Characterization of human S-adenosyl-homocysteine hydrolase in vitro and identification of its potential inhibitors.

ABSTRACT: Human S-adenosyl-homocysteine hydrolase (SAHH, E.C.3.3.1.1) has been considered to be an attractive target for the design of medicines to treat human disease, because of its important role in regulating biological methylation reactions to catalyse the reversible hydrolysis of S-adenosylhomocysteine (SAH) to adenosine (Ado) and l-homocysteine (Hcy). In this study, SAHH protein was successfully cloned and purified with optimized, Pichia pastoris (P. pastoris) expression system. The biological activity results revealed that, among the tested compounds screened by ChemMapper and SciFinder Scholar, 4-(3-hydroxyprop-1-en-1-yl)-2-methoxyphenol (coniferyl alcohol, CAS: 458-35-5, ZINC: 12359045) exhibited the highest inhibition against rSAHH (IC₅₀= 34 nM). Molecular docking studies showe

SUBMITTER: Hao W 

PROVIDER: S-EPMC6445193 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature