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At least 19 recordsLinked to original sources
PubMed1978

Threonine metabolism in vivo: effect of threonine intake and prior induction of threonine dehydratase in rats.

The metabolic fate of threonine was investigated in young male rats fed 15% amino acid diets containing from 0.15% to 0.85% of L-threonine. Liver serine-threonine dehydratase (S-TDH) activity did not increase with increasing dietary threonine content. The level of threonine required for maximum weight gain was not greater than 0.55% of the diet (or about 600 mumoles/day). Tissue free threonine content of rats fed the diets with 0.15% or 0.3% of threonine was very low but increased sharply with increasing dietary threonine content above 0.3%. During ad libitum feeding of these diets containing L-[U-14C]threonine, rate of oxidation of threonine was low when intake was in the range of the requirement for maximum growth, but increased, thereafter as threonine intake increased. A 30-fold induction of liver S-TDH, by prior feeding of an 80% casein diet, did not result in increased oxidation of threonine when dietary threonine content was 0.15%. When dietary threonine content was increased to 0.5%, oxidation of threonine increased slightly but significantly. With 3% of threonine in the diet, rats previously fed a 15% casein diet had extremely high tissue threonine concentrations whereas those with high S-TDH activity, due to the previous feeding of the 80% casein diet, oxidized threonine rapidly and tissue threonine concentrations were elevated much less.

Animals↗
PubMed1976

Bacterial catabolism of threonine. Threonine degradation initiated by L-threonine-NAD+ oxidoreductase.

1. Isolates representing seven bacterial genera capable of growth on L-threonine medium, and possessing high L-threonine 3-dehydrogenase activity, were examined to elucidate the catabolic route. 2. The results of growth, manometric and enzymic experiments indicated the catabolism of L-threonine by cleavage to acetyl-CoA plus glycine, the glycine being further metabolized via L-serine to pyruvate, in all cases. No evidence was obtained of a role for aminoacetone in threonine catabolism or for the metabolism of glycine by the glycerate pathway. 3. The properties of a number of key enzymes in L-threonine catabolism were investigated. The inducibly formed L-threonine 3-dehydrogenase, purified from Corynebacterium sp. B6 to a specific activity of about 30-35 mumol of product formed/min per mg of protein, exhibited a sigmoid kinetic response to substrate concentration. The half-saturating concentration of substrate, [S]0.5, was 20mM and the Hill constant (h) was 1.50. The Km for NAD+ was 0.8mM. The properties of the enzyme were studied in cell-free extracts of other bacteria. 4. New assays for 2-amino-3-oxobutyrate-CoA ligase were devised. The Km for CoA was determined for the first time and found to be 0.14mM at pH8, for the enzyme from Corynebacterium sp. B6. Evidence was obtained for the efficient linkage of the dehydrogenase and ligase enzymes. Cell-free extracts all possessed high activities of the inducibly formed ligase. 5. L-Serine hydroxymethyltransferase was formed constitutively by all isolates, whereas formation of the 'glycine-cleavage system' was generally induced by growth on L-threonine or glycine. The coenzyme requirements of both enzymes were established, and their linked activity in the production of L-serine from glycine was demonstrated by using extracts of Corynebacterium sp. B6. 6. L-Serine dehydratase, purified from Corynebacterium sp. B6 to a specific activity of about 4mumol of product formed/min per mg of protein, was found to exhibit sigmoid kinetics with an [S]0.5 of about 20mM and h identical to 1.4. Similar results were obtained with enzyme preparations from all isolates. The enzyme required Mg2+ for maximum activity, was different from the L-threonine dehydratase also detectable in extracts, and was induced by growth on L-threonine or glycine.

Alcohol Oxidoreductases↗
PubMed1977

Bacterial catabolism of threonine. Threonine degradation initiated by L-threonine acetaldehyde-lyase (aldolase) in species of Pseudomonas.

