Ontology highlight
ABSTRACT:
SUBMITTER: Wang Y
PROVIDER: S-EPMC4223336 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Wang Yun Y Kavran Jennifer M JM Chen Zan Z Karukurichi Kannan R KR Leahy Daniel J DJ Cole Philip A PA
The Journal of biological chemistry 20140923 45
S-Adenosylhomocysteine hydrolase (SAHH) is an NAD(+)-dependent tetrameric enzyme that catalyzes the breakdown of S-adenosylhomocysteine to adenosine and homocysteine and is important in cell growth and the regulation of gene expression. Loss of SAHH function can result in global inhibition of cellular methyltransferase enzymes because of high levels of S-adenosylhomocysteine. Prior proteomics studies have identified two SAHH acetylation sites at Lys(401) and Lys(408) but the impact of these post ...[more]