Adenosylhomocysteine nucleosidase () is an enzyme that catalyzes three related hydrolysis reactions. In one, bacterial enzyme characterised from Escherichia coli was shown to convert S-adenosyl-L-homocysteine to S-ribosylhomocysteine and adenine:
The second reaction catalysed by the enzyme converts 5'-deoxyadenosine to 5-deoxy-D-ribose and adenine:
Finally, the enzyme can convert 5′-methylthioadenosine to S-methyl-5-thio-D-ribose and adenine:
The enzyme has been studied because its inhibition might lead to the development of novel antibiotics.
This enzyme is a hydrolase, specifically a glycosylase that hydrolyses N-glycosyl compounds. The systematic name of this enzyme class is S-adenosyl-L-homocysteine homocysteinylribohydrolase. Other names in common use include S-adenosylhomocysteine hydrolase (ambiguous), S-adenosylhomocysteine nucleosidase, 5'-methyladenosine nucleosidase, S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase, and AdoHcy/MTA nucleosidase.
Structural studies As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References