Enhanced Stress Tolerance in Escherichia coli and Nicotiana tabacum Expressing a Betaine Aldehyde Dehydrogenase/Choline Dehydrogenase Fusion Protein

2002 ◽  
Vol 18 (6) ◽  
pp. 1176-1182 ◽  
Author(s):  
J. Lindberg ◽  
L. Bulow
Keyword(s):  
Escherichia Coli ◽  
Nicotiana Tabacum ◽  
Fusion Protein ◽  
Stress Tolerance ◽  
Aldehyde Dehydrogenase ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde ◽  
Choline Dehydrogenase

Optimization of the Heterologous Expression of Sesuvium portulacastrum Betaine Aldehyde Dehydrogenase in Escherichia coli

2013 ◽  
Vol 864-867 ◽  
pp. 221-224
Author(s):  
Cheng Long Yang ◽  
Rui Mei Li ◽  
Yang Zhou ◽  
Rui Jun Duan ◽  
Shao Ping Fu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Aldehyde Dehydrogenase ◽  
Induction Time ◽  
Expression System ◽  
Betaine Aldehyde Dehydrogenase ◽  
Sesuvium Portulacastrum ◽  
Betaine Aldehyde ◽  
Dehydrogenase Gene ◽  
Full Length Sequence

A full-length sequence coding for a betaine aldehyde dehydrogenase gene from S. portulacastrum was cloned into expression vector pGEX-4T-1, and named pGEX-4T-SpBADH. The GST-SpBADH fusion protein was expressed and the expression conditions were optimized. Through the research on optimization of expression the concentration of IPTG, concentration of bacterium, induction time and temperature and so on, the results showed, the expression of GST-SpBADH increased accompany with the induction time. The expression level of GST-SpBADH fusion protein reached the highest for 5 h cultured and for OD600 is about 0.6 at 37°C, 0.2 mmol/L IPTG can effectively induce the expression of GST-SpBADH in Escherichia coli expression system.

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

Betaine aldehyde dehydrogenase from Pseudomonas aeruginosa: cloning, over-expression in Escherichia coli, and regulation by choline and salt

2005 ◽  
Vol 185 (1) ◽  
pp. 14-22 ◽  
Author(s):  
Roberto Velasco-García ◽  
Miguel Angel Villalobos ◽  
Miguel A. Ramírez-Romero ◽  
Carlos Mújica-Jiménez ◽  
Gabriel Iturriaga ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Aldehyde Dehydrogenase ◽  
Betaine Aldehyde Dehydrogenase ◽  
Over Expression ◽  
Betaine Aldehyde ◽  
Expression In Escherichia Coli

scholarly journals Structural and functional analysis of betaine aldehyde dehydrogenase fromStaphylococcus aureus

2015 ◽  
Vol 71 (5) ◽  
pp. 1159-1175 ◽  
Author(s):  
Andrei S. Halavaty ◽  
Rebecca L. Rich ◽  
Chao Chen ◽  
Jeong Chan Joo ◽  
George Minasov ◽  
...  
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Molecular Mechanisms ◽  
Betaine Aldehyde Dehydrogenase ◽  
Wild Type ◽  
High Osmolarity ◽  
Betaine Aldehyde ◽  
Choline Dehydrogenase ◽  
Buffer Composition ◽  
Primary Substrate

When exposed to high osmolarity, methicillin-resistantStaphylococcus aureus(MRSA) restores its growth and establishes a new steady state by accumulating the osmoprotectant metabolite betaine. Effective osmoregulation has also been implicated in the acquirement of a profound antibiotic resistance by MRSA. Betaine can be obtained from the bacterial habitat or produced intracellularly from cholineviathe toxic betaine aldehyde (BA) employing the choline dehydrogenase and betaine aldehyde dehydrogenase (BADH) enzymes. Here, it is shown that the putative betaine aldehyde dehydrogenase SACOL2628 from the early MRSA isolate COL (SaBADH) utilizes betaine aldehyde as the primary substrate and nicotinamide adenine dinucleotide (NAD+) as the cofactor. Surface plasmon resonance experiments revealed that the affinity of NAD+, NADH and BA forSaBADH is affected by temperature, pH and buffer composition. Five crystal structures of the wild type and three structures of the Gly234Ser mutant ofSaBADH in the apo and holo forms provide details of the molecular mechanisms of activity and substrate specificity/inhibition of this enzyme.

scholarly journals Betaine Aldehyde Dehydrogenase (BADH) vs. Flavodoxin (Fld): Two Important Genes for Enhancing Plants Stress Tolerance and Productivity

