نتایج جستجو برای: oxidoreductases

تعداد نتایج: 1064  

Journal: :Current protein & peptide science 2010
Enrique Herrero Gemma Bellí Celia Casa

Glutaredoxins are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bonds and deglutathionylate mixed disulfides between glutathione and cysteine protein residues. They...

Journal: :Protein science : a publication of the Protein Society 2001
J S Fetrow N Siew J A Di Gennaro M Martinez-Yamout H J Dyson J Skolnick

A function annotation method using the sequence-to-structure-to-function paradigm is applied to the identification of all disulfide oxidoreductases in the Saccharomyces cerevisiae genome. The method identifies 27 sequences as potential disulfide oxidoreductases. All previously known thioredoxins, glutaredoxins, and disulfide isomerases are correctly identified. Three of the 27 predictions are p...

Journal: :Plant physiology 1992
T Hashimoto K Nakajima G Ongena Y Yamada

Tropinone is an alkamine intermediate at the branch point of biosynthetic pathways leading to various tropane alkaloids. Two stereospecifically distinct NADPH-dependent oxidoreductases, TR-I and TR-II, which, respectively, reduce tropinone to 3alpha-hydroxytropane (tropine) and 3beta-hydroxytropane (psi-tropine), were detected mainly in the root of tropane alkaloid-producing plants but not in n...

2014
Ali Ryan Elise Kaplan Jean-Christophe Nebel Elena Polycarpou Vincenzo Crescente Edward Lowe Gail M. Preston Edith Sim

Water soluble quinones are a group of cytotoxic anti-bacterial compounds that are secreted by many species of plants, invertebrates, fungi and bacteria. Studies in a number of species have shown the importance of quinones in response to pathogenic bacteria of the genus Pseudomonas. Two electron reduction is an important mechanism of quinone detoxification as it generates the less toxic quinol. ...

Journal: :The EMBO journal 2012
Emily M Lynes Michael Bui Megan C Yap Matthew D Benson Bobbie Schneider Lars Ellgaard Luc G Berthiaume Thomas Simmen

The mitochondria-associated membrane (MAM) is a domain of the endoplasmic reticulum (ER) that mediates the exchange of ions, lipids and metabolites between the ER and mitochondria. ER chaperones and oxidoreductases are critical components of the MAM. However, the localization motifs and mechanisms for most MAM proteins have remained elusive. Using two highly related ER oxidoreductases as a mode...

Journal: :Journal of cell science 2009
Catherine E Jessop Rachel H Watkins Jennifer J Simmons Mohammed Tasab Neil J Bulleid

At least 17 members of the protein disulphide isomerase (PDI) family of oxidoreductases are present in the endoplasmic reticulum (ER) of mammalian cells. They are thought to catalyse disulphide formation to aid folding or to regulate protein function; however, little is known about their individual functions. Here, we show that some proteins that enter the ER are clients for single oxidoreducta...

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2001
M Okuda N Inoue H Azumi T Seno Y Sumi Hirata Ki S Kawashima Y Hayashi H Itoh J Yodoi M Yokoyama

Oxidative stress is considered an important factor in atherogenesis. Mammalian cells have a complex network of antioxidants such as catalase, superoxide dismutase, and glutathione peroxidase. However, the mechanisms that regulate the cellular redox state in the vessel wall remain unclear. Recent study has shown that thioredoxin, a thiol-disulfide oxidoreductase, is expressed in atherosclerotic ...

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