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PubMed1992

Isoleucine requirement of broiler chicks as affected by the concentrations of leucine and valine in practical diets.

1. Chicks were fed on an isoleucine-deficient diet, with 6 added concentrations of isoleucine to determine their isoleucine requirement and an additional 6 treatments were devised to determine their isoleucine requirement when dietary leucine and valine contents were increased. 2. The diet deficient in isoleucine contained 5.6 g/kg isoleucine with leucine and valine contents of 20.1 and 10.3 g/kg, respectively. Supplementation with leucine and valine increased these to 24.7 and 12.6 g/kg, respectively. 3. The isoleucine requirement was not affected by dietary leucine and valine contents in a diet with 13.4 MJ of ME per kg. Analysis of variance and Least Significant Difference of means indicated an isoleucine requirement of 7.2 g/kg. Non-linear regression of the same data indicated an isoleucine requirement of 8.44 g/kg, based on weight gain, or 8.19 g/kg based on food efficiency. 4. Reasons for the failure to find an imbalancing effect of branched chain amino acids in practical diets are discussed.

Analysis of Variance↗
PubMed1997

Effects of caloric intake on anticancer therapy in rats with valine-depleted amino acid imbalance.

Valine-depleted amino acid imbalance solution markedly inhibits tumor growth but causes fatty liver as a side effect. However, much remains unknown about the mechanism of the development of fatty liver. Valine-depleted amino acid imbalance solution containing various concentrations of calories was administered to tumor-bearing rats for four days by means of total parenteral nutritional methods to investigate the interaction of caloric intake and the development of fatty liver. Compared with the total parenteral nutrition control group the triglyceride content of the liver rose significantly in the group given valine-depleted amino acid imbalance solution with an increase in caloric intake. Plasma total protein and albumin significantly decreased. The very-low-density lipoprotein concentration in serum was also significantly lower than that in the control group. Valine-depleted amino acid imbalance caused hypoproteinemia, suggesting a fall in synthesis of apolipoproteins in the liver indispensable for lipid release. Along with the increase in the total caloric intake, triglyceride synthesis in the liver increased, resulting in augmentation of fatty content of the liver, probably because of the decreased lipid release.

Amino Acids↗
PubMed1997

The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing.

Soluble forms of transforming growth factor-alpha (TGF alpha) are derived by proteolytic processing of an integral membrane glycoprotein precursor (pro TGF alpha). Previous studies indicated that phorbol ester-induced cleavage of pro TGF alpha in CHO cells is dependent on the presence of a valine residue located at the carboxyl terminus of the precursor's cytoplasmic domain. We reassessed this requirement with epitope-tagged constructs introduced into transformed rat liver epithelial cells that normally express and process TGF alpha. We found that pro TGF alpha mutants lacking the terminal valine residues showed greatly reduced maturation to the fully glycosylated form. Additionally, they were present at substantially reduced levels on the cell surface and, instead, accumulated in the endoplasmic reticulum. Consistent with these results, enzyme-linked immunosorbent assay (ELISA) and Western blot analyses revealed little or no soluble TGF alpha in medium conditioned by cells expressing the mutant constructs. Finally, a truncated pro TGF alpha mutant lacking most of the cytoplasmic domain but retaining a carboxyl-terminal valine was processed and cleaved in a near-normal manner. These results, some of which were reproduced in CHO cells, indicate that the predominant effect of the carboxyl-terminal valines is to ensure normal maturation and routing of the precursor.

Animals↗
PubMed1984

Intestinal maturation: effect of growth retardation on L-valine absorption.

The absorption of L-valine was studied in segments of the jejunum and ileum using a one pass in situ perfusion technique in 1-, 2-, 3-, and 4-wk-old healthy control and in growth-retarded rats (suckled with mothers fed a protein-deficient diet and fed the same diet after weaning). In the jejunum of control rats, rate of absorption of L-valine declined from about 270 to 80 mumol/h per g mucosal weight, between 2 and 4 wk of life. At each age period, in both segments, rates of absorption of L-valine based on weight of the segments were significantly greater in the growth-retarded than in the control rats. However, based on length of the intestinal segments rates of absorption were similar in corresponding segments of the control and growth-retarded rats. These findings indicated that although the intestine in the growth-retarded rats was atrophic compared to that in control rats, the capability to absorb L-valine had been preserved, by increasing the rate of absorption per unit weight of intestine.

