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PubMed1989

Quantitative measurements of regional glucose utilization and rate of valine incorporation into proteins by double-tracer autoradiography in the rat brain tumor model.

We examined the rate of glucose utilization and the rate of valine incorporation into proteins using 2-[18F]fluoro-2-deoxyglucose and L-[1-14C]-valine in a rat brain tumor model by quantitative double-tracer autoradiography. We found that in the implanted tumor the rate of valine incorporation into proteins was about 22 times and the rate of glucose utilization was about 1.5 times that in the contralateral cortex. (In the ipsilateral cortex, the tumor had a profound effect on glucose utilization but no effect on the rate of valine incorporation into proteins.) Our findings suggest that it is more useful to measure protein synthesis than glucose utilization to assess the effectiveness of antitumor agents and their toxicity to normal brain tissue. We compared two methods to estimate the rate of valine incorporation: "kinetic" (quantitation done using an operational equation and the average brain rate coefficients) and "washed slices" (unbound labeled valine removed by washing brain slices in 10% trichloroacetic acid). The results were the same using either method. It would seem that the kinetic method can thus be used for quantitative measurement of protein synthesis in brain tumors and normal brain tissue using [11C]-valine with positron emission tomography.

Animals↗
PubMed1992

Isoleucine requirements of the chicken: the effect of excess leucine and valine on the response to isoleucine.

1. Three experiments were designed to determine the response of broiler chickens to dietary isoleucine, and to quantify the antagonistic effects of excess leucine and valine on this response. 2. A dilution technique was used to measure the responses in growth rate and food intake to a range of diets differing in their isoleucine concentrations. A summit diet was formulated to contain isoleucine at 1.14 times the requirement and with leucine (1.76 times the requirement) and valine (1.87 times the requirement) at the minimum possible concentrations, given the ingredients available. A dilution mixture, devoid of protein, was formulated to correspond in all respects, other than in amino acid content, to the summit diet. These two basal diets were blended in different proportions to give a range of diets of decreasing isoleucine and protein content. 3. In experiment 1 the response was measured to isoleucine with leucine and valine remaining in the same proportion to isoleucine throughout the range of diets fed. In experiments 2 and 3, however, L-leucine and L-valine were added to the diets either singly or in combination to give 6 isoleucine concentrations and 3 ratios of each of leucine and valine to isoleucine. 4. Weight gain decreased as the isoleucine content of the diet was reduced, whereas food intake of broilers fed on the marginally deficient diets increased to a maximum and then decreased. FCE decreased curvilinearly as the isoleucine concentration in the food decreased, reflecting a concomitant change in the fat content of the broilers. 5. It is possible that the amount of dietary isoleucine assumed to be available to the broilers in these experiments was overestimated by hydrolysing the food samples for 72 h, and the doubt thus created makes an estimate of the efficiency of retention of isoleucine suspect. 6. Excess valine had no effect on the response to isoleucine, whereas an increase in the leucine to isoleucine ratio depressed food intake and hence weight gain, but only at the lowest concentrations of isoleucine. 7. If the food content of isoleucine is sufficient to meet the requirements of the broiler, relatively large excesses of leucine, of valine, or of both will not depress growth.

Animal Feed↗
PubMed1991

Branched-chain amino acid interactions with reference to amino acid requirements in adult men: valine metabolism at different leucine intakes.

We explored whether the oxidation of valine and by implication the physiological requirement for this amino acid are affected by changes in leucine intake over a physiological range. Six young adult men received, in random order, four L-amino acid-based diets for 5 d supplying either 20 or 10 mg valine.kg body wt-1.d-1, each in combination with 80 or 40 mg leucine.kg-1.d-1. On day 6 subjects were studied with an 8-h continuous intravenous infusion of [1-13C]valine (and [2H3]leucine) to determine valine oxidation in the fasted state (first 3 h) and fed state (last 5 h). Valine oxidation in the fasted state was similar among all diets but was lower (P less than 0.05) in the fed state for the 10 vs 20 mg valine.kg-1.d-1 intake. Leucine intake did not affect valine oxidation. Mean daily valine balance approximated +1.3 mg.kg-1.d-1 for the 20-mg intake and -1.6 mg.kg-1.d-1 for the 10-mg intake. These findings support our previously suggested mean valine requirement estimate of approximately 20 mg.kg-1.d-1.

