Collect. Czech. Chem. Commun. 1983, 48, 2701-2708

S-adenosyl-L-homocysteine hydrolase from mouse leukemic cells: Isolation and properties

Aleš Merta, Ivan Votruba, Jiří Veselý and Antonín Holý

Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6


S-Adenosyl-L-homocysteine hydrolase from mouse leukemic cells L1210 was purified to evident homogeneity with no concomitant enzymatic activities. The isoelectric point of the enzyme is 5.65 and the optimum temperatures for the synthesis and hydrolysis are 52 °C and 47 °C, respectively. The respective KM values for adenosine and S-adenosyl-L-homocysteine (SAH) are 3.8 and 4.4 μmol l-1. The optimum pH value for the synthesis of SAH is 6.95-7.20 and for the hydrolysis 7.15-7.80. The enzyme is competitively inhibited by 9-(S)-(2,3-dihydroxypropyl)adenine and inactivated with both enantiomers of eritadenine and 3-(adenin-9-yl)-2-hydroxypropanoic acid.