Animals↗
PubMed1995

Three conserved glycine residues in valine activation of gramicidin S synthetase 2 from Bacillus brevis.

The translated product from the gene fragment containing the second and third domains of gramicidin S synthetase 2 was purified to an essentially homogeneous state. It showed valine- and ornithine-activating activity and the second domain was proved to be the valine-activating domain. Three mutant genes from Bacillus brevis Nagano, BI-3, E-4, and E-5 strains, which encode defective valine-activating domains of gramicidin S synthetase 2, were sequenced. By comparison with the wild-type gene, single point mutations of guanine to adenine were found at the three conserved glycine codons; the 5303rd guanine in BI-3, the 5378th guanine in E-4, and the 4967th guanine in E-5, which corresponded to codon changes of the 1768th glycine to glutamic acid and the 1793rd and the 1656th glycine to aspartic acid. Loss of valine-adenylation activity by mutation at the 1656th glycine proved the direct participation of the TSGT/STGXPKG motif in the adenylation reaction, and suggests that this glycine residue with the conserved lysine residue of the motif forms the phosphate-binding loop for ATP-binding. The 1793rd glycine is a member of the YGXTE motif which was also conserved among adenylate-forming enzymes except acetyl-CoA synthetases. The 1768th glycine residue appears to maintain the conformation of the active site for aminoacyl adenylation since this residue is retained among the adenylate-forming enzymes, though flanking regions are not conserved. These results suggest that these glycine residues are essential for adenylate formation in the antibiotic peptide synthetase family and some other adenylate-forming enzymes.

Amino Acid Isomerases↗
PubMed1975

Effects of excess intake of leucine and valine deficiency on tryptophan and niacin metabolites in humans.

Nineteen healthy humans (2 men and 17 women) served as experimental subjects in 4 experiments using diets having different levels of leucine and also a valine-deficient diet. The effect of an excess intake of leucine, with and without addition of vitamin B-6, and the effect of a deficiency of valine on urinary excretions of N1-methylnicotinamide, N1-methyl-2-pyridone-5-carboxamide, nicotinic acid, quinolinic acid, and 5-hydroxyindole acetic acid, and on the level of plasma amino acids were investigated. There was no effect of leucine on the excretion of these metabolites, but a marked decrease in the plasma (or serum) valine level was observed. The same decrease was seen when a valine-deficient diet was fed.

Adult↗
PubMed1985

Comparison of in vitro jejunal uptake of L-valine and L-lysine in the rat during maturation.

The maturational characteristics and patterns of absorption of the neutral amino acid L-valine were compared with those of the basic amino acid L-lysine using in vitro preparations of everted sacs obtained from the jejunum of suckling (2 weeks old), weanling (3 weeks old), and adolescent (6 weeks old) rats. Absorption rates determined as net transport into sac fluid and mucosal uptake (mumol/h/g protein or weight of mucosal scrapings) for both valine and lysine were greater in the suckling than in the weanling or adolescent rats. This appeared to be true for both the carrier-mediated and the diffusive processes for absorption, determined from the relationship between the observed absorption rates and the corresponding mucosal incubation medium amino acid concentrations. The major decline in rate of absorption occurred before the period of weaning. Between the period of suckling and adolescence the carrier-mediated absorption decreased by 55% for valine and by 90% for lysine, suggesting that during maturation of the jejunum the number of the carrier macromolecules responsible for absorption of valine and lysine per unit protein or weight of mucosa decreases with increasing age.

Age Factors↗
PubMed2005

Synthesis and X-ray crystal structure study of the hydroxyurea and hydantoin derivatives of L-valine.

