PMID: 6983366Oct 26, 1982Paper

S-Adenosylhomocysteinase: mechanism of inactivation by 2'-deoxyadenosine and interaction with other nucleosides

Biochemistry
R H AbelesB Lapinskas

Abstract

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', and elimination of adenine. This results in irreversible formation of enzyme-bound NADH and of adenine (Ade) and inactivation [Abeles, R. H., TAshjian, A. H., Jr., & Fish, S (1980) Biochem. Biophys. Res. Commun. 95, 612-617]. It has now been established that upon inactivation of SAHase with deoxy[2'(R)-3H]adenosine, 3H2O is formed. This is consistent with the proposed mechanism and of 3H2O release shows that maximally two of the four subunits participate in the reaction that results in 3H2O release. Reaction of SAHase with 2'dAdo results in reduction of two of the enzyme-bound NAD molecules. However, all four NAD molecules can be reduced by NaBH4, but only two are reduced to C-4 NADH. When the enzyme is inactivated with adenine-labeled 2'dAdo, radioactivity corresponding to 0.5-1.0 mumol of 2'dAdo binds tightly per micromole of subunit. This radioactive material is not removed fr...Continue Reading

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