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PubMed2003

Umbilical threonine uptake during maternal threonine infusion in sheep.

OBJECTIVE: The infusion into the maternal circulation of amino acid solutions failed to increase umbilical threonine (THR) uptake above normal even when THR was present in the infusate at a relatively high concentration. The purpose of the present study was to determine whether umbilical THR uptake can be increased by infusing a THR solution that does not contain any other amino acids. STUDY DESIGN: Five pregnant sheep (130+/-1.0 days after conception) were infused for 2h with a threonine solution (4.4+/-0.2 micromol.kg(-1).min(-1)). Plasma amino acids, glucose and lactate, hematocrit, blood O(2) content in maternal arterial, uterine venous, umbilical arterial and venous blood were measured. Uterine and umbilical blood flows were measured before and during the infusion and were used to calculate uterine and umbilical uptakes. Maternal and foetal plasma insulin and glucagon concentrations were also measured. RESULTS: The THR infusion increased maternal plasma THR (904 vs 236 microM, P< 0.001), foetal plasma THR (539 vs 334 microM, P< 0.01), and both uterine (20.4 vs 4.7 micromol.min(-1).kg(-1)(fetalweight), P< 0.05) and umbilical (8.6 vs 3.8 micromol.min(-1).kg(-1)(fetalweight), P< 0.001) THR uptakes. The uterine-umbilical THR uptake difference increased significantly (11.8 vs 0.9 micromol.min(-1).kg(-1)(fetalweight), P< 0.05). There were significant (P< 0.001) decreases in the foetal arterial plasma concentrations of tyrosine and the branched chain amino acids, as well as in isoleucine umbilical uptake (P< 0.05). There was a significant increase in maternal plasma glucagon (P< 0.01). CONCLUSION: A maternal THR infusion that causes a 3.8-fold increase in maternal plasma THR concentration above normal, with no significant increase in the concentration of other amino acids, leads to a 2.3-fold increase in umbilical THR uptake. This contrasts with the absence of a significant increase in umbilical THR uptake when THR was infused as part of an amino acid mixture in previous studies. The evidence supports the hypothesis that, in vivo, THR flux from placenta to foetus is mediated by a saturable, rate limiting transport system which is subject to inhibition by other neutral amino acids.

Amino Acids↗
PubMed1990

Quantitative partition of threonine oxidation in pigs: effect of dietary threonine.

Kinetic aspects of threonine (Thr) metabolism were examined in eight pigs fed hourly with a diet containing either 0.68% (LT group) or 0.81% (HT group) of Thr (wt/wt), corresponding to 10 and 30% Thr excess, respectively, compared with an "ideal" diet. Primary production (PR) and disposal (DR) rates were obtained for Thr, glycine (Gly), and 2-keto-butyrate (KB) after a 12-h continuous infusion of L-[U-14C]-Thr together with [1-13C]Gly and a 6-h continuous infusion of [1-14C]KB. Transfer of Thr into secondary pools was also monitored, and from these the rates of Thr oxidation through the catabolic pathways of L-Thr 3-dehydrogenase (DR(Thr-Gly)) and threonine dehydratase (DR(Thr-KB)) were estimated. For the LT group the results were (mumol.kg-1.h-1) PR(Thr) 314 +/- 3, PR(Gly) 551 +/- 24, PR(KB) 41 +/- 3, DR(Thr-Gly) 22 +/- 2, and DR(Thr-KB) 7 +/- 1. For the HT group they were PR(Thr) 301 +/- 23, PR(Gly) 598 +/- 55, PR(KB) 39 +/- 4, DR(Thr-Gly) 32 +/- 2, and DR(Thr-KB) 8 +/- 1. The increase in Thr intake (14 mumol.kg-1.h-1, P less than 0.01) induced a commensurate increase in the sum of DR(Thr-Gly) and DR(Thr-KB) (14 mumol.kg-1.h-1, P less than 0.001) when liver was used as the precursor pool. This was mainly due to the increased DR(Thr-Gly) (13 mumol.kg-1.h-1, P less than 0.01); the change in DR(Thr-KB) was not statistically significant. By comparison of intracellular-to-plasma ratios of specific activities (or enrichments) for different tissues with each type of infusion, liver was shown to be the major site of production of Gly and KB from Thr. These data suggest that in fed growing pigs a 30% excess of Thr in the diet does not alter the partition of Thr oxidation, since 80% of Thr oxidation occurs through the L-Thr 3-dehydrogenase pathway for both LT and HT groups.