The novel hydroxyurea 5 derivative of L-valine was prepared by aminolysis of N-(1-benzotriazolecarbonyl)-L-valine cyclohexanemethylamide 4 with hydroxylamine. The corresponding hydantoin derivative 6 was synthesized by base catalyzed cyclization of the amide 4. The exact stereostructure of hydantoin derivative 6 has been determined by X-ray crystal structure analysis. The chiral atom of the hydantoin ring in 6 has S configuration what is in agreement with its configuration in the starting L-valine. The molecules of 6 are joined into infinite chains by N-H...O intermolecular hydrogen bond. The infinite chains are additionally linked by two C-H...O hydrogen bonds, thus forming two-dimensional network. The hydantoin derivative of L-valine 6 and its L-leucine analogue LH have similar packing arrangements, so they are homostructural.

Crystallography, X-Ray↗
PubMed1983

Isoleucyl-tRNA synthetase from Baker's yeast. Catalytic mechanism, 2',3'-specificity and fidelity in aminoacylation of tRNAIle with isoleucine and valine investigated with initial-rate kinetics using analogs of tRNA, ATP and amino acids.

The aminoacylation of three modified tRNAIle species with isoleucine and with valine by isoleucyl-tRNA synthetase has been investigated by initial rate kinetics. For aminoacylation of tRNAIle-C-C-3'dA with isoleucine, a bi-bi uni-uni ping-pong mechanism has been found by bisubstrate kinetics and inhibition by products and by 3'dATP; for aminoacylation with valine a bi-uni uni-bi ping-pong mechanism. For isoleucylation of tRNAIle-C-C-A(3'NH2) bisubstrate kinetics, inhibition by products and by isoleucinol show a random uni-bi uni-uni-uni ping-pong mechanism; for valylation of this tRNA a bi-bi uni-uni ping-pong mechanism is observed by bisubstrate kinetics and product inhibition. tRNAIle-C-C-2'dA was aminoacylated under modified conditions with isoleucine in a bi-bi uni-uni ping-pong mechanism with a rapid equilibrium segment as observed by bisubstrate kinetics, inhibition by AMP, by P[NH]P as product analog and by isoleucinol. Aminoacylation with valine is achieved in a rapid-equilibrium sequential random AB, ordered C mechanism indicated by bisubstrate kinetics and inhibition by 3'dATP and valinol. All six reactions exhibit orders of substrate addition and product release which are different from those observed in aminoacylation of the natural tRNAIle-C-C-A. The Km values of the three substrates and the kcat values of the six reactions are given. For aminoacylation at the terminal 2'OH group of the tRNA differences of 13.38 and 13.17 kJ in binding energies between valine and isoleucine have been calculated which result in discrimination factors of 181 and 167. For aminoacylation at the terminal 3'-OH group a difference of only 4.43 kJ and a low discrimination factor of only 6 is observed. Thus maximal discrimination between the cognate and the noncognate amino acid is only achieved in aminoacylation at the 2'-OH group and conclusions drawn from experiments with modified tRNAs concerning 2',3'-specificity have led to correct results in spite of different catalytic cycles in aminoacylation of the natural and the modified tRNAs. The stability of Ile-tRNAIle-C-C-2'dA and Val-tRNAIle-C-C-2'dA, the lesser stability of Val-tRNAVal-C-C-2'dA and the instability of Thr-tRNAVal-C-C-2'dA are consistent with postulations for a 'pre-transfer' proofreading step for isoleucyl-tRNA synthetase and a 'post-transfer' hydrolytic editing step for valyl-tRNA synthetase at the terminal 3'OH group of the tRNA.

Amino Acyl-tRNA Synthetases↗
PubMed2002

Linking central metabolism with increased pathway flux: L-valine accumulation by Corynebacterium glutamicum.

Mutants of Corynebacterium glutamicum were made and enzymatically characterized to clone ilvD and ilvE, which encode dihydroxy acid dehydratase and transaminase B, respectively. These genes of the branched-chain amino acid synthesis were overexpressed together with ilvBN (which encodes acetohydroxy acid synthase) and ilvC (which encodes isomeroreductase) in the wild type, which does not excrete L-valine, to result in an accumulation of this amino acid to a concentration of 42 mM. Since L-valine originates from two pyruvate molecules, this illustrates the comparatively easy accessibility of the central metabolite pyruvate. The same genes, ilvBNCD, overexpressed in an ilvA deletion mutant which is unable to synthesize L-isoleucine increased the concentration of this amino acid to 58 mM. A further dramatic increase was obtained when panBC was deleted, making the resulting mutant auxotrophic for D-pantothenate. When the resulting strain, C. glutamicum 13032DeltailvADeltapanBC with ilvBNCD overexpressed, was grown under limiting conditions it accumulated 91 mM L-valine. This is attributed to a reduced coenzyme A availability and therefore reduced flux of pyruvate via pyruvate dehydrogenase enabling its increased drain-off via the L-valine biosynthesis pathway.