Adult↗
PubMed1978

The neurotoxicity of valine deficiency in rats.

When valine, an essential amino acid, was withdrawn from the diet of weanling rats, the animals rapidly developed a unique pattern of neurological symptoms characterized by head retraction, staggering and aimless circling. At necropsy degenerative changes were most prominent in the neurons of the red nuclei, brain stem structures which modulate motor function. To explore the pathogenesis of the neurotoxicity associated with valine deficiency, we fed rats purified diets deficient in valine alone or in valine plus other branched chain and neutral amino acids, and we examined brain tissues by light microscopy. Motor disfunction and red nuclei damage occurred only in rats fed diets lacking valine alone and not in rats fed diets lacking all three branched chain amino acids. These results suggest that the neurotoxicity of valine deficiency results from amino acid imbalance rather than from lack of dietary valine per se.

Animals↗
PubMed1991

Conformational equilibria of valine studied by dynamics simulation.

The conformational probability distribution of a valine residue in the valine dipeptide and of the valine side chain in an alpha-helix, as well as the change in helix stability for replacing alanine with valine, has been calculated by molecular dynamics simulations of explicitly hydrated systems: dipeptide, tetrapeptide and 10-, 14- and 18-residue oligoalanine helices. All computed free-energy differences are means from at least eight separate slow-growth simulations, four in each direction and are reported with their root-mean-square deviations. Different values for the change in free energy of folding (delta delta G degrees) have been calculated with the use of forcefields having an all-atom and a central-atom representation of methyl groups, etc. The value obtained with the all-atom forcefield agrees well with new experimental values (3 kJ/mol = 0.7 kcal/mol). Furthermore, the most stable valine side-chain rotamer in the helix is different for these two representations. The most stable rotamer for the all atom conformation is the same one that predominates for valines in alpha-helices in proteins of known conformation. The lower conformational freedom of the valine side chain in the helix contributes 1 kJ/mol to the difference in stability computed with the all-atom potential; unfavorable interactions of the side chain with helix, even in the most stable conformation, further increase delta delta G degrees.

Alanine↗
PubMed1970

Metabolism of valine by the filamentous fungus Arthrobotrys conoides.

Uptake of valine by Arthrobotrys conoides was an active process and was independent of its incorporation into cellular protein. Chemical fractionation of cells supplied with (14)C-l-valine for different time intervals revealed that the amino acid initially entered a pool of metabolic intermediates and was extractable with cold trichloroacetic acid. After a 4-min interval, some intracellular valine was incorporated into cell proteins, but most underwent metabolic transformation to a variety of products that included carboxylic acids and other amino acids. Carbon derived from valine was not localized in the lipid or nucleic acid fraction of cells, but some was completely oxidized and recovered as metabolic (14)CO(2). Autoradiograms of paper and thin-layer chromatograms of acid hydrolysates of cellular protein identified the following amino acids as having originated from valine: glutamate, aspartate, alanine, and leucine. Similar analysis of cold trichloroacetic acid extracts established that (14)C supplied as l-valine had been transformed also to alpha-ketoisovalerate, isobutyrate, propionate, succinate, malate, oxalacetate, pyruvate, and alpha-ketoglutarate. Pathways for transformation of the carbon skeleton of valine to various metabolic products are proposed.

Alanine↗
PubMed1971

Multivalent repression and genetic depression of isoleucine-valine biosynthetic enzymes in Serratia marcescens.

The regulation of the formation of isoleucine-valine biosynthetic enzymes was examined to elucidate the mechanism of isoleucine-valine accumulation by alpha-aminobutyric acid-resistant (abu-r) mutants of Serratia marcescens. In the isoleucine-valine auxotroph, l-threonine dehydratase, acetohydroxy acid synthetase, and transaminase B were repressed when isoleucine, valine, and leucine were simultaneously added to minimal medium. These enzymes were derepressed at the limitation of any single branched-chain amino acid. Pantothenate, which stimulated growth of this auxotroph, had no effect on the enzyme levels. It became evident from these results that in S. marcescens isoleucine-valine biosynthetic enzymes are subject to multivalent repression by three branched-chain amino acids. The abu-r mutants had high enzyme levels in minimal medium, with or without three branched-chain amino acids. Therefore, in abu-r mutants, isoleucine-valine biosynthetic enzymes are genetically derepressed. This derepression was considered to be the primary cause for valine accumulation and increased isoleucine accumulation.

