Results 151 to 160 of about 3,470 (173)
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Inactivation of rat liver S-adenosylhomocysteinase by iodoacetamide
Biochemistry, 1982S-Adenosylhomocysteine (EC 3.3.1.1) from rat liver is inactivated by iodoacetamide following pseudo-first-order reaction kinetics. The apparent first-order rate constant for inactivation is proportional to the concentration of the modifier, and a value of 7.55 M-1 min-1 is obtained for the second-order rate constant at pH 9.06 and 25 degrees C.
T, Gomi, M, Fujioka
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Cyclic AMP-adenosine binding protein/S-adenosylhomocysteinase from mouse liver
Biochimica et Biophysica Acta (BBA) - General Subjects, 19791. Adenosine bound to the cyclic AMP-adenosine binding protein/S-adenosylhomocysteinase from mouse liver was partly converted to a product which was identified as adenine in four chromatographic systems. Ribose was formed in equivalent amounts. 2. The time course of the reaction was characterized by an initial burst phase lasting for less than one ...
Per Magne Ueland, John Saebø
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Adenosylhomocysteinase from yellow lupine
1987Publisher Summary This chapter discusses the adenosylhomocysteinase from yellow lupine. Adenosylhomocysteinase seems to occur in all eukaryotes and was recently demonstrated in some bacteria. Yellow lupine seeds are suitable for preparation of homogeneous enzyme.
A, Guranowski, H, Jakubowski
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Rat liver S-adenosylhomocysteinase. Spectrophotometric study of coenzyme binding
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989Rat liver S-adenosylhomocysteinase, a homotetramer, was resolved by treatment with acid ammonium sulfate into apoenzyme and NAD. The apoenzyme thus prepared retained a tetrameric structure but differed in the mobility on nondenaturing polyacrylamide gel electrophoresis. The inactive apoenzyme was reactivated upon incubation with NAD. The restoration of
T, Gomi, Y, Takata, M, Fujioka
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Journal of Microbiology, 2020
Hepatitis C virus (HCV) life cycle is highly dependent on cellular proteins for viral propagation. In order to identify the cellular factors involved in HCV propagation, we previously performed a protein microarray assay using the HCV nonstructural 5A (NS5A) protein as a probe.
Yun-Sook, Lim +5 more
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Hepatitis C virus (HCV) life cycle is highly dependent on cellular proteins for viral propagation. In order to identify the cellular factors involved in HCV propagation, we previously performed a protein microarray assay using the HCV nonstructural 5A (NS5A) protein as a probe.
Yun-Sook, Lim +5 more
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Biology of Reproduction, 2023
Abstract Adenosylhomocysteinase (AHCY), a key enzyme in the methionine cycle, is essential for the development of embryos and the maintenance of mouse embryonic stem cells (mESCs). However, the precise underlying mechanism of Ahcy in regulating pluripotency remains unclear.
Qi, Jiang +8 more
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Abstract Adenosylhomocysteinase (AHCY), a key enzyme in the methionine cycle, is essential for the development of embryos and the maintenance of mouse embryonic stem cells (mESCs). However, the precise underlying mechanism of Ahcy in regulating pluripotency remains unclear.
Qi, Jiang +8 more
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5'-[p-(Fluorosulfonyl)benzoyl]adenosine-mediated inactivation of S-adenosylhomocysteinase
Biochemistry, 1984Rat liver S-adenosylhomocysteinase (EC 3.3.1.1) is inactivated by 5'-[p-(fluorosulfonyl)benzoyl]adenosine following pseudo-first-order kinetics. A plot of the apparent first-order rate constant for inactivation vs. the 5'-[p-(fluorosulfonyl)benzoyl]adenosine concentration exhibits a hyperbolic curve indicative of the formation of a reversible enzyme ...
Y, Takata, M, Fujioka
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
The spectral changes observed on interaction of S-adenosylhomocysteinase with adenine and cordycepin are approximated by the addition of dimethylsulfoxide to the aqueous solutions of these compounds, but not by protonation of the compounds. Although adenosine when bound to the enzyme undergoes partial reactions, it gives a spectral change similar to ...
T, Gomi, M, Fujioka
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The spectral changes observed on interaction of S-adenosylhomocysteinase with adenine and cordycepin are approximated by the addition of dimethylsulfoxide to the aqueous solutions of these compounds, but not by protonation of the compounds. Although adenosine when bound to the enzyme undergoes partial reactions, it gives a spectral change similar to ...
T, Gomi, M, Fujioka
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Biochemistry, 1982
S-Adenosylhomocysteinase (SAHase), a tetrameric enzyme, is inactivated by 2'-deoxyadenosine (2'dAdo) in a time-dependent process [Hirshfield, M. S. (1979) J. Biol. Chem. 254, 22-25]. It has been proposed that inactivation involves oxidation of 2'dAdo at C-3' by enzyme-bound nicotinamide adenine dinucleotide (NAD), subsequent proton abstraction at C-2',
R H, Abeles, S, Fish, B, Lapinskas
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S-Adenosylhomocysteinase (SAHase), a tetrameric enzyme, is inactivated by 2'-deoxyadenosine (2'dAdo) in a time-dependent process [Hirshfield, M. S. (1979) J. Biol. Chem. 254, 22-25]. It has been proposed that inactivation involves oxidation of 2'dAdo at C-3' by enzyme-bound nicotinamide adenine dinucleotide (NAD), subsequent proton abstraction at C-2',
R H, Abeles, S, Fish, B, Lapinskas
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Biochemistry, 1981
Plant (Lupinus luteus) S-adenosylhomocysteinase, an alpha 2 dimer, forms a 1:2 enzyme-adenosine complex. The binding sites for adenosine are not equivalent. Binding of the first molecule of adenosine is fast (k greater than 7 x 10(5) M-1 s-1), whereas the second molecule of adenosine binds in a slow process with a half-life of 5 min. Adenosine in the 1:
H, Jakubowski, A, Guranowski
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Plant (Lupinus luteus) S-adenosylhomocysteinase, an alpha 2 dimer, forms a 1:2 enzyme-adenosine complex. The binding sites for adenosine are not equivalent. Binding of the first molecule of adenosine is fast (k greater than 7 x 10(5) M-1 s-1), whereas the second molecule of adenosine binds in a slow process with a half-life of 5 min. Adenosine in the 1:
H, Jakubowski, A, Guranowski
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