NADP+-dependent reaction. The kinetics of P. aeruginosa BADH is very similar to that of glucose-6-phosphate dehydrogenase, suggesting that both enzymes fulfil a similar amphibolic metabolic role when the bacteria grow in choline and when they grow in glucose.

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