2021 ◽  
Vol 12 ◽  
Author(s):  
Mohsen Niazian ◽  
Seyed Ahmad Sadat-Noori ◽  
Masoud Tohidfar ◽  
Seyed Mohammad Mahdi Mortazavian ◽  
Paolo Sabbatini
Keyword(s):  
Stress Tolerance ◽  
Plant Species ◽  
Aldehyde Dehydrogenase ◽  
Abiotic Stresses ◽  
Plant Stress ◽  
Photosynthetic Apparatus ◽  
Betaine Aldehyde Dehydrogenase ◽  
Enzymatic Antioxidants ◽  
Betaine Aldehyde ◽  
Plant Stress Tolerance

Abiotic stresses, mainly salinity and drought, are the most important environmental threats that constrain worldwide food security by hampering plant growth and productivity. Plants cope with the adverse effects of these stresses by implementing a series of morpho-physio-biochemical adaptation mechanisms. Accumulating effective osmo-protectants, such as proline and glycine betaine (GB), is one of the important plant stress tolerance strategies. These osmolytes can trigger plant stress tolerance mechanisms, which include stress signal transduction, activating resistance genes, increasing levels of enzymatic and non-enzymatic antioxidants, protecting cell osmotic pressure, enhancing cell membrane integrity, as well as protecting their photosynthetic apparatus, especially the photosystem II (PSII) complex. Genetic engineering, as one of the most important plant biotechnology methods, helps to expedite the development of stress-tolerant plants by introducing the key tolerance genes involved in the biosynthetic pathways of osmolytes into plants. Betaine aldehyde dehydrogenase (BADH) is one of the important genes involved in the biosynthetic pathway of GB, and its introduction has led to an increased tolerance to a variety of abiotic stresses in different plant species. Replacing down-regulated ferredoxin at the acceptor side of photosystem I (PSI) with its isofunctional counterpart electron carrier (flavodoxin) is another applicable strategy to strengthen the photosynthetic apparatus of plants under stressful conditions. Heterologous expression of microbially-sourced flavodoxin (Fld) in higher plants compensates for the deficiency of ferredoxin expression and enhances their stress tolerance. BADH and Fld are multifunctional transgenes that increase the stress tolerance of different plant species and maintain their production under stressful situations by protecting and enhancing their photosynthetic apparatus. In addition to increasing stress tolerance, both BADH and Fld genes can improve the productivity, symbiotic performance, and longevity of plants. Because of the multigenic and complex nature of abiotic stresses, the concomitant delivery of BADH and Fld transgenes can lead to more satisfying results in desired plants, as these two genes enhance plant stress tolerance through different mechanisms, and their cumulative effect can be much more beneficial than their individual ones. The importance of BADH and Fld genes in enhancing plant productivity under stress conditions has been discussed in detail in the present review.

Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: purification, characterization, and comparison with human cytoplasmic E3 isozyme

1999 ◽  
Vol 77 (3) ◽  
pp. 179-187 ◽  
Author(s):  
Ming -Kai Chern ◽  
Regina Pietruszko
Keyword(s):  
Substrate Specificity ◽  
Rat Liver ◽  
Aldehyde Dehydrogenase ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde ◽  
Choline Dehydrogenase ◽  
First Time

Betaine aldehyde dehydrogenase has been purified to homogeneity from rat liver mitochondria. The properties of betaine aldehyde dehydrogenase were similar to those of human cytoplasmic E3 isozyme in substrate specificity and kinetic constants for substrates. The primary structure of four tryptic peptides was also similar; only two substitutions, at most, per peptide were observed. Thus, betaine aldehyde dehydrogenase is not a specific enzyme, as formerly believed; activity with betaine aldehyde is a property of aldehyde dehydrogenase (EC 1.2.1.3), which has broad substrate specificity. Up to the present time the enzyme was thought to be cytoplasmic in mammals. This report establishes, for the first time, mitochondrial subcellular localization for aldehyde dehydrogenase, which dehydrogenates betaine aldehyde, and its colocalization with choline dehydrogenase. Betaine aldehyde dehydrogenation is an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source. This is the first purification and characterization of mitochondrial betaine aldehyde dehydrogenase from any mammalian species.Key words: betaine, aldehyde, dehydrogenase, mitochondria, rat liver.

Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH) : structural similarity to mammalian ALDHs and a plant BADH

Gene ◽  
1991 ◽  
Vol 103 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Lesley A. Boyd ◽  
Luc Adam ◽  
Lawrence E. Pelcher ◽  
Alan McHughen ◽  
Rozina Hirji ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Aldehyde Dehydrogenase ◽  
Structural Similarity ◽  
Betaine Aldehyde Dehydrogenase ◽  
Gene Encoding ◽  
Betaine Aldehyde

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
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