Biological Transport↗
PubMed1972

Enzymes of the isoleucine-valine pathway in Acinetobacter.

Regulation of four of the enzymes required for isoleucine and valine biosynthesis in Acinetobacter was studied. A three- to fourfold derepression of acetohydroxyacid synthetase was routinely observed in two different wild-type strains when grown in minimal medium relative to cells grown in minimal medium supplemented with leucine, valine, and isoleucine. A similar degree of synthetase derepression was observed in appropriately grown isoleucine or leucine auxotrophs. No significant derepression of threonine deaminase or transaminase B occurred in either wild-type or mutant cells grown under a variety of conditions. Three amino acid analogues were tested with wild-type cells; except for a two- to threefold derepression of dihydroxyacid dehydrase when high concentrations of aminobutyric acid were added to the medium, essentially the same results were obtained. Experiments showed that threonine deaminase is subject to feedback inhibition by isoleucine and that valine reverses this inhibition. Cooperative effects in threonine deaminase were demonstrated with crude extracts. The data indicate that the synthesis of isoleucine and valine in Acinetobacter is regulated by repression control of acetohydroxyacid synthetase and feedback inhibition of threonine deaminase and acetohydroxyacid synthetase.

Alcaligenes↗
PubMed1974

Role of the leu-3 cistron in the regulation of the synthesis of isoleucine and valine biosynthetic enzymes of Neurospora.

The production by Neurospora of the enzymes of isoleucine and valine synthesis in response to specific end product-derived signals depends upon the presence of an effective leu-3 regulatory product and its effector alpha-isopropylmalate (alpha-IPM). In leu-3(+) strains, threonine deaminase production is repressed as a function of available isoleucine, acetohydroxy acid synthetase as a function of valine, and the isomeroreductase and dihydroxy acid dehydratase as a function of isoleucine and leucine. In the absence of an effective leu-3 regulatory product, alpha-isopropylmalate, or both, the production of isoleucine and valine biosynthetic enzymes is fixed at or near fully repressed levels even under conditions of severe end product limitation. Thus, in addition to its involvement in the regulation of expression of the three structural genes of leucine synthesis, the leu-3 alpha-IPM regulatory product is necessary for full expression of at least four genes specifying the structure of the enzymes of isoleucine and valine synthesis. It is suggested that the leu-3 alpha-IPM regulatory element may facilitate transcription of the genetically dispersed cistrons either by imposing specificity on ribonucleic acid polymerase for structurally similar promoters adjacent to each of the cistrons or by "opening" promoters after interaction with nearly identical stretches of deoxyribonucleic acid near each of the structural genes.

Alcohol Oxidoreductases↗
PubMed1979

Transaminase B from Escherichia coli: quaternary structure, amino-terminal sequence, substrate specificity, and absence of a separate valine-alpha-ketoglutarate activity.

Transaminase B (branched-chain amino acid aminotransferase, EC 2.6.1.42), the ilvE gene product, was purified to apparent homogeneity from an Escherichia coli K-12 strain which carries the ilvE gene both on the host chromosome and on a plasmid. The oligomeric structure of the enzyme, as determined by analytical ultracentrifugation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was confirmed to be that of a hexamer with a molecular weight of about 182,000 and apparently identical subunits. Cross-linking with dimethylsuberimidate yielded trimers, dimers, and monomers, but essentially no species of higher molecular weight. These results are consistent with a double-trimer arrangement of the subunits in native enzyme. The amino-terminal sequence was found to be: Gly Thr Lys Lys Ala Asp Tyr Ile (Trp) Phe Asn Gly (Thr) (Met) Val. Purified transaminase B catalyzed transamination between alpha-ketoglutarate and l-isoleucine, l-leucine, l-valine, and, to a lesser extent, l-phenylalanine and l-tyrosine, the latter reacting very sluggishly. The enzyme was free of aspartate transaminase and of transaminase C. The apparent K(m) values for the branched-chain alpha-ketoacids were smaller than those for the corresponding amino acids. The lowest K(m) was recorded for dl-alpha-keto-beta-methyl-n-valerate, and the highest was recorded for l-valine. The ratio of the valine- and isoleucine-alpha-ketoglutarate activities did not change significantly during purification, and both activities were quantitatively removed from crude extract by antibody raised against purified transaminase B. These observations argue against the existence of a separate valine-alpha-ketoglutarate transaminase. Anti-E. coli transaminase B antibody cross-reacted with crude extract from Salmonella typhimurium, but not with extract obtained from Pseudomonas aeruginosa.

