Synthesis of 3-arsonopyruvate and its interaction with phosphoenolpyruvate mutase.
3-Arsonopyruvate was prepared in four steps from glycine. The arsenic-carbon bond was formed by a Meyer reaction between alkaline arsenite and 2-bromo-3-hydroxy-2-(hydroxymethyl)propionic acid; the 3-arsono-2-hydroxy-2-(hydroxymethyl) propionic acid formed was oxidized with periodate to give 3-arsonopyruvate. This proves to be an alternative substrate for phosphoenolpyruvate mutase, giving pyruvate, which was assayed using lactate dehydrogenase. The K(m) is 20 microM, similar to that observed for the natural substrate phosphonopyruvate (17 microM), whereas the kcat. of 0.01 s-1 was much lower than that for phosphonopyruvate (58 s-1). Arsonopyruvate competitively inhibited the action of the mutase on phosphonopyruvate.
Chawla
S
S
Department of Biochemistry, University of Cambridge, U.K.
Mutenda
E K
EK
Dixon
H B
HB
Freeman
S
S
Smith
A W
AW
D001152:Arsenicals / Q000138:chemical synthesis* / Q000378:metabolism*; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D017875:Phosphotransferases (Phosphomutases) / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000378:metabolism; D011773:Pyruvates / Q000138:chemical synthesis* / Q000378:metabolism*; D013379:Substrate Specificity
C102551:3-arsonopyruvate; D001152:Arsenicals; D004791:Enzyme Inhibitors; D011773:Pyruvates; D007770:L-Lactate Dehydrogenase; D011770:Pyruvate Kinase; D017875:Phosphotransferases (Phosphomutases); C057167:phosphoenolpyruvate mutase