1. The route of l-threonine degradation was studied in four strains of the genus Pseudomonas able to grow on the amino acid and selected because of their high l-threonine aldolase activity. Growth and manometric results were consistent with the cleavage of l-threonine to acetaldehyde+glycine and their metabolism via acetate and serine respectively. 2. l-Threonine aldolases in these bacteria exhibited pH optima in the range 8.0-8.7 and K(m) values for the substrate of 5-10mm. Extracts exhibited comparable allo-l-threonine aldolase activities, K(m) values for this substrate being 14.5-38.5mm depending on the bacterium. Both activities were essentially constitutive. Similar activity ratios in extracts, independent of growth conditions, suggested a single enzyme. The isolate Pseudomonas D2 (N.C.I.B. 11097) represents the best source of the enzyme known. 3. Extracts of all the l-threonine-grown pseudomonads also possessed a CoA-independent aldehyde dehydrogenase, the synthesis of which was induced, and a reversible alcohol dehydrogenase. The high acetaldehyde reductase activity of most extracts possibly resulted in the underestimation of acetaldehyde dehydrogenase. 4. l-Serine dehydratase formation was induced by growth on l-threonine or acetate+glycine. Constitutively synthesized l-serine hydroxymethyltransferase was detected in extracts of Pseudomonas strains D2 and F10. The enzyme could not be detected in strains A1 and N3, probably because of a highly active ;formaldehyde-utilizing' system. 5. Ion-exchange and molecular exclusion chromatography supported other evidence that l-threonine aldolase and allo-l-threonine aldolase activities were catalysed by the same enzyme but that l-serine hydroxymethyltransferase was distinct and different. These results contrast with the specificities of some analogous enzymes of mammalian origin.

Acetaldehyde↗
PubMed1996

Threonine is catabolized by L-threonine 3-dehydrogenase and threonine dehydratase in hepatocytes from domestic cats (Felis domestica).

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-14C]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 14CO2 and [14C]glucose. At the same time, large amounts of [14C]glycine but no [14C]ethanol was formed. Inclusion of 10 mmol/L 2-ketobutyrate + 2-hydroxybutyrate decreased 14CO2 but not [14C]glucose production and resulted in the formation of [14C]2-hydroxybutyrate. Under all incubation conditions, 14CO2 and [14C]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.

Acetaldehyde↗
PubMed1980

Role of L-threonine deaminase and L-threonine 3-dehydrogenase in the utilization of L-threonine by Pseudomonas aeruginosa.

Mutants of Pseudomonas aeruginosa PAC1 which could grow on L-threonine were isolated. These mutants, like the parent strain, synthesized a biosynthetic threonine deaminase, but its apparent Km value for threonine was higher than that of the enzyme from strain PAC1. These mutants also synthesized an inducible NAD-dependent threonine dehydrogenase, which was not present in the parent strain. No threonine aldolase activity could be detected. The results suggest that the threonine deaminase with lowered affinity for L-threonine, together with L-threonine dehydrogenase, enabled these mutants to utilize L-threonine as the sole source of carbon for growth.

Alcohol Oxidoreductases↗
PubMed1997

The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme.

The GLY1 gene of Saccharomyces cerevisiae is required for the biosynthesis of glycine for cell growth [McNeil, J. B., McIntosh, E. V., Taylor, B. V., Zhang, F-R., Tang, S. & Bognar, A. L. (1994) J. Biol. Chem. 269, 9155-9165], but its gene product has not been identified. We have found that the GLY1 protein is similar in primary structure to L-allo-threonine aldolase of Aeromonas jandiae DK-39, which stereospecifically catalyzes the interconversion of L-allo-threonine and glycine. The GLY1 gene was amplified by PCR, with a designed ribosome-binding site, cloned into pUC118, and expressed in Escherichia coli cells. The enzyme was purified to homogeneity, as judged by polyacrylamide gel electrophoresis. The enzyme has a molecular mass of about 170 kDa and consists of four subunits identical in molecular mass. The enzyme contains 2 mol pyridoxal 5'-phosphate/4 mol of subunit as a cofactor, and its absorption spectrum exhibits maxima at 280 nm and 420 nm. The enzyme catalyzes the cleavage of not only L-allo-threonine to glycine but also L-threonine. We have termed the enzyme a low-specific L-threonine aldolase to distinguish it from L-allo-threonine aldolase.

Aeromonas↗
PubMed1982

Threonine metabolism of chicks fed threonine-imbalanced diets.