Amino Acids↗
PubMed1994

Factors improving L-threonine production by a three L-threonine biosynthetic genes-amplified recombinant strain of Brevibacterium lactofermentum.

When a Brevibacterium lactofermentum L-threonine producer that accumulated L-lysine as well, was transformed with a recombinant plasmid carrying the indigenous hom, thrB, and thrC genes, delayed growth and plasmid instability were observed. Addition of organic nutrients, vitamins (thiamine.HCl and d-biotin), and NaCl under the optimal culture conditions solved these problems and further increased threonine production in a small jar fermentor.

Brevibacterium↗
PubMed1990

A shared internal threonine-glutamic acid-threonine-proline repeat defines a family of Dictyostelium discoideum spore germination specific proteins.

A cDNA denoted pRK270 hybridizes to two mRNA species in RNA blots. The mRNAs specific to this clone are not expressed during vegetative growth and multicellular development. They are, however, found predominantly during early stages of spore germination, suggesting that their synthesis is rapidly and coordinately turned on during germination. Two different cDNAs named 270-6 and 270-11 were isolated, representing the two mRNAs. DNA blot analysis shows that 270 is a multigene family. Four genes were isolated from Dictyostelium genomic libraries and sequenced. The putative proteins coded for by these genes are about 51,000, 55,000, 76,000, and 100,000 Da. Two of the genes are expressed during spore germination while transcripts for the other two are not present during spore germination, vegetative growth, or the stages of multicellular development studied. The cDNAs and genes code for deduced proteins that possess a very unusual internal amino acid repeat comprised of the tetrapeptide threonine-glutamic acid-threonine-proline. The other portions of the proteins have no homology among themselves. The 270-6 protein shows excellent identity with avocado (Persea americana) cellulase, indicating that it may function as an endo-(1,4)-beta-D-glucanase.

Amino Acid Sequence↗
PubMed1988

Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase.

The nucleotide sequence of the gene, ilvA, for biosynthetic threonine deaminase (Tda) from Salmonella typhimurium was determined. The deduced amino acid sequence was compared with the deduced amino acid sequences of the biosynthetic Tda from Escherichia coli K-12 (ilvA) and Saccharomyces cerevisiae (ILV1) and the biodegradative Tda from E. coli K-12 (tdc). The comparison indicated the presence of two types of blocks of homologous amino acids. The first type of homology is in the N-terminal portion of all four isozymes of Tda and probably indicates amino acids involved in catalysis. The second type of homology is found in the C-terminal portion of the three biosynthetic isozymes and presumably is involved in either (i) the binding or interaction of the allosteric effector isoleucine with the enzyme, or (ii) subunit interactions. The sites of amino acid changes of two E. coli K-12 ilvA alleles with altered response to isoleucine are consistent with the conclusion that the C-terminal portion of biosynthetic Tda is involved in allosteric regulation.

Alleles↗
PubMed2004

Determination of d- and l-enantiomers of threonine and allo-threonine in mammals using two-step high-performance liquid chromatography.

