Threonine is catabolized by L-threonine 3-dehydrogenase and threonine dehydratase in hepatocytes from domestic cats (Felis domestica)
Threonine is catabolized by L-threonine 3-dehydrogenase and threonine dehydratase in hepatocytes from domestic cats (Felis domestica)
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DOI:
10.1093/jn/126.9.2218
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发表时间:
1996-09-01
影响因子:
4.2
通讯作者:
Freedland, RA
中科院分区:
文献类型:
--
作者:
Hammer, VA;Rogers, QR;Freedland, RA
Isolated hepatocytes were used to study threonine catabolism in kittens, and dietary threonine and crude protein were varied to study enzyme adaptation. Cells were isolated from 21-wk-old kittens which had been fed diets containing threonine at 4 or 8 g/kg of diet with either 200 or 500 g crude protein/kg of diet (2 x 2 factorial, n = 4/group). Production of CO2, glucose and various metabolites from [U-C-14]threonine were measured. Inclusion of 10 mmol/L glycine, or glycine in combination with 10 mmol/L acetaldehyde + ethanol, in the incubation medium decreased formation of (CO2)-C-14 and [C-14]glucose. At the same time, large amounts of [C-14]glycine but no [C-14]ethanol was formed. Inclusion of 10 mmol/L 2-ketobutyrate + 2-hydroxybutyrate decreased (CO2)-C-14 but not [C-14]glucose production and resulted in the formation of [C-14]2-hydroxybutyrate. Under all incubation conditions, (CO2)-C-14 and [C-14]glucose production changed in response to alterations in dietary protein but not dietary threonine. It appears that threonine dehydratase and L-threonine 3-dehydrogenase, but not threonine aldolase, are active pathways for threonine metabolism in cats, and both enzymes are sensitive to levels of dietary protein.