PMID: 8589053Jan 1, 1995Paper

In vitro oxidative decarboxylation of L-2-hydroxy-4-methylthiobutanoic acid by L-2-hydroxy acid oxidase A from chicken liver

Biochimie
A Ferjancic-BiaginiA Puigserver

Abstract

The first step in the set of reactions responsible for the biological utilization of L-2-hydroxy-4-methylthiobutanoic acid, the methionine hydroxy analogue, in protein synthesis was investigated in vitro using pure L-2-hydroxy acid oxidase A from chicken liver. The reaction yielded no more than 20% of the corresponding alpha-keto acid, the well-known intermediate in methionine metabolism, and as much as 80% of the subsequent decarboxylation product, 3-methylthiopropionate, suggesting that L-2-hydroxy-4-methylthiobutanoic acid cannot be completely converted into methionine in vivo. It was therefore concluded that chicken liver L-2-hydroxy acid oxidase, a peroxisomal enzyme requiring flavin mononucleotide as a coenzyme, also has an oxidative decarboxylation activity in vitro, which was found to be NADH-dependent. The mechanism possibly underlying the successive conversion of the methionine hydroxy analogue into alpha-keto acid and 3-methylthiopropionate by this NADH:flavin oxidoreductase-decarboxylase activity is described.

References

Mar 16, 1976·European Journal of Biochemistry·J A Duley, R S Holmes
Mar 10, 1971·Biochimica Et Biophysica Acta·M Schuman, V Massey
Nov 1, 1980·Poultry Science·A C Christensen, J O Anderson
Dec 16, 1980·Biochemical and Biophysical Research Communications·J L Dixon, N J Benevenga
May 1, 1965·Poultry Science·R S GORDON, I W SIZER

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Citations

Oct 20, 2009·Nutrition Research Reviews·Caroline Bauchart-ThevretDouglas G Burrin
Mar 20, 2018·EFSA Journal·UNKNOWN EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP)Robert John Wallace

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