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PubMed2000

Tracer methodology in whole body and organ balance metabolic studies: plasma sampling is required. A study in post-absorptive rats using isotopically labeled arginine, phenylalanine, valine and leucine.

BACKGROUND AND AIMS: Radioactive and stable amino acid isotopes are frequently used in metabolic research. Blood cells contain amino acid transporters, which may influence tracer distribution in blood. The aim of this study was to determine whether plasma or whole blood specific activity or enrichment of amino acid tracers should be used in the calculation of whole body and organ production rates. METHODS: Seven male Wistar rats were infused with L-[2,3-(3)H]-Arginine, L-[2, 6-(3)H]-Phenylalanine, L-[3,4-(3)H]-Valine, and [L-[4,5-(3)H]-Leucine. Whole body and portal drained visceral, hepatic and renal production rates of arginine, phenylalanine, valine and leucine were determined in plasma and in whole blood. RESULTS: Amino acid tracers that equilibrate well between plasma and blood cells (for instance phenylalanine, valine and leucine) yield similar whole body production rates when whole blood or plasma is sampled. Also, organ production rates measured using these amino acid tracers are consistent. However, a discrepancy exists between the whole body production rate and the sum of PDV, hepatic and renal production rates. When tracers are used that do not equilibrate well between plasma and blood cells (for instance arginine) the use of whole blood specific activity in the calculations yield overestimations of whole body and organ production rates. CONCLUSION: From our data we recommend plasma sampling and strongly advise against whole blood sampling in metabolic organ balance studies in which amino acid tracers are used.

Amino Acids↗
PubMed2006

Dissociative electron attachment to gas phase valine: a combined experimental and theoretical study.

Using a crossed electron/molecule beam technique the dissociative electron attachment (DEA) to gas phase L-valine, (CH(3))(2)CHCH(NH(2))COOH, is studied by means of mass spectrometric detection of the product anions. Additionally, ab initio calculations of the structures and energies of the anions and neutral fragments have been carried out at G2MP2 and B3LYP levels. Valine and the previously studied aliphatic amino acids glycine and alanine exhibit several common features due to the fact that at low electron energies the formation of the precursor ion can be characterized by occupation of the pi* orbital of the carboxyl group. The dominant negative ion (M-H)(-) (m/Z=116) is observed at electron energies of 1.12 eV. This ion is the dominant reaction product at electron energies below 5 eV. Additional fragment ions with m/Z=100, 72, 56, 45, 26, and 17 are observed both through the low lying pi* and through higher lying resonances at about 5.5 and 8.0-9.0 eV, which are characterized as core excited resonances. According to the threshold energies calculated here, rearrangements play a significant role in the formation of DEA fragments observed from valine at subexcitation energies.

Computer Simulation↗
PubMed1974

Mechanism of renaturation of pyruvate kinase of Saccharomyces carlsbergensis: activation by L-valine and magnesium and manganese ions.

Pyruvate kinase (EC 2.7.1.40) of S. carlsbergensis is a tetrameric enzyme, composed of four identical subunits each of which contains 1 mole of L-valine noncovalently bound. The enzyme readily dissociates into monomeric units. L-Valine and magnesium or manganese ions are specific primers of the renaturation process of the enzyme. The amino acid induces renaturation with a K(0.5) of 17 muM and a pseudo first-order rate constant of 0.019 min(-1) at 25 degrees with respect to the monomeric species, indicating that L-valine influences the folding of the monomeric form from a disordered state to its native conformation being followed by a spontaneous reassociation with formation of the tetrameric enzyme. Independently, magnesium and manganese ions induce the renaturation with a first-order rate constant of the same magnitude.

Enzyme Activation↗
PubMed1981

Molecular basis of valine resistance in Escherichia coli K-12.

The relationship of valine resistance to the expression of the ilvGEDA operon of Escherichia coli K-12 has been determined. DNA sequence and in vivo protein analyses indicate that in wild-type E. coli K-12 there is a frameshift site within the gene (ilvG) for valine resistance. The ilvG+2096 (formerly designated ilv02096) mutation displaces this frameshift site, resulting in the expression of ilvG and the relief of transcriptional polarity on the distal genes of this operon. Thus, the "ilv0" mutation, which concomitantly confers valine resistance and increased expression of the ilvEDA genes, is, in fact, the "reversion" of a polar site within the first structural gene of the ilvGEDA operon.

Base Sequence↗
PubMed1988

Secretion in yeast of human lysozymes with different specific activities created by replacing valine-110 with proline by site-directed mutagenesis.

