Pyruvate kinase catalyzed phosphorylation of 3-nitro-2-hydroxypropionate by ATP and concomitant inactivation of the enzyme.
Pyruvate kinase catalyzes the phosphorylation of 3-nitro-2-hydroxypropionate by ATP. The product (3-nitro-2-phosphopropionate) decomposes nonenzymatically and inactivates the enzyme. The inactivation process is irreversible and the enzyme is completely protected against inactivation by mercaptoethanol or the competitive inhibitor oxalate. The Km for 3-nitro-2-hydroxypropionate (DL) is 40 mM and kcat = 5 s-1 at pH 8.6. In terms of kcat/km, 3-nitro-2-hydroxypropionate is a fourfold better substrate than glycolate.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D007773:Lactates / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D010766:Phosphorylation; D011770:Pyruvate Kinase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011817:Rabbits
C024846:3-nitro-2-hydroxypropionate; D007773:Lactates; D000255:Adenosine Triphosphate; D011770:Pyruvate Kinase