نتایج جستجو برای: dismutation

تعداد نتایج: 364  

Journal: :The FEBS journal 2005
Blanaid Mee Dermot Kelleher Jesus Frias Renee Malone Keith F Tipton Gary T M Henehan Henry J Windle

Cinnamyl alcohol dehydrogenases (CAD; 1.1.1.195) catalyse the reversible conversion of p-hydroxycinnamaldehydes to their corresponding alcohols, leading to the biosynthesis of lignin in plants. Outside of plants their role is less defined. The gene for cinnamyl alcohol dehydrogenase from Helicobacter pylori (HpCAD) was cloned in Escherichia coli and the recombinant enzyme characterized for subs...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1997
A L Pinto H W Hellinga J P Caradonna

The rational protein design algorithm DEZYMER was used to introduce the active site of nonheme iron superoxide dismutase (SOD) into the hydrophobic interior of the host protein, Escherichia coli thioredoxin (Trx), a protein that does not naturally contain a transition metal-binding site. Reconstitution of the designed protein, Trx-SOD, showed the incorporation of one high-affinity metal-binding...

Journal: :The Journal of biological chemistry 1969
R W Burg E E Snell

Pyridoxal dehydrogenase is specific for DPNf and does not oxidize benzaldehyde, acetaldehyde, salicylaldehyde, or Sdeoxypyridoxal. In the presence of the latter compound, oxidation of pyridoxal is stimulated, apparently because of the occurrence of the dismutation reaction (ii). Z-Demethyl-Z-ethylpyridoxal is dehydrogenated at the same rate as pyridoxal. At high substrate concentrations the pH

2003
CARL M. LYMAN

Pyruvic acid is one of the most reactive substances among those of importance in cellular metabolism. When carbohydrate is split during fermentation, pyruvic acid is the main end-product of the resulting series of phosphorylated oxidation-reductions. It thus becomes the immediate source for the formation of both lactic acid and alcohol. Pyruvic acid is decarboxylated by yeast; it may react with...

Journal: :Methods in enzymology 2002
Vincent Nivière Murielle Lombard

Superoxide radical (O2.-) is the univalent reduction product of molecular oxygen and belongs to the group of the so-called toxic oxygen derivatives. For years the only enzymatic system known to catalyze the elimination of superoxide was the superoxide dismutase (SOD), which catalyzes dismutation of superoxide radical anions to hydrogen peroxide and molecular oxygen

Journal: :Plant physiology 1994
A S Akkapeddi D I Shin M T Stanek D F Karnosky G K Podila

aerobic and many anaerobic are Table 1. Characteristics of the chloroplastic Cu/Zn-SOD from aspen subiect to oxidative stress resulting from the deleterious efv fects of reduced oxygen species. SOD has been identified as a key enzyme in protecting the cells from oxidative damage by catalyzing the dismutation of superoxide radicals (O2-) to hydrogen peroxide and molecular oxygen (Fridovich, 1986...

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