S-adenosylhomocysteinase from mouse liver. Catalytic properties at cellular enzyme level.
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منابع مشابه
S-Adenosylhomocysteinase from mouse liver. Inactivation of the enzyme in the presence of metabolites.
1. S-Adenosylhomocysteinase (S-adenosylhomocysteine hydrolase, EC 3.3.1.1) was slowly inactivated in the presence of adenine and adenine nucleotides (Ueland & Saebø, 1979b). 2. The enzyme was stabilized by 2-mercaptoethanol and dithiothreitol, and was slowly inactivated at 37 degrees C in the absence of reducing agents and rapidly inactivated in the presence of 5,5'-dithiobis-(2-nitrobenzoic ac...
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Cyclic AMP-binding proteins not associated with protein kinase activity have been described in various tissues [l-7 1. Most of these proteins have been shown to bind adenosine [3,6,7]. We have purified to apparent homogeneity a cyclic AMP adenosine-binding protein from mouse liver 273. The molecular properties of this protein and its interaction with adenosine, adenine and adenine nucleotides h...
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Rat liver S-adenosylhomocysteinase (EC 3.3.1.1) is inactivated by phenylglyoxal following pseudo-first order kinetics. The dependence of the apparent first order rate constant for inactivation on the phenylglyoxal concentration shows that the inactivation is second order in reagent. This fact together with the reversibility of inactivation upon removal of excess reagent and the lack of reaction...
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Selenophosphate synthetase, the product of the selD gene, produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide. Isolation of the enzyme and characterization of some of its physical and catalytic properties are described. Magnesium ion and a monovalent cation, K+, NH4+, or Rb+, are required for catalytic activity. Polyphosphates and other common nu...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43890-8