Experiments were conducted to determine the metabolic fate of threonine in chicks fed threonine-imbalanced diets. Threonine imbalance was produced by the addition of 3% serine to a threonine-limited diet, and prevented by the addition of 0.2% threonine to the diet. Serine decreased plasma and liver free threonine concentrations, and increased hepatic threonine dehydrogenase and threonine aldolase activities. All changes, including reduced food intake, appeared to occur within 1 day of feeding the imbalanced diet. Despite the decrease in free threonine concentrations and the increase in threonine aldolase and threonine dehydrogenase activities, net threonine catabolism was not markedly increased. This was evidenced by similar amounts of 14CO2 exhaled by chicks fed control and imbalanced diets containing L-[U-14C] threonine, and by similar growth of chicks that were forced-fed both diets to maintain equivalent food intake. It is possible that increases in threonine catabolism contribute to depressions of plasma and tissue threonine concentrations. However, the growth depression caused by serine-induced threonine imbalance is due to depressed food intake.

Alcohol Oxidoreductases↗
PubMed1995

In vivo threonine oxidation rate is dependent on threonine dietary supply in growing pigs fed low to adequate levels.

Threonine oxidation was examined in 12 growing pigs fed a well-balanced control diet or a threonine-deficient diet supplemented (Glu) or not (LT) with glutamic acid during constant infusion of L-[1-(13)C]-threonine, [1-(14)C]glycine and [1-(14)C]alpha-ketobutyrate for 10 h. During these infusion, liver glycine enrichment was significantly lower than plasma enrichment. Moreover, the pancreas to plasma glycine enrichment ratio was higher than the liver to plasma ratio (70-89%), showing that an important part of glycine de novo synthesis in pancreas occurred through the threonine dehydrogenase (TDG) pathway. These results imply that calculation of threonine oxidation into glycine should be made with the assumption of both hepatic and extrahepatic oxidation. Plateau values of plasma threonine, glycine and alpha-ketobutyrate enrichments and specific radio activities allowed estimations of threonine oxidation through the TDG and threonine dehydratase (TDH) pathways. Threonine oxidation into glycine was 12.16 +/- 2.06, 2.89 +/- 0.61 and 2.13 +/- 0.44 mumol/(kg.h), respectively, in pigs fed the control, LT and Glu diets, and threonine oxidation into alpha-ketobutyrate was 1.80 +/- 0.31, 0.88 +/- 0.02 and 0.55 +/- 0.06 mumol/ (kg.h) for the control, LT and Glu groups, respectively. Total threonine oxidation rates were 75 and 81% lower in the LT and Glu groups, respectively, than in the control group. Liver TDG and TDH activity measured in vitro were not affected by either the level of dietary threonine supply the addition of glutamic acid. On the basis of plasma data, it may be concluded that the addition of glutamic acid to a threonine-deficient diet had no significant effect on threonine oxidation but did reduce the rate of threonine release from protein breakdown. Oxidation appears to be related to plasma threonine concentration.

Animals↗
PubMed1983

Metabolic homoeostasis of L-threonine in the normally-fed rat. Importance of liver threonine dehydrogenase activity.

Threonine dehydratase, threonine aldolase and threonine dehydrogenase activities were assayed in livers of rats that had been normally-fed, starved for 72 h, fed a high-protein diet or normally-fed and injected with glucagon or cortisone. A modified continuous spectrophotometric assay for threonine aldolase overcame interference resulting from threonine dehydratase activity and revealed that threonine aldolase activity was very low in rat liver, irrespective of the metabolic state of the animal. The concentration of free threonine was determined in livers of animals subjected to the same treatments as described above. Using Michaelis-Menten kinetics to estimate enzyme activities in vivo at intracellular threonine concentrations it was calculated that in the normally-fed state, 87% of the threonine degraded was catabolized by threonine dehydrogenase. In other metabolic states (except in glucagon-treated animals) threonine dehydratase was the major enzyme catalysing threonine catabolism. It was concluded that threonine dehydrogenase activity plays a hitherto unrecognized role in the metabolic homoeostasis of threonine in the normally-fed rat and that this enzyme activity, in association with 2-amino-3-oxobutyrate CoA-ligase, accounts for the known rate of glycine formation from threonine in the rat.

