The keto acid 2-oxo-4[methylthio]-butanoic acid (OMTB) is an intermedi
ate in the conversion of synthetic feed grade methionine sources to L-
methionine in vivo in poultry and other animals. Because methionine so
urces are utilized by the chick with considerably less than 100% effic
iency as sources of L-methionine, it is important tb determine what me
tabolic process may limit the utilization of these sources. Because OM
TB is converted to L-methionine by transamination, a study was conduct
ed to determine which amino acids might serve as nitrogen donors in th
e conversion of OMTB to L-methionine in the chicken. Dialyzed tissue h
omogenates, mitochondria, and cytosol from liver, kidney, intestine, a
nd skeletal muscle were incubated with OMTB and individual L-amino aci
ds (isoleucine, leucine, valine, glutamic acid, aspartic acid, alanine
, glutamine, asparagine, and phenylalanine) and the methionine that ac
cumulated was determined by ion exchange chromatography. Tissues diffe
red in the conversion of OMTB to methionine: kidney was most active, l
iver and intestinal mucosa were intermediate, and skeletal muscle had
lowest activity. All amino acids supported methionine Synthesis. Branc
hed-chain amino acids and glutamic acid were the most effective substr
ates in tissue cytosols except in intestinal mucosa, in which asparagi
ne was also effective. The preferred substrates in mitochondria were g
lutamate in liver mitochondria, isoleucine and alanine in kidney mitoc
hondria, and branched-chain amino acids and glutamic acid in skeletal
muscle mitochondria. All amino acids except alanine supported methioni
ne synthesis from OMTB in mitochondria of intestinal mucosa. We conclu
de that a wide variety of amino acids can serve as substrates for tran
samination of OMTB in the chicken, and that the availability of nitrog
en donors is unlikely to be a limiting factor in the conversion of OMT
B to methionine.