Pleiotropic Actions of Aldehyde Reductase (AKR1A). [PDF]
Metabolites, 2021 We provide an overview of the physiological roles of aldehyde reductase (AKR1A) and also discuss the functions of aldose reductase (AKR1B) and other family members when necessary. Many types of aldehyde compounds are cytotoxic and some are even carcinogenic.
Fujii J, Homma T, Miyata S, Takahashi M.
europepmc +6 more sources
Elucidation of xenobiotic metabolism pathways in human skin and human skin models by proteomic profiling [PDF]
, 2012 Human skin has the capacity to metabolise foreign chemicals (xenobiotics), but knowledge of the various enzymes involved is incomplete. A broad-based unbiased proteomics approach was used to describe the profile of xenobiotic metabolising enzymes present
Cupitt, John +7 more
core +17 more sources
Mathematical model of the Lux luminescence system in the terrestrial bacterium Photorhabdus luminescens. [PDF]
, 2009 A mathematical model of the Lux luminescence system, governed by the operon luxCDABE in the terrestrial bacterium Photorhabdus luminescens, was constructed using a set of coupled ordinary differential equations.
Stekel, Dov J, Welham, Patricia A
core +1 more source
Functional characterization of SlscADH1, a fruit-ripening associated short-chain alcohol dehydrogenase of tomato [PDF]
, 2012 A tomato short-chain dehydrogenase-reductase (SlscADH1) is preferentially expressed in fruit with a maximum expression at the breaker stage while expression in roots, stems, leaves and flowers is very weak.
Abel +54 more
core +3 more sources
Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa [PDF]
, 2020 Ene reductases enable the asymmetric hydrogenation of activated alkenes allowing the manufacture of valuable chiral products. The enzymes complement existing metal- and organocatalytic approaches for the stereoselective reduction of activated C=C double ...
Aregger, David +2 more
core +1 more source
Immunochemical characterization of aldo-keto reductases from human tissues [PDF]
, 1985 Aldose reductase, aldehyde reductase and carbonyl reductase constitute a family of monomeric NADPH-dependent oxidoreductases with similar physical and chemical properties.
Wermuth, Bendicht, Wirth, Hans-Peter
core +1 more source
Functional and immunological relationships between metyrapone reductase from mouse liver microsomes and 3α-hydroxysteroid dehydrogenase from Pseudomonas testosteroni [PDF]
, 1992 3α-Hydroxysteroid dehydrogenase (3α-HSD) from Pseudomonas testosteroni was shown to reduce the xenobiotic carbonyl compound metyrapone (MPON). Reversely, MPON reductase purified from mouse liver microsomes and previously characterized as aldehyde ...
Bannenberg, Gudula +3 more
core +1 more source
Stereospecificity of cinnamyl alcohol dehydrogenase and synthesis of stereospecifically labelled coniferyl alcohol [PDF]
, 1978 Using horse liver alcohol dehydrogenase, stereospecifically tritiated (R)- and (S)-(γ-3H)-coniferyl alcohol was synthesized. Using both of these substrates it was demonstrated that cinnamyl alcohol dehydrogenase from lignifying Forsythia tissue ...
Klischies, Martina +2 more
core +1 more source
Aldose and Aldehyde Reductase Exhibit Isocorticosteroid Reductase Activity [PDF]
European Journal of Biochemistry, 1983 In this paper we describe the reduction of corticosteroid metabolites containing the 17 beta-aldol side chain (isocorticosteroids) by aldose and aldehyde reductase from human tissues. Aldose reductase catalyzed the reduction of the aldehydes derived from cortisol and corticosterone at about the same rate, whereas aldehyde reductase preferentially acted
Carl Monder, Bendicht Wermuth
openaire +3 more sources
The key role of nitric oxide in hypoxia: hypoxic vasodilation and energy supply-demand matching [PDF]
, 2013 Significance: a mismatch between energy supply and demand induces tissue hypoxia with the potential to cause cell death and organ failure. Whenever arterial oxygen concentration is reduced, increases in blood flow - 'hypoxic vasodilation' - occur in an ...
Alex Dyson +23 more
core +1 more source