Aldehyde reductase activity in the antennae ofHelicoverpa armigera

2014 ◽  
pp. n/a-n/a ◽  
Author(s):  
H. Guo ◽  
A. Del Corso ◽  
L-Q. Huang ◽  
U. Mura ◽  
P. Pelosi ◽  
...  
Keyword(s):  
Reductase Activity ◽  
Aldehyde Reductase

scholarly journals Aldehyde reductase is a major protein associated with 3-deoxyglucosone reductase activity in rat, pig and human livers

1991 ◽  
Vol 279 (3) ◽  
pp. 903-906 ◽  
Author(s):  
T Kanazu ◽  
M Shinoda ◽  
T Nakayama ◽  
Y Deyashiki ◽  
A Hara ◽  
...  
Keyword(s):  
Rat Liver ◽  
Reductase Activity ◽  
Catalytic Efficiency ◽  
Major Protein ◽  
Aldehyde Reductase ◽  
Reductase Inhibitors ◽  
Major Species ◽  
Human Livers

3-Deoxyglucosone reductase activity in the extracts of rat, pig and human livers was potently inhibited by aldehyde reductase inhibitors. The major species of 3-deoxyglucosone reductase purified from human and pig livers were biochemically and immunochemically identical with aldehyde reductase. The two enzymes and rat liver aldehyde reductase exhibited higher catalytic efficiency for 3-deoxyglucosone than for D-glucuronate, a representative substrate of aldehyde reductase.

Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity

Extremophiles ◽  
2017 ◽  
Vol 21 (6) ◽  
pp. 1101-1110 ◽  
Author(s):  
Raza Ashraf ◽  
Naeem Rashid ◽  
Tamotsu Kanai ◽  
Tadayuki Imanaka ◽  
Muhammad Akhtar
Keyword(s):  
Alcohol Dehydrogenase ◽  
Reductase Activity ◽  
Aldehyde Reductase ◽  
Pyrobaculum Calidifontis

A549 subclones demonstrate heterogeneity in toxicological sensitivity and antioxidant profile

2002 ◽  
Vol 283 (4) ◽  
pp. L726-L736 ◽  
Author(s):  
Nobuo Watanabe ◽  
Dale A. Dickinson ◽  
David M. Krzywanski ◽  
Karen E. Iles ◽  
Hongqiao Zhang ◽  
...  
Keyword(s):  
Actinomycin D ◽  
Reductase Activity ◽  
A549 Cells ◽  
Aldehyde Reductase ◽  
Mechanistic Studies ◽  
Caspase Activation ◽  
Protein Synthesis Inhibitors ◽  
Antioxidant Profile ◽  
Glutathione Reductase Activity ◽  
Limiting Dilution

In A549 cell culture, significant variability was found in sensitivity to actinomycin D. Using limiting dilution, actinomycin D-susceptible (G4S) and -resistant (D3R) subclones were isolated. G4S cells were also susceptible to protein synthesis inhibitors, a redox cycling quinone, and an electrophile with concomitant activation of caspases 3 and 9. D3R cells were resistant to these agents without caspase activation. Antioxidant profiles revealed that D3R cells had significantly higher glutathione and glutathione reductase activity but markedly lower catalase, glutathione peroxidase, and aldehyde reductase activities than G4S cells. Thus A549 cells contain at least two distinct subpopulations with respect to predisposition to cell death and antioxidant profile. Because sensitivities to agents and the antioxidant profile were inconsistent, mechanisms independent of antioxidants, including the apparent inability to activate caspases in D3R cells, may play an important role. Regardless, the results suggest that antioxidant profiles of asymmetrical cell populations cannot predict sensitivity to oxidants and warn that the use of single subclones is advisable for mechanistic studies using A549 or other unstable cell lines.

scholarly journals Escherichia coliYqhD Exhibits Aldehyde Reductase Activity and Protects from the Harmful Effect of Lipid Peroxidation-derived Aldehydes

2008 ◽  
Vol 283 (12) ◽  
pp. 7346-7353 ◽  
Author(s):  
José Manuel Pérez ◽  
Felipe A. Arenas ◽  
Gonzalo A. Pradenas ◽  
Juan M. Sandoval ◽  
Claudio C. Vásquez
Keyword(s):  
Lipid Peroxidation ◽  
Reductase Activity ◽  
Harmful Effect ◽  
Aldehyde Reductase

Further investigation on aldehyde reductase activity in ageing rat tissues

1985 ◽  
Vol 37 (10) ◽  
pp. 744-748 ◽  
Author(s):  
H. Cao Danh ◽  
P. Pasquier-Béchet ◽  
M. Strolin Benedetti ◽  
P. Dostert
Keyword(s):  
Reductase Activity ◽  
Rat Tissues ◽  
Aldehyde Reductase

scholarly journals Unusual Aldehyde Reductase Activity for Production of Full-length Fatty Alcohol by Cyanobacterial Aldehyde Deformylating Oxygenase  

2020 ◽  
Author(s):  
Supacha Buttranon ◽  
Pattarawan Intasian ◽  
Nidar Treesukkasem ◽  
Juthamas Jaroensuk ◽  
Somchart Maenpuen ◽  
...  
Keyword(s):  
Binding Site ◽  
Reductase Activity ◽  
Md Simulations ◽  
Full Length ◽  
Fatty Alcohols ◽  
Aldehyde Reductase ◽  
Anaerobic Conditions ◽  
Alcohol Production ◽  
Reduction Activity ◽  
Fatty Aldehydes

Abstract Background: Aldehyde-deformylating oxygenase (ADO) is a non-heme di-iron enzyme that catalyzes deformylation of aldehydes to generate alkanes/alkenes. In this study, we report for the first time that under anaerobic or limited oxygen conditions, Prochlorococcus marinus (PmADO) can generate full-length fatty alcohols from fatty aldehydes without eliminating a carbon unit. Results: Unlike the native activity of ADO which requires electrons from the Fd/FNR electron transfer complex, the aldehyde reduction activity of ADO requires only NADPH. Our results demonstrated that yield of alcohol products can be affected by oxygen concentration and type of aldehyde. Under O2-scant conditions (10-15%), yields of octanol and dodecanol were around 40-60% and could be increased up to 80% under strict anaerobic conditions (>0.0004%). Unexpectedly, Fe2+ cofactor is not involved in the aldehyde reductase activity of PmADO because yields of alcohols obtained from holo- and apo-enzymes were similar under anaerobic conditions. The direct hydride transfer activity of PmADO is highly specific to substrates; NADPH not NADH can be used as a reductant to reduce medium-chain fatty aldehydes (C6-C10) with decanal as the most preferred substrate (the highest kcat/Km value with 98% bioconversion yield). Molecular dynamics (MD) simulations was used to identify a binding site of NADPH which is located close to the aldehyde binding site. In the metabolic engineered cells containing PmADO, dual activities of alkane and alcohol production could be detected. Conclusion: The findings reported herein highlight a new activity of PmADO which may be applied as a biocatalyst for industrial synthesis of fatty alcohols in the future.

Age-Related Changes in Aldehyde Reductase Activity of Rat Brain, Liver and Heart

Gerontology ◽  
1984 ◽  
Vol 30 (3) ◽  
pp. 159-166 ◽  
Author(s):  
H. Cao Danh ◽  
M. Strolin Benedetti ◽  
P. Dostert
Keyword(s):  
Rat Brain ◽  
Reductase Activity ◽  
Aldehyde Reductase ◽  
Age Related ◽  
Age Related Changes
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