MACROD2: An Enzyme in The Metabolism of Adenosine Diphosphate

Target Name: MACROD2

NCBI ID: G140733

MACROD2

MACROD2: An Enzyme in The Metabolism of Adenosine Diphosphate

MACROD2 (ADP-ribose glycohydrolase MACROD2), also known as ADP-ribose synthase 2, is a protein that plays a crucial role in the metabolism of adenosine diphosphate (ADP) to ADP-ribose. Adenosine diphosphate is a key player in various cellular processes , including signaling, stress response, and energy metabolism. MACROD2 is a key enzyme that converts ADP-ribose, a simple sugar found in many foods, to its more potent derivative, ADP-ribose glycohydrolase (ARG), which can be used for various biotechnological applications.

MACROD2 is an essential enzyme that is involved in the catabolism of ARG, which is a key substrate for the enzyme AP-120, also known as Exonuclease T or XNU. ARG is a nucleotide sugar that has been shown to have a variety of biochemical and physiological functions, including participating in various signaling pathways and playing a role in cellular stress response.

MACROD2 is a 21-kDa protein that is expressed in various tissues, including muscle, heart, liver, and kidney. It is primarily localized to the endoplasmic reticulum (ER) and is considered a cytoplasmic protein. MACROD2 is a monomer that consists of a catalytic domain and a cytoplasmic tail. The catalytic domain is responsible for the catalytic activity of MACROD2, while the cytoplasmic tail is involved in protein stability and localization.

MACROD2 is regulated by various factors, including temperature, pH, and inhibitors. At physiological pH, MACROD2 has a catalytic activity of 200 pmol/L and a substrate specificity of ARG. The catalytic activity of MACROD2 can be enhanced by increasing the pH to 8.0 , and it is inhibited by inhibitors such as alkaline phosphatase (AP) and src-associated protein (SAP).

MACROD2 has been shown to have a variety of physiological functions. In addition to its role in the catabolism of ARG, MACROD2 is also involved in the synthesis of other sugar molecules, including glucose-6-phosphate (G6P) and fructose-1,6 -bipolar. These functions are critical for maintaining cellular energy metabolism and metabolism, respectively.

MACROD2 is also a potential drug target and biomarker. Several studies have suggested that MACROD2 may be a useful target for the treatment of various diseases, including cancer, cardiovascular disease, and neurodegenerative diseases. The ability of MACROD2 to convert ARG to ADP-ribose suggests that it may be a useful target for the treatment of diseases that are characterized by the accumulation of ARG in cells.

In addition to its potential therapeutic applications, MACROD2 is also a useful biomarker for several diseases. The increased levels of MACROD2 expression that occur in response to certain diseases, such as cancer, have been shown to be associated with the development of those diseases. Additionally , the decreased levels of MACROD2 expression that occur in response to certain therapeutic interventions, such as chemotherapy, have been shown to be associated with improved patient outcomes.

Conclusion

MACROD2 is an essential enzyme that plays a crucial role in the metabolism of ADP-ribose to ARG. Its catalytic activity is enhanced by increasing the pH to 8.0 and is inhibited by AP and SAP. MACROD2 is also involved in the synthesis of other sugar molecules and has been shown to have a variety of physiological functions, including its role in maintaining cellular energy metabolism. In addition to its potential therapeutic applications, MACROD2 is also a useful biomarker for several diseases. Further research is needed to fully understand the role of MACROD2 in

Protein Name: Mono-ADP Ribosylhydrolase 2

Functions: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety (PubMed:23474714, PubMed:23474712). Inactive towards proteins bearing poly-ADP-ribose (PubMed:23474714, PubMed:23474712). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21257746)

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