Amino Acid Sequence↗
PubMed1961

Role of valine and isoleucine as regulators of actinomycin peptide formation by Streptomyces chrysomallus.

Katz, Edward (Rutgers, The State University, New Brunswick, N. J.), Clarence R. Waldron, and Mary Lou Meloni. Role of valine and isoleucine as regulators of actinomycin peptide formation by Streptomyces chrysomallus. J. Bacteriol. 82:600-608. 1961-d-Valine is an effective inhibitor of actinomycin synthesis by Streptomyces chrysomallus; l-valine stimulates actinomycin production and reverses the inhibition due to the d-enantiomorph. The incorporation of l-valine into the medium results, particularly, in a marked increase in actinomycin IV formation. In studies with various isoleucine isomers it was shown that l-isoleucine enhances actinomycin VII production; the principal effect of d-alloisoleucine and, especially, d-isoleucine, is to bring about synthesis of two new actinomycins which contain N-methylisoleucine. Both l- and d-threonine were observed to have an effect similar to that obtained with l-isoleucine. An interpretation of these findings has been discussed.

Amino Acids↗
PubMed1969

Control of isoleucine, valine, and leucine biosynthesis. VI. Effect of 5',5',5'-trifluoroleucine on repression in Salmonella typhimurium.

The leucine analogue 5',5',5',-trifluoroleucine (fluoroleucine) replaced leucine for repression of the isoleucine-valine biosynthetic enzymes in Salmonella typhimurium. In contrast, the analogue had no effect on derepression of the leucine biosynthetic enzymes in leucine auxotrophs grown on limiting amounts of leucine. The effect of fluoroleucine on repression appeared to be specific for leucine since derepression of the isoleucine-valine enzymes due to an isoleucine or valine limitation was not affected by the analogue. The prevention of derepression by fluoroleucine was probably due to repression and not to the formation of false proteins, since the analogue had no effect on the derepression of a number of enzymes unrelated to the isoleucine-valine pathway. Fluoroleucine was able to attach to leucine transfer ribonucleic acid (tRNA) as evidenced by the ability of the analogue to protect about 70% of leucine tRNA from oxidation by periodate. We propose that the differential effects of fluoroleucine on repression are due to differences in the ability of the analogue to bind to the various species of leucine tRNA.

Acyltransferases↗
PubMed1993

Poliovirus capsid proteins derived from P1 precursors with glutamine-valine cleavage sites have defects in assembly and RNA encapsidation.

