Results 51 to 60 of about 63,777 (193)

Characterisation of components and mechanisms involved in redox-regulation of protein import into chloroplasts [PDF]

open access: yes, 2009
The vast majority of chloroplast proteins is encoded in the nucleus and thus has to be posttranslationally imported into the organelle, a process that is facilitated by two multimeric protein machineries, the Toc and Tic complexes (translocon at the ...
Stengel, Anna
core  

Dynamic and Static Regulation of Nicotinamide Adenine Dinucleotide Phosphate: Strategies, Challenges, and Future Directions in Metabolic Engineering

open access: yesMolecules
Reduced nicotinamide adenine dinucleotide phosphate (NADPH) is a crucial cofactor in metabolic networks. The efficient regeneration of NADPH is one of the limiting factors for productivity in biotransformation processes.
Nana Ding   +3 more
doaj   +1 more source

Short-Term Low Temperature Induces Nitro-Oxidative Stress that Deregulates the NADP-Malic Enzyme Function by Tyrosine Nitration in Arabidopsis thaliana

open access: yesAntioxidants, 2019
Low temperature (LT) negatively affects plant growth and development via the alteration of the metabolism of reactive oxygen and nitrogen species (ROS and RNS).
Juan C. Begara-Morales   +8 more
doaj   +1 more source

A Novel Type II NAD+-Specific Isocitrate Dehydrogenase from the Marine Bacterium Congregibacter litoralis KT71. [PDF]

open access: yesPLoS ONE, 2015
In most living organisms, isocitrate dehydrogenases (IDHs) convert isocitrate into ɑ-ketoglutarate (ɑ-KG). Phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-
Ming-Cai Wu   +5 more
doaj   +1 more source

Flavin-containing monooxygenases: mutations, disease and drug response [PDF]

open access: yes, 2008
NOTICE: this is the author’s version of a work that was accepted for publication in Trends in Pharmacological Sciences. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality ...
Phillips, IR, Shephard, EA
core   +1 more source

Complex‐Forming Properties of Spinach NADP+ Reductase with Ferredoxin, Ferrocyanide and NADP+ [PDF]

open access: yesEuropean Journal of Biochemistry, 1980
The flavoprotein NADP+ reductase from spinach chloroplasts may form a ternary complex with one molecule of NADP+ and one molecule of ferredoxin. Spectroscopic titration studies show that the NADP+ binding site and the ferredoxin binding site are totally independent, that is previous binding of ferredoxin does not modify binding of NADP+, and conversely.
Grigorios Diamantidis   +2 more
openaire   +3 more sources

Mitochondrial NAD kinase in health and disease

open access: yesRedox Biology, 2023
Nicotinamide adenine dinucleotide phosphate (NADP), a co-enzyme and an electron carrier, plays crucial roles in numerous biological functions, including cellular metabolism and antioxidation.
Ren Zhang, Kezhong Zhang
doaj  

Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation

open access: yesAntioxidants, 2019
NADP-dependent (Nicotinamide Adénine Dinucléotide Phosphate-dependent) isocitrate dehydrogenases (NADP-ICDH) are metabolic enzymes involved in 2-oxoglutarate biosynthesis, but they also supply cells with NADPH. Different NADP-ICDH genes are
Adnan Khan Niazi   +6 more
doaj   +1 more source

Stereospecificity of cinnamyl alcohol dehydrogenase and synthesis of stereospecifically labelled coniferyl alcohol [PDF]

open access: yes, 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

Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties. [PDF]

open access: yesJournal of Biological Chemistry, 1986
The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex. With the exception of 3'-NADP+, only adenosine nucleotides with a 2'-adenosyl phosphate bound to Fd-NADP ...
C J Batie, H Kamin
openaire   +2 more sources

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