Results 141 to 150 of about 14,441 (168)

S-Adenosylhomocysteine hydrolase activity in human myocardium

Cardiovascular Research, 1992
Measurement of S-adenosylhomocysteine (SAH) accumulation in the heart reflects the concentration of free cytosolic adenosine and is thus a sensitive indicator of regional myocardial ischaemia. To evaluate the possibility of applying this method in combination with 11C-SAH positron emission tomography (PET) to patients with ischaemic heart disease the ...
M M, Borst, A, Deussen, J, Schrader
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Inactivation of S-adenosylhomocysteine hydrolase by nucleosides

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxyadenosine inactivates as potently as 9-beta-D-arabinofuranosyladenine (Ara-A).
I Y, Kim, C Y, Zhang, G L, Cantoni, J A, Montgomery, P K, Chiang   +4 more
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Structure and Function of S-Adenosylhomocysteine Hydrolase

Cell Biochemistry and Biophysics, 2000
In mammals, S-adenosylhomocysteine hydrolase (AdoHcyase) is the only known enzyme to catalyze the breakdown of S-adenosylhomocysteine (AdoHcy) to homocysteine and adenosine. AdoHcy is the product of all adenosylmethionine (AdoMet)-dependent biological transmethylations.
M A, Turner, X, Yang, D, Yin, K, Kuczera, R T, Borchardt, P L, Howell   +5 more
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Enzymatic synthesis of S-adenosylhomocysteine: immobilization of recombinant S-adenosylhomocysteine hydrolase from Corynebacterium glutamicum (ATCC 13032)

Applied Microbiology and Biotechnology, 2011
Recombinant S-adenosylhomocysteine hydrolase from Corynebacterium glutamicum (CgSAHase) was covalently bound to Eupergit® C. The maximum yield of bound protein was 91% and the catalytic efficiency was 96.9%. When the kinetic results for the immobilized enzyme were compared with those for the soluble enzyme, no decrease in the catalytic efficiency of ...
J D, Lozada-Ramírez, A, Sánchez-Ferrer, F, García-Carmona   +2 more
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A colorimetric assay for S-adenosylhomocysteine hydrolase

Journal of Biochemical and Biophysical Methods, 2006
A colorimetric method for S-adenosyl-L-homocysteine hydrolase (SAHase) which uses S-adenosyl-L-homocysteine (SAH) as substrate is described. This method involves the hydrolytic conversion of SAH into adenosine (ADO) and L-homocysteine (HCY). The formation of HCY is quantified using Ellman's reagent and spectrophotometrical measured at 412 nm.
J D, Lozada-Ramírez, I, Martínez-Martínez, A, Sánchez-Ferrer, F, García-Carmona   +3 more
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Microsomal phosphatidylethanolamine methyltransferase: Inhibition by S‐adenosylhomocysteine

Lipids, 1981
AbstractInhibition by S‐adenosylhomocysteine (AdoHcy) of the three reactions of phosphatidylethanolamine methyltransferase which catalyzes the production of phosphatidylcholine from phosphatidyl‐ethanolamine in guinea pig and rat liver microsomes has been evaluated. Five of the six methylation reactions in these two species exhibit greater affinity for
D R, Hoffman, J A, Haning, W E, Cornatzer   +2 more
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Influence of S-adenosylhomocysteine hydrolase inhibitors on S-adenosylhomocysteine and S-adenosylmethionine pool levels in L929 cells

Biochemical Pharmacology, 1990
S-Adenosylhomocysteine hydrolase has been recognized as the target enzyme for the antiviral activity of several carbocyclic and acyclic adenosine analogues. In a previous study [Cools M and De Clercq E, Biochem Pharmacol 38: 1061-1067, 1989], we found a close correlation between the antiviral activity of six adenosine analogues [S)-9-(2,3 ...
M, Cools, E, De Clercq
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S-Adenosylhomocysteine hydrolase deficiency

2008
S-Adenosylhomocysteine hydrolase (AdoHcy) deficiency is a disorder in methionine metabolism. The enzyme catalyzes the hydrolysis of S-adenosylhomocysteine to homocysteine and adenosine. Its deficiency in human was first reported in 2003. Since then few other patients have been identified.
Ćuk, Mario, Barić, Ivo, Vugrek, Oliver, Fumić, Ksenija   +3 more
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Binding of S-adenosylhomocysteine to hydroxyindole O-methyltransferase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Biochim Biophys Acta 1984 May 31;787(1 ) 1-7 (S-adenosyl-L-methionine:N-acetylserotonin O-methyltransferase, EC 2.1.1.4) purified from bovine pineal gland forms a complex with S-adenosylhomocysteine, one of the products of the reaction catalyzed by the enzyme. The binding of S-adenosylhomocysteine to the enzyme has been characterized by the use of S-[8-
R, Kuwano, Y, Takahashi
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Inhibition of indolethylamine-N-methyltransferase by S-Adenosylhomocysteine

Biochemical and Biophysical Research Communications, 1973
Abstract S -Adenosylhomocysteine (SAH) is a potent product inhibitor for indoleamine- N -methyltransferase (INMT) from rabbit lung. The kinetic studies showed that this inhibition was competitive with respect to S -adenosylmethionine (SAM) and noncompetitive with respect to N -methylserotonin (NMS). The K i value of 1.0 ×
R L, Lin, N, Narasimhachari, H E, Himwich   +2 more
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