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

Abstract

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 K_M 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.