S-adenosylhomocysteine hydrolase from rat liver.
The kinetic constants for the reversible adenosylhomocysteine hydrolase from rat liver have been determined. The Km values of the enzyme for S-adenosylhomocysteine, adenosine, and l-homocysteine were 12.3 micro M, 0.94 micro M, and 164 micro M, respectively. Under the specified conditions the Vmax for the synthetic reaction was 6.2 mumol/min per milligram, while the Vmax for the hydrolytic reaction was 0.72 mumol/min per milligram. l-Homocysteine acted as a mixed-type inhibitor of the hydrolytic reaction. Adenosine, a competitive inhibitor of both the synthetic and hydrolytic reactions (Ki = 1.2 +/- 0.2 micro M), was found to be a product of the reaction. In the absence of l-homocysteine about 0.8 nmol of adenosine was hydrolyzed to adenine and ribose per minute per milligram enzyme.
D000225:Adenine / Q000494:pharmacology; D000241:Adenosine / Q000378:metabolism; D043383:Adenosylhomocysteinase; D000818:Animals; D002846:Chromatography, Affinity; D006867:Hydrolases / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D012435:S-Adenosylhomocysteine / Q000378:metabolism
D012435:S-Adenosylhomocysteine; D006867:Hydrolases; D043383:Adenosylhomocysteinase; D000225:Adenine; D000241:Adenosine