Computer graphics indicate that a steric hindrance exists between valine-110 side chain of human lysozyme (EC 3.2.1.17) and an acetyl group of a modified substrate that contains N6,O-diacetylmuramic acid. To alter the substrate specificity of human lysozyme to be effective on the modified substrate, we replaced the valine-110 residue with various amino acids by site-directed mutagenesis. One of the mutant proteins (valine residue replaced with proline:P110) was secreted in Saccharomyces cerevisiae as at least four components (P110-A, P110-B, P110-C, and P110-D) with different specific activities. Two components, P110-B and P110-D, were isolated in a pure form and structurally characterized. The results suggest that this mutation lowered the lytic activity against Micrococcus lysodeikticus by changing a local conformation of the catalytic site while keeping almost the same substrate binding sites. Our results also indicate that cis/trans isomerization of prolyl peptide bonds probably occurs in vivo and that the conformational change of protein as well as point mutations in genes might influence the molecular evolution of the protein.

Amino Acid Sequence↗
PubMed1989

Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation.

Site-directed mutants of cytochrome P-450cam (the cytochrome P-450 that acts as the terminal monooxygenase in the d-camphor monooxygenase system), in which threonine-252 had been changed to alanine, valine, or serine, were employed to study the role of the hydroxy amino acid in the monooxygenase reaction. The mutant enzymes were expressed in Escherichia coli and were purified by a conventional method. All the mutant enzymes in the presence of d-camphor exhibited optical absorption spectra almost indistinguishable from those of the wild-type enzyme in their ferric, ferrous, oxygenated, and carbon monoxide ferrous forms. In a reconstituted system with putidaredoxin and its reductase, the alanine enzyme consumed O2 at a rate (1100 per min per heme) comparable to that of the wild-type enzyme (1330 per min per heme), whereas the amount of exo-5-hydroxycamphor formed was less than 10% of that formed by the wild-type enzyme. About 85% of the O2 consumed was recovered as H2O2. The valine enzyme also exhibited an oxidase activity to yield H2O2 accompanied by a relative decrease in the monooxygenase activity. On the other hand, the serine enzyme exhibited essentially the same monooxygenase activity as that of the wild-type enzyme. Thus, uncoupling of O2 consumption from the monooxygenase function was produced by the substitution of an amino acid without a hydroxyl group. When binding of O2 to the ferrous forms was examined, the alanine and valine enzymes formed instantaneously an oxygenated form, which slowly decomposed to the ferric form with rates of 5.5 and 3.2 x 10(-3) sec-1 for the former and latter enzymes, respectively. Since these rates were too slow to account for the overall rates of O2 consumption, the formation of H2O2 was considered to proceed not by way of this route but through the decomposition of a peroxide complex formed by reduction of the oxygenated form by reduced putidaredoxin. Based on these findings, a possible mechanism for oxygen activation in this monooxygenase reaction has been discussed.

Alanine↗
PubMed1996

Aminoacylation identity switch of turnip yellow mosaic virus RNA from valine to methionine results in an infectious virus.

The turnip yellow mosaic virus genomic RNA terminates at its 3' end in a tRNA-like structure that is capable of specific valylation. By directed mutation, the aminoacylation specificity has been switched from valine to methionine, a novel specificity for viral tRNA-like structures. The switch to methionine specificity, assayed in vitro under physiological buffer conditions with wheat germ methionyl-tRNA synthetase, required mutation of the anticodon loop and the acceptor stem pseudoknot. The resultant methionylatable genomes are infectious and stable in plants, but genomes that lack strong methionine acceptance (as previously shown with regard to valine acceptance) replicate poorly. The results indicate that amplification of turnip yellow mosaic virus RNA requires aminoacylation, but that neither the natural (valine) specificity nor interaction specifically with valyl-tRNA synthetase is crucial.

Kinetics↗
PubMed2001

The carboxyl-terminal valine is required for transport of glycoprotein CD8 alpha from the endoplasmic reticulum to the intermediate compartment.

There is evidence that a carboxyl-terminal valine residue is an anterograde transport signal for type I transmembrane proteins. Removal of the signal would either delay glycosylation in the Golgi complex of proteins destined to recycle to the endoplasmic reticulum or determine accumulation in the endoplasmic reticulum of newly synthesized proteins destined for the plasma membrane. We used the human CD8 alpha glycoprotein to investigate the role of the carboxyl-terminal valine in the exocytic pathway. Using immunofluorescence light microscopy, metabolic labeling, and cell fractionation, we demonstrate that removal of the carboxyl-terminal valine residue delays transport of CD8 alpha from the endoplasmic reticulum to the intermediate compartment. Removal of the residue did not affect the other steps of the exocytic pathway or the folding/dimerization and glycosylation processes. Therefore, it is likely that this signal plays a role in the transport of CD8 alpha from the endoplasmic reticulum to the intermediate compartment either before or during the formation of the transport vesicles that drive the exit the protein from the endoplasmic reticulum.

Amino Acid Sequence↗
PubMed1975

Amino acid requirements of the young turkey: leucine, isoleucine and valine.

1. The leucine, isoleucine and valine requirements of the 3-week-old turkey were determined in a factorial experiment and were found to be 1-42, 0-84 and 1-21% respectively in semi-purified diets containing 12-5 MJ ME/kg. 2. It is suggested that the efficiency with which turkeys and chicks utilise isoleucine and valine is similar, and that a daily intake of about 325 mg of valine would sustain a rate of growth of about 23 g/d in both species.