Cell-Free System↗
PubMed1974

Mutations affecting the different transport systems for isoleucine, leucine, and valine in Escherichia coli K-12.

Uptake of isoleucine, leucine, and valine in Escherichia coli K-12 is due to several transport processes for which kinetic evidence has been reported elsewhere. A very-high-affinity transport process, a high-affinity transport process, and three different low-affinity transport processes were described. In this paper the existence of these transport processes is confirmed by the isolation and preliminary characterization of mutants altered in one or more of them. The very-high-affinity transport process is missing either in strains carrying the brnR6(am) mutation or in strains carrying the brn-8 mutation. This appears to be a pleiotropic effect since other transport systems are also missing. Mutant analysis shows that more than one transport system with high affinity is present. One of them, high-affinity 1, which needs the activity of a protein produced by the brnQ gene, transports isoleucine, leucine, and valine and is unaffected by threonine. The other, high-affinity 2, which needs the activity of a protein produced by the brnS gene, transports isoleucine, leucine, and valine; this uptake is inhibited by threonine which probably is a substrate. Another protein, produced by the brnR gene, is required for uptake through both high-affinity 1 and high-affinity 2 transport systems. The two systems therefore appear to work in parallel, brnR being a branching point. The brnQ gene is located close to phoA at 9.5 min on the chromosome of E. coli, the brnR gene is located close to lac at 9.0 min, and the brnS gene is close to pdxA at 1 min. A mutant lacking the low-affinity transport system for isoleucine was isolated from a strain in which the high-affinity system was missing because of a brnR mutation. This strain also required isoleucine for growth because of an ilvA mutation. The mutant lacking the low-affinity transport system was unable to grow on isoleucine but could grow on glycylisoleucine. This mutant had lost the low-affinity transport for isoleucine, whereas those for leucine and valine were unaffected. A pleiotropic consequence of this mutation (brn-8) was a complete absence of the very-high-affinity transport system due either to the alteration of a common gene product or to any kind of secondary interference which inhibits it. Mutants altered in isoleucine-leucine-valine transport were isolated by taking advantage of the inhibition that valine exerts on the K-12 strain of E. coli. Mutants resistant both to valine inhibition (Val(r)) and to glycylvaline inhibition are regulatory mutants. Val(r) mutants that are sensitive to glycylvaline inhibition are transport mutants. When the very-high-affinity transport process is repressed (for example by methionine) the frequency of transport mutants among Val(r) mutants is higher, and it is even higher if the high-affinity transport process is partially inhibited by leucine.

Alanine↗
PubMed1975

Effect of a leu-linked mutation on the valine sensitivity of acetohydroxy acid synthase activity in Escherichia coli.

A spontaneous leu-linked mutation (ilvH2015) in Escherichia coli K-12 made the strain resistant to 1 mM valine and l mM glycylvaline (Val-r) and caused the isoleucine and valine biosynthetic enzyme, acetohydroxy acid synthase, to be less sensitive to feedback inhibition by valine than the wild-type enzyme. Transfer of the ilvDAC deletion into a strain carrying ilvH2015 abolished the effect of the marker on the acetohydroxy acid synthase and rendered it as sensitive to valine as the enzyme in the isogenic control strain without the Val-r marker under both repressing and limiting conditions. In contrast, auxotrophy caused by transfer of an ilvC lesion into the Val-r strain did not interfere with the effect of ilvH2015 on valine sensitivity of acetohydroxy acid synthase. In addition, the presence of the Val-r marker produced minor but significant pleiotropic effects on several other isoleucine and valine biosynthetic enzymes but did not cause derepression of the ilv gene cluster. These studies suggest some type of interaction between a product produced by a gene close to leu and the isoleucine and valine biosynthetic enzymes.