Assembly of poliovirus virions requires proteolytic cleavage of the P1 capsid precursor polyprotein between two separate glutamine-glycine (QG) amino acid pairs by the viral protease 3CD. In this study, we have investigated the effects on P1 polyprotein processing and subsequent assembly of processed capsid proteins caused by substitution of the glycine residue at the individual QG cleavage sites with valine (QG-->QV). P1 cDNAs encoding the valine substitutions were created by site-directed mutagenesis and were recombined into wild-type vaccinia virus to generate recombinant vaccinia viruses which expressed the mutant P1 precursors. The recombinant vaccinia virus-expressed mutant P1 polyproteins were analyzed for proteolytic processing defects in cells coinfected with a recombinant vaccinia virus (VVP3) that expresses the poliovirus 3CD protease and for processing and assembly defects by using a trans complementation system in which P1-expressing recombinant vaccinia viruses provide capsid precursor to a defective poliovirus genome that does not express functional capsid proteins (D. C. Ansardi, D. C. Porter, and C. D. Morrow, J. Virol. 67:3684-3690, 1993). The QV-substituted precursors were proteolytically processed at the altered sites both in cells coinfected with VVP3 and in cells coinfected with defective poliovirus, although the kinetics of cleavage at the altered sites were slower than those of cleavage at the wild-type QG site in the precursor. Completely processed capsid proteins VP0, VP3, and VP1 derived from the mutant precursor containing a valine at the amino terminus of VP3 (VP3-G001V) were unstable and failed to assemble stable subviral structures in cells coinfected with defective poliovirus. In contrast, capsid proteins derived from the P1 precursor with a valine substitution at the amino terminus of VP1 (VP1-G001V) assembled empty capsid particles but were deficient in assembling RNA-containing virions. The assembly characteristics of the VP1-G001V mutant were compared with those of a previously described VP3-VP1 cleavage site mutant (K. Kirkegaard and B. Nelsen, J. Virol. 64:185-194, 1990) which contained a deletion of the first four amino-terminal residues of VP1 (VP1-delta 1-4) and which was reconstructed for our studies into the recombinant vaccinia virus system. Complete proteolytic processing of the VP1-delta 1-4 precursor also occurred more slowly than complete cleavage of the wild-type precursor, and formation of virions was delayed; however, capsid proteins derived from the VP1-G001V mutant assembled RNA-containing virions less efficiently than those derived from the VP1-delta 1-4 precursor.(ABSTRACT TRUNCATED AT 400 WORDS)

3C Viral Proteases↗
PubMed1992

Flooding with L-[1-13C]leucine stimulates human muscle protein incorporation of continuously infused L-[1-13C]valine.

To investigate why flooding methods give higher rates than constant-infusion methods for muscle protein synthesis, we studied seven healthy postabsorptive male volunteers (20-42 yr; 67-74 kg) during a 7.5-h primed constant infusion of L-[1-13C]valine (99 atoms %, 1.5 mg/kg prime, 1.5 mg.kg-1.h-1); at 6.5 h they were given a flood of L-[1-13C]leucine (20 atoms %, 0.05 g/kg). Musculus tibialis anterior biopsies were taken at 0.5, 6, and 7.5 h, and blood was sampled as appropriate. The enrichment of valine and leucine in muscle protein (isotope ratio mass spectrometry of protein amino acid-derived 13CO2) was compared with the average enrichment of various amino acid pools (gas chromatography-mass spectrometry). During infusion of [13C] valine the rate of muscle protein synthesis measured using alpha-ketoisovalerate (alpha-KIV) as precursor surrogate was 0.043 +/- 0.002%/h (SE). After flooding with leucine, the incorporation rate of [13C]valine increased by 70% (P less than 0.05), i.e., apparent muscle protein synthetic rate (based on alpha-[13C]KIV) increased to 0.065 +/- 0.009%/h (P less than 0.05); the rate calculated from the [13C]leucine flood was 0.060 +/- 0.005%/h (P less than 0.01). The synthetic rates calculated using the constant-infusion method were higher after flooding, irrespective of the precursor chosen, raising serious concern about the validity of the flooding-dose method.

Adult↗
PubMed1983

Postnatal increase in the metabolism of leucine and valine.

The catabolism of tritium-labeled leucine, valine, and glycine was determined by measuring the appearance of tritium-labeled water at various postnatal and adult ages in rats. Results for leucine and valine show a marked increase in the formation of labeled water during the 3rd postnatal week. The partial exclusion of leucine and valine from brain, as a result of the blood-brain barrier, particularly enhances observation of labeled water formation in that the product (water) and precursor (amino acid) are largely separated (supporting experiments demonstrate the prior existence of the blood-brain barrier for leucine). Results for glycine indicate its extensive metabolic degradation at all postnatal ages. These data indicate that the metabolic rate of intraperitoneally administered, radioactively labeled leucine and valine changes appreciably during early postnatal development. The early postnatal manifestation of human disorders of branched-chain amino acid metabolism is consistent with the chronology of development in the rat.

Age Factors↗