Alcohol Oxidoreductases↗
PubMed1983

Threonine metabolism in sheep. I. Threonine catabolism and gluconeogenesis in mature Blackface wethers given poor quality hill herbage.

In three experiments, mature Blackface wethers were given freeze-stored Agrostis festuca herbage by continuous feeder. In Expt 1, on separate occasions [U-14C]threonine, [U-14C]glucose and NaH14CO3 were infused over 12 h periods to obtain estimates of irreversible loss rate (ILR) of threonine, glucose and carbon dioxide in the plasma and of the exchange of C between these metabolites. In Expts 2 and 3, during periods when glucose and threonine metabolism were examined, glucose loss across the kidneys (23-29 g/d) was induced by infusion of phloridzin. Results from the four sheep used in Expts 1 and 3 are presented as three-pool models. They indicate that threonine ILR (7.8 g/d; 3.1 g C/d) was approximately three times the estimated rate of absorption of exogenous threonine (1 g C/d). Glucose ILR was approximately 76 g/d (mean +/- SE; 30.3 +/- 0.57 g C/d). Only 0.3% of the glucose-C (0.09 g/d) was derived directly from threonine-C (i.e. 3% of the threonine-C ILR). Bicarbonate ILR was 170 +/- 7.3 g C/d, and glucose contributed 11.1 +/- 3.52 g C/d to this, accounting for 51 +/- 4.4% of glucose-C ILR. Threonine contributed 0.20 +/- 0.026 g C/d to the bicarbonate-C ILR, accounting for only 6.4 +/- 0.87% of the threonine-C ILR. When, in Expts 2 and 3, phloridzin was infused, glucose ILR was increased by 28 +/- 1.5% and bicarbonate ILR was increased by 13 +/- 2.4%. Threonine ILR (3.1 g C/d) was not increased, but the metabolic distribution of threonine-C was altered. The transfer of threonine-C into glucose and CO2 was increased by 39 and 69% respectively to 0.125 and 0.45 g C/d, accounting for 4 and 13% of the threonine ILR respectively. Both technical and metabolic considerations which affect interpretation of these results in terms of rates of catabolism of threonine and of quantitative estimates of gluconeogenesis from threonine are discussed.

Animal Feed↗
PubMed1978

Catabolism of threonine in mammals by coupling of L-threonine 3-dehydrogenase with 2-amino-3-oxobutyrate-CoA ligase.

There is doubt about the L-threonine 3-dehydrogenase (EC 1.1.1.103) and threonine aldolase (EC 2.1.2.1) catabolic pathways of L-threonine in mammals which are believed to produce aminoacetone and glycine plus acetaldehyde, respectively. L-Threonine 3-dehydrogenase in disrupted guinea-pig liver mitochondria was investigated in a reaction mixture containing L-threonine without and with CoA and oxaloacetate; L-[U-14C]threonine was included in four similar experiments for autoradiograms. Threonine aldolase was examined in similar mitochondria from liver and kidney. CoA reduced the aminoacetone formed from L-threonine to 10-14% and CoA plus oxaloacetate produced citrate (from CoASAc) in approximately equal amounts to the decrease in aminoacetone. Autoradiograms confirmed the decrease in aminoacetone with the simultaneous appearance of citrate and glycine. No evidence was obtained that threonine aldolase catabolised L-threonine at the concentration used to assay the dehydrogenase. It is concluded that 2-amino-3-oxobutyrate (precursor of aminoacetone), which is produced from L-threonine by L-threonine 3-dehydrogenase, undergoes CoA-dependent cleavage to glycine and CoASAc by 2-amino-3-oxobutyrate-CoA ligase. The results suggest that the coupling of these enzymes provides a new pathway for the catabolism of threonine in mammals.

Acetone↗
PubMed1996

In vivo threonine oxidation in growing pigs fed on diets with graded levels of threonine.