Chromosome Mapping↗
PubMed1966

Oxidation of D- and L-valine by enzymes of Pseudomonas aeruginosa.

Norton, J. E. (University of Oklahoma School of Medicine, Oklahoma City), and J. R. Sokatch. Oxidation of d- and l-valine by enzymes of Pseudomonas aeruginosa. J. Bacteriol. 92:116-120. 1966.-Cell-free extracts prepared from Pseudomonas aeruginosa grown on dl-valine catalyzed the consumption of oxygen with several d-amino acids, but not with the corresponding l-amino acids. The product of d-valine oxidation was identified as 2-oxoisovalerate by the preparation and characterization of 2-oxoisovalerate 2,4-dinitrophenylhydrazone. The enzyme catalyzing d-amino acid oxidation was present in extracts of cells grown on valine, but not on glucose, had a pH optimum of approximately 9.0, consumed 1 atom of oxygen per mole of keto acid produced, and was not stimulated by any of the usual electron transport cofactors. It was not possible to demonstrate either the direct oxidation of l-valine or the conversion of l- to d-valine by these enzyme preparations. However, a possible route of l-valine metabolism by transamination with 2-oxoglutarate with regeneration of the amino group acceptor by glutamate oxidation was established by identification of the transaminase and l-glutamate dehydrogenase in these enzyme preparations.

Amino Acids↗
PubMed2000

Effects of dietary valine concentration on lactational performance of sows nursing large litters. NCR-42 Committe on Swine Nutrition.

A cooperative study, using 231 primiand multiparous crossbred sows from six experiment stations (IN, KS, MI, MN, ND, and OH), was conducted to determine the effects of elevating dietary valine concentration in corn-soybean meal diets on lactational performance of sows nursing large litters. Crossbred sows were fed diets containing a minimum of .60% lysine during gestation. Sows were allotted at farrowing to four dietary valine concentrations, .80, .95, 1.10, and 1.25%. Crystalline L-valine replaced cornstarch to maintain a constant ratio of corn:soybean meal across diets. Dietary lysine, provided by corn, soybean meal, and .15% crystalline L-lysine x HCl, was .90% in all diets. Sows were allowed ad libitum access to feed. Sows were weighed within 24 h after farrowing, and all litters were adjusted to > or = 10 pigs/litter by d 2 following farrowing. Average sow parity, number of pigs on d 2, and lactation length for the four treatments were, respectively, 2.3, 2.3, 2.3, 2.5; 10.9, 10.8, 10.8, 10.7; and 25.1, 24.5, 25.2, 25.0 d. The ADFI during lactation was 5.87, 5.77, 5.87, and 5.74 kg (P > .50); hence, valine intakes were 41, 48, 55, and 61 g/d (linear, P < .01). Lysine intake ranged from 51.5 to 52.7 g/d (P > .50). Sow weight after farrowing averaged 198 kg (P > .60). Overall pig survival to weaning was high (>92%), and the number of pigs weaned (10.1, 10.3, 10.3, 10.3) did not differ (P > .30) among treatments. Litter weaning weights (73.6, 73.6, 74.5, 72.6 kg), litter weight gains (55.1, 55.1, 56.0, 54.1 kg), sow weight change during lactation (-4.9, -5.4, -4.8, -6.3 kg), and return-to-estrus interval (7.5, 6.4, 6.9, 8.2 d) were not affected (P > .30) by dietary valine. There were no station x treatment interactions (P > .50). These results indicate no benefit of elevated dietary valine for lactating sows nursing > or = 10 pigs and consuming a corn-soybean meal diet containing .90% lysine and .80% valine.

Animal Feed↗
PubMed1992

Paramagnetic molecular centers in gamma-irradiated precipitates in the system AlCl3-DL-alpha-valine-NaOH.

