Aldolase-catalyzed diketone phosphate formation from oxoaldehydes. NMR studies and metabolic significance. |
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Authors: | C Rae W A Bubb P W Kuchel |
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Institution: | Department of Biochemistry, University of Sydney, New South Wales, Australia. |
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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. |
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