Abstract
Soluble adenosine-binding proteins were first described by Yuh and Tao in rabbit erythrocytes [1], and similar proteins were later isolated from various eukaryotes [2–8]. The physiological role of these binding proteins for adenosine (Ado) remained obscure until Hershfield [9] and Hershfield and Kredich [10] demonstrated that such proteins from human placenta, spleen, and lymphoblasts were identical to S-adenosylhomocysteine (AdoHcy) hydrolase (EC: 3.3.1.1), the enzyme responsible for the metabolic degradation of the endogenous transmethylase inhibitor, AdoHcy [11]. This finding has been confirmed by others [12–14]. This chapter is a brief review of the properties of AdoHcy hydrolase, with emphasis on the interaction of the enzyme with Ado.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