Formation and stability of paramagnetic molecular centers were studied in AlCl3-NaOH-DL-alpha-valine by ESR spectroscopy. In Al3(OH)9(valine)1 x 3H2O gamma-irradiated at room temperature the valine radical [formula: see text] was detected. The radical was formed by abstraction of a hydrogen atom from the valine molecule coupled to the aluminum hydroxide matrix. Stability of the radical depended critically on structural properties of the aluminum hydroxide matrix. In aluminum hydroxide with the ratio (Al)/(Valine) = 20, either no paramagnetic species were detected (irradiation in air) or a singlet at g = 2.008 of 1.8 mT linewidth was detected (irradiation in vacuum) at room temperature. Primary paramagnetic species (gamma irradiation at 77 K) in Al3(OH)9(Val)1 x 3H2O are chloride paramagnetic centers and the primary neutral valine radical [formula: see text] It was formed by abstraction of the NH2 group from the valine molecule. With warming, this radical was not transformed to the radical (I).

Aluminum Chloride↗
PubMed2004

[Metabolic flux analysis of L-valine fermentation in Corynebacterium glutamicum].

In industrial fermentation of amino acids the cells are often forced to synthesize the biochemicals excessive of their physiological needs. The knowledge of metabolic networks and their regulation relevant usually come from biochemical research, especially from enzymology, not from engineering study. To enrich the knowledge of metabolic sub-network of L-valine syntheses for higher production of L-valine, Corynebacterium glutamicum AS1.495 and its genetic derivatives AA361, AAT231, AATV341 were used for metabolic flux analysis. AS1.495 is a leucine auxotrophic (Leu-), and the three derivatives carry additional mutations. AA361 contains D-aspartic acid-beta-hydroxamate supersensitive marker (Leu-, L-AAHss), AAT231 (Leu-, L-AAHss, 2-TAr) is D-aspartic acid-beta-hydroxamate supersensitive and 2-thiazole alanine resistant, and AAT341 (Leu-, L-AAHss, 2-TAr, Vd-) is a D-aspartic acid-beta-hydroxamate supersensitive, 2-thiazole alanine resistant and valine-decompose-ability imperfect (Vd-). The concentrations of extra-cellular metabolites were determined under sub-steady-state of the batch culture. The metabolic flux distribution maps of the four strains were obtained, compared and analyzed. Our analysis showed that the flux ratio of EMP and HMP from the glucose-6-phosphate had increased from 0.205 in the parental strain AS1.495 to 0.321 in the multiple-mutation strain AATV341; the flux ratio of L-valine synthesis branch and the rest branches from the pyruvate node increased from 0.188 in AS1.495 to 3.29 in AATV341; the flux of lactic acid synthesis branch decreased from 11.1 in AS1.495 to 1.16 in AATV341; the flux of L-valine synthesis branch increased from 5.37 in AS1.495 to 37.3 in AATV341; and the productivity of L-valine correspondently increased from 4 g/L in AS1.495 to 24.5 g/L in AATV341. These results indicate that the introduction of analog supersensitive marker L-AAH55 and/or analog resistant marker 2-TAr skew the metabolic flux towards the formation of L-valine. This study revealed the usefulness of the metabolic flux analysis as a tool for verification of existing production strains. The analysis may play an important role in helping us b to rationally re-design metabolism for further improvement of fermentation process.

Corynebacterium glutamicum↗
PubMed1976

[L-valine transport by the actinomycete Actinomyces species 26-115, the producer of actinomycin C].

Transport of L-valine by Actinomyces species 26-115, an organism producing actinomycin C depended on L-valine concentration in the medium and temperature and required a source of intrinsic energy. Km for L-valine transport was 3.5.10(-6)--6.0.10(-6) M. It somewhat differed from experiment to experiment. The above system transported also other neutral amino acids. L-isoleucine was a competing inhibitor of L-valine transport. The transport of L-valine was stereospecific. The activity of the transport system was regulated by the intracellular content of L-valine. Probably because of this the amino acid transport depended on the culture age, so far as the level of free valine in the mycelium at various stages of development was different.

Actinomyces↗
PubMed1977

[Source of valine for protein V biosynthesis in a producer of actinomycin C].