Threonine oxidation to glycine was investigated in vivo in twelve growing pigs (27.4 kg live weight) fed on one of the following three diets with graded levels of threonine supply: a low-threonine diet (LT), a control well-balanced diet (C) or a high-threonine diet (HT), during 10 h constant infusion of L-[1-13C]threonine and [2-3H]glycine in the cranial vena cava and [1-14C]glycine in the portal vein. 13C-threonine and glycine enrichments and [3H]glycine and [14C]glycine specific radioactivities (SR) were determined at plateau in peripheral venous plasma, liver and pancreas. Glycine production rates calculated from plasma [2-3H]glycine or [1-14C]glycine SR gave similar values suggesting that [1-14C]glycine SR could be used in order to estimate whole-body glycine flux. The high pancreas [1-13C]glycine enrichment provided evidence that the pancreas may be, with the liver, a major site of threonine oxidation to glycine. Moreover, the present findings suggest that threonine transport into the liver could be the limiting step of threonine oxidation in this tissue when dietary threonine supply is low. Total threonine oxidation to glycine, calculated from plasma values of enrichment and specific radioactivity, was low and constant when the estimated absorbed threonine was lower than 4 g/d and increased for higher amounts of absorbed threonine.

Animals↗
PubMed1996

Efficiency of lysine or threonine retention in growing rats fed diets limiting in either lysine or threonine.

Over a 21-d experiment, the efficiency of lysine and threonine retention was determined in 80 male Sprague-Dawley rats (65.9 +/- 0.3 g, means +/- SE) fed purified diets containing an amino acid mix limiting in either lysine or threonine. With additional increments of the first limiting amino acid, lysine concentration in total body protein (g/16 g N) increased (P < 0.01) in rats fed lysine-limiting diets but, when fed threonine-limiting diets, lysine concentration in body protein first increased and then decreased (P < 0.01). As increments of the first limiting amino acid were added, the threonine concentration in total body protein increased then decreased when both lysine- (P < 0.01) and threonine- (P < 0.06) limiting diets were fed. Lysine and threonine retention were calculated based on comparative slaughter. Sixteen rats were killed on d 0 to estimate the grams of amino acid in the body. Retention responses were analyzed using a logistic equation in which lysine or threonine intake was used to predict retention. The maximum marginal efficiency (dr/dI, retention/intake) was observed at <40% of maximum retention. For lysine retention, it was 81% when lysine was limiting and 70% when threonine was limiting. For threonine retention, it was 58% when threonine was limiting and 49% when lysine was limiting. The maximum cumulative efficiency (retention adjusted for maintenance relative to cumulative intake) for lysine retention was 62% when lysine was limiting or 58% when threonine was limiting. For threonine retention, it was 51% when threonine was limiting and 35% when lysine was limiting. Thus, amino acid concentration in body protein is not constant, and amino acids are used with higher efficiency when first limiting.

Amino Acids↗
PubMed1985

Threonine requirement of pigs weighing 5 to 15 kg and the effect of excess methionine in diets marginal in threonine.

Experiments were conducted to estimate the threonine requirement of pigs weighing 5 to 15 kg and to determine whether excess methionine increased the threonine requirement. Feeding .70% dietary threonine in Exp. 1 maximized (P less than .01) gain/feed and minimized (P less than .01) plasma urea N. Plasma threonine was increased (P less than .01) by threonine supplementation and the rate of increase accelerated above .65% dietary threonine. Threonine supplementation did not affect plasma methionine, tryptophan and(or) lysine, but it increased leucine (P less than .01) and isoleucine (P less than .05). In Exp. 2, additions of .40% methionine and(or) .30% threonine to a 16% crude protein diet that had calculated concentrations of .57% sulfur amino acids and .68% threonine did not affect (P less than .10) pig performance or plasma urea N. In Exp. 3, a 15% crude protein diet that had calculated concentrations of .54% sulfur amino acids and .61% threonine was supplemented with .40% methionine and(or) .15% threonine. Amino acid additions did not affect performance of pigs, but pigs fed supplemental threonine had the least plasma urea N, indicating that .61% dietary threonine was marginally deficient for pigs weighing 5 to 15 kg.

Animal Feed↗
PubMed1994

Dietary threonine imbalance alters threonine dehydrogenase activity in isolated hepatic mitochondria of chicks and rats.