A sensitive and selective method for the determination of four threonine (Thr) isomers (L-Thr, D-Thr, L-allo-Thr and D-allo-Thr) in mammalian tissues has been established using two-step high-performance liquid chromatography. This method includes the precolumn fluorescence derivatization of amino acids with 4-fluoro-7-nitro-2,1,3-benzoxadiazole (NBD-F), and the separation using a combination of a reversed-phase column and a chiral column. The calibration ranges of D-Thr, D-allo-Thr and L-allo-Thr spiked in the rat cerebellum sample are 2.5 fmol-5 pmol per injection, and that of L-Thr is 50 fmol-50 pmol. Within-day and day-to-day precisions of the determination of the four Thr isomers are approximately 5% in the rat cerebellum. By using this method, the tissue distributions of D-Thr, D-allo-Thr and L-allo-Thr in mammals have been demonstrated for the first time in rats, and found that significant amounts of D-Thr and D-allo-Thr are present in the frontal brain areas and urine. Among the 12 tissues tested, the highest amounts of D-Thr (0.85 +/- 0.05 nmol/g wet tissue) and D-allo-Thr (5.01 +/- 0.32 nmol/g wet tissue) were found in the corpus striatum. L-allo-Thr was not present in any of the tested tissues and physiological fluids.

4-Chloro-7-nitrobenzofurazan↗
PubMed1997

Maintenance threonine requirement and efficiency of its use for accretion of whole-body threonine and protein in young chicks.

Broiler chicks were fed on chemically-defined crystalline amino acid diets containing graded levels of L-threonine (Thr) during the period 10-20 d post-hatching. Doses of Thr represented 5, 10, 15, 40, 55, 70 and 95% of its ideal level for maximal weight gain and feed efficiency. Other amino acids were maintained at minimized excess levels that were 15% (of ideal) above the various doses of Thr. Following 10 d of feeding and a 24 h fast, chicks were killed for whole-body protein and amino acid analysis. Using pen accretion means, weight gain (r2 0.98), protein accretion (r2 0.99), and Thr accretion (r2 0.99) were linear (P < 0.01) functions of Thr intake. Slope of the Thr accretion regression line indicated that 82% of the Thr intake was recovered in whole-body protein. At zero Thr intake, chicks lost 11.9 mg Thr/d. The Thr maintenance requirement was 45.7 mg/d per kg body weight 0.75. Increasing doses of Thr resulted in increased (P < 0.05) concentrations of methionine, isoleucine, histidine and lysine in whole-body protein. Other indispensable amino acids, including Thr, also tended to increase. Whole-body glycine, proline, serine and cystine concentrations decreased (P < 0.05) as Thr was increased in the diet. The maintenance need for Thr represented 5.5% of the total need for Thr. The data suggest that efficiency of Thr utilization is constant at all levels of Thr intake between 5 and 95% of the level required for maximal weight gain and feed efficiency.

Analysis of Variance↗
PubMed2006

Maintenance threonine requirement and efficiency of its use for accretion of whole-body threonine and protein in Atlantic salmon (Salmo salar L.) fry.

Eighteen groups of seventy Atlantic salmon (Salmo salar L.) fry (initial mean body weight 0.8 (sd 0.01) g) were fed on semi-purified diets containing graded levels of l-threonine (Thr) in 15 litres aquaria at a temperature of 14.5+/-1 degrees C. Doses of Thr represented 1, 31, 41, 51, 62, 72, 83 and 93 % of its ideal level for optimum protein deposition. Indispensable amino acids other than Thr were included in the same proportion (on a g/16 g N basis) as in the Atlantic salmon fry whole-body carcass. Following 36 d of feeding and a 36 h fast, fry were killed for whole-body protein and amino acid analysis. Weight gain (r2 0.98), protein accretion (r2 0.97), and Thr accretion (r2 0.97) were linear (P<0.01) functions of Thr intake. Slope of the Thr accretion regression line showed that the efficiency of Thr utilisation above maintenance was 76 %. At zero Thr intake, fry lost 5.4 mg Thr/kg body weight0.75 per d. The Thr maintenance requirement was 7.2 mg/kg body weight0.75 per d and the Thr requirement for growth was 66 mg for 1 g protein deposition. Increasing doses of Thr resulted in increased (P<0.05) concentrations of histidine and lysine, and decreased concentrations of isoleucine in whole-body protein. The maintenance need for Thr represented 13.4 % of the total need for Thr. The data suggest that efficiency of Thr utilisation above maintenance is constant at all levels of Thr intake between 1 and 93 % of the level required for optimum protein deposition.

