Carnosine-cleaving Enzyme

Carnosine-cleaving enzymes primarily catalyze the breakdown of carnosine, facilitating its conversion into beta-alanine and histidine. This process is essential for maintaining cellular homeostasis and regulating the levels of these amino acids in tissues. The main family members include carnosinase 1 (CN1) (CNDP1) and carnosinase 2 (CN2) (CNDP2). CN1 is found in serum and brain tissue and specifically degrades both carnosine and homocarnosine, while CN2 is a cytosolic enzyme with broader substrate specificity but does not hydrolyze homocarnosine^[1].
br/> Alterations of serum CN1 activity and dyshomeostasis of the main carnosinase substrate (carnosine) is associated with several pathological conditions, such as neurological disorders, chronic diseases and cancer. The dyshomeostasis of carnosinase expression and activity cause several physiological dysfunctions and diseases, such as diabetes, ischemia, neurological diseases, wound healing, ocular diseases, etc^[1].

References:

[1]. Bellia F, et al. Carnosinases, their substrates and diseases. Molecules. 2014 Feb 21;19(2):2299-329. [Content Brief]

Carnosine-cleaving Enzyme Inhibitor (1)

Carnosine-cleaving Enzyme Related Products (1):

Cat. No.	Product Name	Effect	Purity	Chemical Structure

HY-112431

Carnostatine	Inhibitor
Carnostatine (SAN9812) is a potent and selective carnosinase 1 (CN1) inhibitor with a K_i of 11 nM for human recombinant CN1. Carnostatine (SAN9812) can be used for the treatment of diabetic nephropathy (DN).

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