The specific activity of 14C-valine in valyl-tRNA formed during incubation of the actinomycin C-producing organism with 14C-valine was constant and lower than that of the whole cell pool. The constancy of the valyl-tRNA was indicative of the presence of a separate compartment for the valine pool used for protein biosynthesis. A lower specific activity of valine in valyl-tRNA as compared to that of the whole cell pool may be indicative of a low rate of valine metabolism in such separate compartment with exogenic 14-valine or a higher concentration of free valine in it as compared to the specific activity of this amino acid at average per cell.

Actinomyces↗
PubMed1989

A human tRNA gene cluster encoding the major and minor valine tRNAs and a lysine tRNA.

A human genomic DNA clone hybridizing to mammalian valine tRNA(IAC) contained a cluster of three tRNA genes. Two valine tRNA genes with anticodons of AAC and CAC, encoding the major and minor cytoplasmic valine tRNA isoacceptors, respectively, and a lysine tRNA(CUU) gene were identified by Southern blot hybridization and DNA sequence analysis of a 7.1-kb region. At least nine Alu family members were interspersed throughout the 18.5-kb human DNA fragment, with three Alu elements in the intergenic region between the valine tRNA(AAC) gene and the lysine tRNA gene. Each of the five Alu family members in the sequenced region can be categorized into one of the four Alu subfamilies. The coding regions of all three tRNA genes contain characteristic internal split promoter sequences and typical RNA polymerase III termination signals in the 3'-flanking regions. The tRNA genes are accurately transcribed by RNA polymerase III in a HeLa cell extract, since the RNase T1 fingerprints of the mature-sized tRNA transcription products are consistent with the structural genes. The lysine tRNA(CUU) gene was transcribed only slightly more efficiently than the valine tRNA(CAC) gene in the homologous in vitro transcription system. Surprisingly, the valine tRNA(CAC) gene was transcribed about eightfold more efficiently than the valine tRNA(AAC) gene, implicating the presence of a modulatory element in the upstream region flanking the tRNA(CAC) gene.

Base Sequence↗
PubMed1990

Purification of an inducible L-valine dehydrogenase of Streptomyces coelicolor A3(2).

Valine dehydrogenase (VDH) from Streptomyces coelicolor A3(2) was purified from cell-free extracts to apparent homogeneity. The enzyme had an Mr 41,000 in denaturing conditions and an Mr 70,000 by gel filtration chromatography, indicating that it is composed of two identical subunits. It oxidized L-valine and L-alpha-aminobutyric acid efficiently, L-isoleucine and L-leucine less efficiently, and did not act on D-valine. It required NAD+ as cofactor and could not use NADP+. Maximum dehydrogenase activity with valine was at pH 10.5 and the maximum reductive amination activity with 2-oxoisovaleric acid and NH4Cl was at pH 9. The enzyme exhibited substrate inhibition in the forward direction and a kinetic pattern with NAD+ that was consistent with a sequential ordered mechanism with non-competitive inhibition by valine. The following Michaelis constants were calculated from these data: L-valine, 10.0 mM; NAD+, 0.17 mM; 2-oxoisovalerate, 0.6 mM; and NADH, 0.093 mM. In minimal medium, VDH activity was repressed in the presence of glucose and NH4+, or glycerol and NH4+ or asparagine, and was induced by D- and L-valine. The time required for full induction was about 24 h and the level of induction was 2- to 23-fold.

Amino Acid Oxidoreductases↗
PubMed1980

Synthesis of proteins and RNA of the 60S ribosomal subunit in HeLa cells recovering from valine deprivation.

The synthesis of ribosomes in HeLa cells was studied during recovery from a 20-hour deprivation for valine. The rates of incorporation of labeled precursors into ribosomal pre-RNA, processed rRNA, total cellular proteins, and proteins of the 60S ribosomal subunit returned to normal or nearly normal levels immediately after restoration of valine to the medium. Specific proteins of the 60S ribosomal subunit, whose apparent net synthesis is reduced more than that of the other proteins of the 60S ribosomal subunit during valine deprivation, were no longer undersynthesized after valine was restored. This rapid recovery suggests that the apparent decrease in the net rate of synthesis of these ribosomal proteins during valine deprivation is effected at the translational or post-translational level. No evidence of significant synchrony in any particular stage of the cell cycle was observed after a 20-hr valine deprivation.

Cell Cycle↗