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In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different K M values), or are regulated differently.
In experiential studies, isoenzymes, which are distinct forms of alkaline phosphatase generated by these tumors, can raise the total volume of alkaline phosphatase in the blood. The Regan isoenzyme [clarification needed] [13] is one of the best studied [clarification needed] of these isoenzymes that is linked to several human cancers. Basically ...
Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD + to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle.
Download QR code; Print/export Download as PDF; Printable version; In other projects ... From Wikipedia, the free encyclopedia. Redirect page. Redirect to: Isozyme ...
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The most significant difference between the isoenzymes, which allows for selective inhibition, is the substitution of isoleucine at position 523 in COX-1 with valine in COX-2. The smaller Val 523 residue in COX-2 allows access to a hydrophobic side-pocket in the enzyme (which Ile 523 sterically hinders).
Hence, this isoenzyme is an important regulator of glycolysis and additional functions in other novel roles that have recently emerged. Recent evidence indicates that intervening in the complex regulatory network of PKM2 has severe consequences on tumor cell proliferation, indicating the potential of this enzyme as a target for tumor therapy.