Download Class 1 Oxidoreductases VII: EC 1.4 (Springer Handbook of by Antje Chang, Dietmar Schomburg, Ida Schomburg PDF

By Antje Chang, Dietmar Schomburg, Ida Schomburg

Springer guide of Enzymes offers facts on enzymes sufficiently good characterised. It deals concise and entire descriptions of a few 5,000 enzymes and their program components. info sheets are prepared of their EC-Number series and the volumes themselves are prepared based on enzyme periods. This new, moment variation displays huge growth in enzymology: many enzymes are newly categorized or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the homes of enzymes the place the series has been changed). the entire volume of fabric inside the instruction manual has greater than doubled in order that the full moment variation involves 39 volumes in addition to a Synonym Index. additionally, beginning in 2009, all newly categorised enzymes are taken care of in complement Volumes. Springer instruction manual of Enzymes is a perfect resource of data for researchers in biochemistry, biotechnology, natural and analytical chemistry, and nutrients sciences, in addition to for medicinal functions.

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Purification, molecular properties and metal ion activation of the enzymes from Lemna minor and Pisum sativum. Z. Naturforsch. , purification and comparative kinetic studies of the organ-specific multiple forms. Z. Naturforsch. : Purification and properties of the phospho and dephospho forms of yeast NAD-dependent glutamate dehydrogenase. J. Biol. : Characterization of Peptostreptococcus asaccharolyticus glutamate dehydrogenase purified by dye-ligand chromatography. J. Gen. : Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots.

13, 18> [7, 13]) [7, 13] P 2-oxopentanoate + NH3 + NADH S l-serine + H2 O + NAD+ <18> (<18> deamination at 29% the rate of lglutamate deamination [13]) (Reversibility: ? 5% the rate of deamination of l-glutamate [8]) (Reversibility: ? <16> [8]) [8] P ? : Glutamate dehydrogenase. The Enzymes, 3rd Ed. : An NAD-specific glutamate dehydrogenase from cyanobacteria. Identification and properties. : Glutamate dehydrogenase of lupin nodules: kinetics of the deamination reaction. Arch. Biochem. : Some properties of the NADspecific glutamate dehydrogenase from Crithidia fasciculata.

FEMS Microbiol. : Kinetic properties and the mechanism of activation of NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum. Biochem. Mol. Biol. , 38, 729-738. : A new class of glutamate dehydrogenases (GDH). J. Biol. : Properties of NAD-dependent glutamate dehydrogenase from the tylosin producer Streptomyces fradiae. Can. J. : Unusually stable NAD-specific glutamate dehydrogenase from the alkaliphile Amphibacillus xylanus. : Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents.

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