Human placental S-adenosylhomocysteine (AdoHcy) hydrolase (EC 3.3.1.1) was inactivated
by 5′,5-dithiobis(2-nitrobenzoic acid) following pseudo-first-order kinetics. Modification of …

(1'R,2'S,3')-9-(2',3'-Dihydroxycyclopentan-1'-yl)adenine (DHCaA), (1'R,2'S,3'R)-9-(2',3'-dihydroxycyclopentan-1'-yl)-3-deazaadenine
(3-deaza-DHCaA), (4'R)-4'-methyl-DHCaA, and (4'R)…

S-Adenosylhomocysteine (AdoHcy) hydrolase catalyzes the conversion of AdoHcy to adenosine
(Ado) and homocysteine (Hcy), as well as the reverse reaction, through a mechanism …

Two synthetic analogues of aristeromycin, which were shown in a separate study to be
inhibitors of S-adenosylhomocysteine hydrolase and devoid of substrate activity with adenosine …

(1′R,2′S,3′R)-9-(2′,3′-Dihydroxycycloperrt-4′-en-1′-yl)-adenine (DHCeA) and -3-deazaadenine
(3-deaza-DHCeA), which are potent inhibitors of S-adenosylho-mocysteine (…

… at 45 sites in conserved regions results in the loss of all activities in some cases; in some
other cases, one activity is retained more than the other activities (CM Tzeng, D Ault-Riché & A …

… Results from this study support a previously described model (DB Ault-Riché, CS Yuan, and
RT Borchardt (1994) J. Biol. Chem., 269,31,472-31,478) in which the formation of the active …

… binding affinity but retains the wild type’s tetrameric structure, while the corresponding mutant
of Hs-SAHH (HsK426A) loses both cofactor affinity and tetrameric structure [Ault-Riche, DB…