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- W1591643354 abstract "NMR spectroscopy showed fructose-1,6-bisphosphate aldolase from rabbit muscle accepts as substrates, in lieu of glyceraldehyde 3-phosphate, the oxoaldehydes methylglyoxal and phenylglyoxal but not hydroxymethylglyoxal. The enzyme catalyzed an aldol condensation between the oxoaldehyde and dihydroxyacetone phosphate to form a monophosphorylated diketone and was inactivated in the process. Circumvention of this reaction, by metabolism of oxoaldehydes to hydroxy acids, may be a metabolic role for the glyoxalase enzyme system. Transketolase and transaldolase were found not to accept oxoaldehydes as substrates in place of glyceraldehyde 3-phosphate." @default.
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- W1591643354 date "1992-05-01" @default.
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- W1591643354 title "Aldolase-catalyzed diketone phosphate formation from oxoaldehydes. NMR studies and metabolic significance." @default.
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- W1591643354 doi "https://doi.org/10.1016/s0021-9258(19)50149-1" @default.
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