Amino Acids↗
PubMed2001

Influence of threonine intake on whole-body protein deposition and threonine utilization in growing pigs fed purified diets.

The relationship between available threonine (Thr) intake and whole-body protein deposition (PD) was established using the serial slaughter method in 36 individually housed growing gilts between 39 and 77 kg live BW. Pigs were prescreened for their maximum PD (PDmax), based on a N balance starting at 25 kg BW while they consumed semi-ad libitum a nonlimiting diet. Pigs were fed combinations of a casein and cornstarch-based diet that was confirmed to be first-limiting in Thr and a protein-free diet starting at approximately 30 kg BW. Casein-bound Thr was provided at 60, 70, 80, 90, 100, or 120% of estimated Thr requirements for PDmax. Energy intake was kept constant across treatments and exceeded requirements for PDmax. Pigs were fed three equal meals per day; feeding levels were adjusted weekly based on BW. Pigs were killed at either 39 kg BW (n = 2 per treatment) or 77 kg BW (n = 4 per treatment) for determining chemical body composition. Composition of 39-kg BW pigs was not different across treatments (P > 0.10); therefore, an overall mean initial body composition was used to estimate body protein content at the initial BW. Across treatments, mean daily ME intake was 25.3 (SE 0.08) MJ/d and did not differ (P > 0.10) among treatments. Average daily true ileal digestible Thr intake varied between 5.33 and 9.66 g/d, representing means for pigs on the lowest and the highest Thr intakes, respectively. Mean PD was 93, 102, 118, 124, 139, and 133 (SE 4.2) g/d for pigs on the six respective treatments. Dietary Thr intake did not influence (P > 0.10) Thr content of body protein at the final BW or the partitioning of body protein between carcass, viscera, and blood. The efficiency of Thr utilization for PD was lowest (P < 0.05) at the highest Thr intake level and highest (P < 0.05) at the lowest Thr intake level. It was similar (P > 0.10) at the four intermediate Thr intake levels, in which the relationship between true ileal digestible Thr intake and PD was linear. Based on these four treatments, calculated Thr disappearance, which is closely associated with inevitable Thr catabolism, was 23.5 (SE 0.55)% of available Thr intake. This value is consistent with an efficiency of using available Thr intake above maintenance Thr requirements (54 mg/kg BW0.75) for Thr retention with PD of 73.4 (SE 1.11)%. Based on N balances conducted at approximately 40 and 75 kg BW, the marginal efficiency of Thr utilization was not influenced by BW.

Animal Feed↗
PubMed2006

Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool.

Amino acids are not only fundamental protein constituents but also serve as precursors for many essential plant metabolites. Although amino acid biosynthetic pathways in plants have been identified, pathway regulation, catabolism, and downstream metabolite partitioning remain relatively uninvestigated. Conversion of Thr to Gly and acetaldehyde by Thr aldolase (EC 4.1.2.5) was only recently shown to play a role in plant amino acid metabolism. Whereas one Arabidopsis thaliana Thr aldolase (THA1) is expressed primarily in seeds and seedlings, the other (THA2) is expressed in vascular tissue throughout the plant. Metabolite profiling of tha1 mutants identified a >50-fold increase in the seed Thr content, a 50% decrease in seedling Gly content, and few other significant metabolic changes. By contrast, homozygous tha2 mutations cause a lethal albino phenotype. Rescue of tha2 mutants and tha1 tha2 double mutants by overproduction of feedback-insensitive Thr deaminase (OMR1) shows that Gly formation by THA1 and THA2 is not essential in Arabidopsis. Seed-specific expression of feedback-insensitive Thr deaminase in both tha1 and tha2 Thr aldolase mutants greatly increases seed Ile content, suggesting that these two Thr catabolic enzymes compete for a common substrate pool.

Aldehyde-Lyases↗