Experiments were conducted on chicks and rats to determine whether hepatic threonine dehydrogenase activity is modified by the consumption of a threonine-imbalanced diet and to determine the tissue distribution of this enzyme. Threonine imbalances were created by supplementing basal diets with branched-chain amino acids (6 g/100 g diet for chicks) or a mixture of indispensable amino acid (5.6 g/100 g diet for chicks and 5.4 g/100 g diet for rats). Chicks fed threonine-imbalanced diets consistently had twice the hepatic threonine dehydrogenase activity of those fed the basal diet when measured in one experiment at 24 h and in two experiments at 216 h (P < 0.05). Rats received the experimental diets for 12 or 24 h in one experiment and for 12, 24, 72 or 168 h in another experiment. In the first experiment, rats fed the threonine-imbalanced diet had significantly greater hepatic threonine dehydrogenase activity (P < 0.05) at 12 h but not at 24 h. In the other rat experiment, threonine dehydrogenase activity in the rats fed the threonine-imbalanced diet was significantly greater than in controls at 72 h, but tended to be lower at 168 h, which coincided with the adaptation of the rats to the imbalanced diet. Threonine dehydrogenase activity was widespread in tissues of both species. The results indicate that alterations in hepatic threonine dehydrogenase activity occur in chicks and rats subjected to threonine imbalance.

Acetone↗
PubMed1994

Threonine requirement and threonine imbalance in broiler chickens.

Three experiments were conducted to determine the effect of excess dietary protein on threonine requirement of broiler chicks to 14 d of age (Experiments 1 and 2) and to determine the threonine requirement from 16 to 28 d of age (Experiment 3). Two dietary protein levels were used in Experiments 1 and 2:20% CP in a threonine-limiting basal diet containing wheat, peanut meal, and selected amino acids and 25% CP in the same basal diet supplemented with a mixture of amino acids lacking threonine. A threonine-limiting 25% CP diet based on corn, soybean meal, and amino acids was also included in Experiment 2. The threonine requirement of chicks from 16 to 28 d of age was determined using a single CP level (20%) in Experiment 3. Threonine requirements were estimated by broken line regression analysis of weight gain and feed efficiency. Threonine requirements based on weight gain were 7.7 and 6.7 g/kg of diet in Experiments 1 and 2, respectively, for chicks receiving the 20% CP diets. The requirements increased to 8.6 and 8.2 g/kg, respectively, for chicks fed the 25% CP diets based on wheat, peanut meal, and amino acids. The requirement for maximum weight gain of chicks fed 25% CP based on corn, soybean meal, and amino acids was 7.7 g/kg of diet. However, chicks ate more of this diet, and on an intake basis, the requirement of the chicks fed the 25% CP diets based on wheat and peanut meal or corn and soybean meal did not differ. Requirements based on feed efficiency were equal to, or less than, those based on weight gain in Experiments 1 and 2. Body moisture and fat contents were affected by dietary CP level (P < .01), ingredient composition (P < .01), and threonine content (P < .05). Estimates of threonine requirements based on regression analysis of plasma threonine concentrations were higher than those based on weight gain or feed efficiency. The threonine requirements of chicks fed a 20% CP diet from 16 to 28 d of age were 6.3 and 6.9 g/kg of diet based on weight gain and feed efficiency, respectively.

Animal Feed↗
PubMed1986

Threonine kinetics at graded threonine intakes in young men.

A study was undertaken in eight healthy young men to examine the effects of varying intakes of threonine on plasma free threonine concentrations and threonine kinetics, using a 3 h constant intravenous infusion of L-[1-13C]threonine. Subjects consumed diets based on an L-amino acid mixture, in which the quality of threonine was reduced every 7 days. On the last day of each diet period, determinations of plasma threonine flux and threonine oxidation were carried out while subjects consumed small meals, each supplying 1/12 daily intake, at hourly intervals. Threonine oxidation rates fell with reduced threonine intake, reaching a relatively constant level at intakes of 20 mg.kg-1.day-1 and below. These metabolic data are discussed in relation to the currently established value of 7 mg.kg-1.day-1 as the upper range of the threonine requirement for healthy young adults. It is concluded that actual threonine requirements may be considerably higher for this age group.

Adolescent↗