Anti-SAHH antibody [EPR9261]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

S-Adenosylhomocysteine hydrolase also known as SAHH plays a critical mechanical role in cellular metabolism. It catalyzes the reversible hydrolysis of S-adenosylhomocysteine (SAH) to homocysteine and adenosine. This enzyme approximately 48 kDa in mass is ubiquitously expressed in most tissues highlighting its universal importance in biological systems. SAHH maintains the cellular methylation balance by regulating the concentrations of SAH a byproduct of methylation reactions.

Biological function summary

S-Adenosylhomocysteine hydrolase acts as an important player in the methylation processes within the cell. By breaking down SAH it ensures proper methylation of DNA proteins and lipids through the recycling of homocysteine and adenosine. SAHH operates as a homotetramer forming a complex essential for its enzymatic function. The balance maintained by SAHH in cellular methylation allows for proper gene expression and signal transduction within various cellular processes.

Pathways

S-Adenosylhomocysteine hydrolase plays an essential role in the methionine cycle and one-carbon metabolism pathways. These pathways are interconnected with the folate cycle important for nucleotide synthesis and cellular methylation. SAHH works with enzymes like methionine synthase and adenosylmethionine linking it to regulation of homocysteine levels. These interconnections are fundamental for maintaining cellular function and homeostasis.

Associated diseases and disorders

S-Adenosylhomocysteine hydrolase dysregulation can have significant implications. Hyperhomocysteinemia a condition characterized by high levels of homocysteine in the blood often results from SAHH dysfunction leading to cardiovascular diseases. Additionally aberrant SAHH activity connects to certain types of cancer as altered methylation patterns can disrupt normal cell proliferation. The interplay of SAHH with other proteins such as methylenetetrahydrofolate reductase (MTHFR) illustrates the complex network within which this enzyme operates affecting disease outcomes.