Search results for "REDUCTASE"
showing 10 items of 798 documents
The NreA Protein Functions as a Nitrate Receptor in the Staphylococcal Nitrate Regulation System
2013
Staphylococci are able to use nitrate as an alternative electron acceptor during anaerobic respiration. The regulation of energy metabolism is dependent on the presence of oxygen and nitrate. Under anaerobic conditions, staphylococci employ the nitrate regulatory element (Nre) for transcriptional activation of genes involved in reduction and transport of nitrate and nitrite. Of the three proteins that constitute the Nre system, NreB has been characterized as an oxygen sensor kinase and NreC has been characterized as its cognate response regulator. Here, we present structural and functional data that establish NreA as a new type of nitrate receptor. The structure of NreA with bound nitrate w…
Antioxidant properties, superoxide dismutase and glutathione reductase activities in HepG2 cells with a fungal endophyte producing apigenin from pige…
2012
Abstract A fungal endophyte MD89 with obvious antioxidant activities was isolated from pigeon pea and identified as Chaetomium globosum by ITS sequence. Different fractions from MD89 culture were compared and evaluated by total phenol (TP) content, total flavonoid (TFL) content, DPPH radical scavenging, reducing power and lipid peroxidation assays, respectively. Results showed that EtOAc extracts had high content of TP and TFL, and strong antioxidant activities (IC 50 value was 6.87, 15.19, 16.78 μg/mL, respectively). Furthermore, the EtOAc extracts were analyzed by LC–MS/MS and a good antioxidant compound, apigenin, was found. The activities of superoxide dismutase (SOD) and glutathione re…
Semiquantitative bioluminescent assay of glutathione
1998
A novel technique has been developed for semiquantitative detection of glutathione (GSH) in small volumes of liquid samples. GSH is detected via enzymatic linkage to the NADP/NADPH + H+ redox system through glutathione reductase. Accumulated NADPH is measured via the bioluminescent FMN oxidoreductase bacterial luciferase reaction. A linear correlation is obtained between bioluminescence intensity of the luciferase reaction and the GSH content of the liquid sample. Possible applications of this procedure are discussed. © 1998 John Wiley & Sons, Ltd.
Thioredoxin-related protein of 14 kDa may directly reduce protein cysteinylation motifs
2018
Disulfide stress has been associated with inflammation and characterized by an increase in cystine levels and protein cysteinylation. Furthermore, it was recently discovered that thioredoxin-related protein of 14 kDa (TRP14, encoded by TXNDC17) exhibits efficient cystine reductase activity. The aim of our research was to elucidate if TRP14 is also able to reduce cysteinylated proteins in mammalian cells. Thus, protein cysteinylation was assessed in control and TRP14 knockdown cells in vitro through their pre-treatment with 25 µg/ml cycloheximide for 30 min and incubation with 250 µM biotinylated cysteine for 1 h. Moreover, such TRP14 knockdown cell lysates were tested as cysteinylated subst…
Structure and function of ferredoxin-NADP+-oxidoreductase
1987
The redox-enzyme ferredoxin-NADP-oxidoreductase has been shown to be activated by light and inactivated in the dark. This review will summarize recent data concerning the biochemical characterization of the enzyme compared to its in-vivo activation. Further-more the mechanism of this activation process is discussed as a conformational change caused by the light-driven proton gradient.
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a lig…
1984
The structure and function of the 2-oxoglutarate binding site of prolyl 4-hydroxylase was studied by assaying the inhibitory potential of 24 selected aliphatic or aromatic compounds. All except one of them inhibited the enzyme competitively with respect to 2-oxoglutarate and noncompetitively with respect to Fe2+, the Ki values ranging from 0.8 microM to over 15 mM. The Ki values for the two most effective inhibitors, pyridine 2,5-dicarboxylate and 2,4-dicarboxylate, were about 0.8 microM and 2 microM, these compounds being the most potent inhibitors of prolyl 4-hydroxylase with respect to 2-oxoglutarate known so far. Only one of the compounds tested, 2-oxoadipinate, was able to support hydr…
Coping with Oxygen
2010
Sometime before 2.7 BYA, a new and biologically toxic substance began to appear in the environment. Biologically produced dioxygen, O2, probably first began to accumulate in small pools or layers above cyanobacterial mats. These photosynthesizers must have already developed ways to at least partially deal with dioxygen and, with greater difficulty, the reactive oxygen species (ROS) derived from it (see Chap. 1 and below). But for primitive anaerobes in the vicinity, these new substances must have been especially toxic. Nevertheless, it is clear that they evolved ways to cope with the new threats. One way was to simply avoid dioxygen altogether.
Kinetic and functional characterization of a membrane-bound NAD(P)H dehydrogenase located in the chloroplasts of Pleurochloris meiringensis (Xanthoph…
1996
Using isolated chloroplasts or purified thylakoids from photoautotrophically grown cells of the chromophytic alga Pleurochloris meiringensis (Xanthophyceae) we were able to demonstrate a membrane bound NAD(P)H dehydrogenase activity. NAD(P)H oxidation was detectable with menadione, coenzyme Q0, decylplastoquinone and decylubiquinone as acceptors in an in vitro assay. K m-values for both pyridine nucleotides were in the μmolar range (K m[NADH]=9.8 μM, K m[NADPH]=3.2 μM calculated according to Lineweaver-Burk). NADH oxidation was optimal at pH 9 while pH dependence of NADPH oxidation showed a main peak at 9.8 and a smaller optimum at pH 7.5-8. NADH oxidation could be completely inhibited with…
Role of hexagonal structure-forming lipids in diadinoxanthin and violaxanthin solubilization and de-epoxidation
2005
In this study, we have examined the influence of different lipids on the solubility of the xanthophyll cycle pigments diadinoxanthin (Ddx) and violaxanthin (Vx) and on the efficiency of Ddx and Vx de-epoxidation by the enzymes Vx de-epoxidase (VDE) from wheat and Ddx de-epoxidase (DDE) from the diatom Cyclotella meneghiniana, respectively. Our results show that the lipids MGDG and PE are able to solubilize both xanthophyll cycle pigments in an aqueous medium. Substrate solubilization is essential for de-epoxidase activity, because in the absence of MGDG or PE Ddx and Vx are present in an aggregated form, with limited accessibility for DDE and VDE. Our results also show that the hexagonal st…
Evidence for an intra- and extraplastidic pre-chorismate pathway.
1982
Pea plants grown under different conditions of cultivation, and eight different plant species with variegated leaves were used to study the intracellular localization of shikimate oxidoreductase (EC 1.1.1.25), the marker enzyme of the pre-chorismate pathway. The two series of experiments indicated an intra-and an extraplastidic compartimentalization of the enzyme, and both enzyme activities are regulated differentially. While the extraplastidic activity is permanently demonstrable, the intraplastidic activity is subject to the plants' developmental state and also depends on both illumination and fertilization.