Animals↗
PubMed1997

Biological fate of sulphur mustard: identification of valine and histidine adducts in haemoglobin from casualties of sulphur mustard poisoning.

1. Analytical methods were developed for the detection of N-terminal valine and histidine adducts in haemoglobin alkylated with sulphur mustard. 2. N-(2-hydroxyethylthioethyl)-N-terminal valine was selectively cleaved from globin with the Edman reagent pentafluorophenyl isothiocyanate. The resulting thiohydantoin derivative was analysed by high resolution gc-ms using negative ion chemical ionization. An alternative procedure, involving acid hydrolysis of globin to its constituent amino acids and conversion of the adduct to its di-TBDMS derivative, was less sensitive. 3. N-(2-hydroxyethylthioethyl)histidine was analysed, after acid hydrolysis of globin, as its fluorenylmethyloxycarbonyl derivative by lc-ms-ms using electrospray ionisation and selected reaction monitoring. 4. N-(2-hydroxyethylthioethyl)valine and (2-hydroxyethylthioethyl)histidine were detected in globin isolated from a rat treated percutaneously with sulphur mustard, and in globin from five blood samples collected from human casualties of sulphur mustard poisoning. The adducts are proposed as biological markers of sulphur mustard poisoning. in addition to urinary metabolites and DNA adducts.

Alkylating Agents↗
PubMed1977

Dielectric dispersion of DL-alpha-valine in aqueous solution.

The complex permittivity (epsilon = epsilon - jepsilon) of an (0.5 M) aqueous solution of DL-alpha-valine was measured at microwave frequencies over the temperature range 0.3 - 40 degrees C. The magnitude and relaxation time of the dispersions were determined, and the results interpreted in terms of the molecular structure of the valine molecule in solution. The peak in the dielectric loss due to the relaxation of the valine molecules occurs at approximately 2.6 GHz at 37 degrees C.

Electric Conductivity↗
PubMed1972

Separation of mitochondrial membranes of Neurospora crassa. II. Submitochondrial localization of the isoleucine-valine biosynthetic pathway.

Separation of Neurospora mitochondrial outer membranes from the inner membrane/matrix fraction was effected by digitonin treatment and discontinuous density gradient centrifugation. The solubilization of four isoleucine-valine biosynthetic enzymes was studied as a function of digitonin concentration and time of incubation in the detergent. The kinetics of the appearance of valine biosynthetic function in fractions outside of the inner membrane/matrix fraction, coupled with enzyme solubilization patterns similar to that for the matrix marker, mitochondrial malate dehydrogenase, indicate that the four isoleucine-valine pathway enzymes are localized in the mitochondrial matrix.

Alcohol Oxidoreductases↗
PubMed1998

Glycine-valine dimorphism at the 86th amino acid of HLA-DRB1 influenced the prognosis of postschistosomal hepatic fibrosis.

Chinese patients (n = 113) with schistosomal hepatic fibrosis diagnosed by ultrasonography (grade I, II, or III) and 184 age- and sex-matched persons with no clinical information of schistosomal infection were typed for their HLA-DRB1 alleles by DNA typing. There was no single allele that conferred susceptibility or resistance to fibrosis. However, there were three groups of alleles that showed decreased (resistant), increased (susceptible), or neutral frequency in the patients with fibrosis. The susceptible alleles, DRBI *1202, DRB1 *1404, and DRBI *1405, shared a valine at amino acid residue 86, whereas the resistant alleles, DRB1*11011, DRB1*0409, and DRB1*0701, all had glycine at position 86. Therefore, this study focused on the glycine-valine dimorphism at aa 86, which influences the depth of the P1 pocket in the antigen binding groove, and found that the 86th valine allele was significantly increased in the patients with fibrosis (odds ratio = 2.2; 95% CI = 1.34-3.61, corrected P < .05).

Alleles↗
PubMed1980

The need of essential amino acids in children. An evaluation based on the intake of phenylalanine, tyrosine, leucine, isoleucine, and valine in children with phenylketonuria, tyrosine amino transferase defect, and maple syrup urine disease.

The diet of children with blocks in the metabolism of five amino acids has been investigated to evaluate the need for these amino acids in the maintenance of normal growth and development. Two children with phenylketonuria, one child with tyrosine aminotransferase defect and one child with maple syrup urine disease are included in the study. The growth and development of the children have been within the normal range except for language development, which was retarded in the maple syrup urine disease child. The need for phenylalanine, phenylalanine and tyrosine combined and isoleucine, leucine, and valine for protein synthesis in growing children was investigated by registering the intake of phenylalanine in the phenylketonuria children, the intake of phenylalanine and tyrosine in the tyrosine amino transferase defect child and isoleucine, leucine and valine in the maple syrup urine disease child. The significance of this intake, defined as the sufficient intake, is discussed, as well as the difference between the sufficient intake and requirement. The sufficient intake is compared with former studies on requirement. There is good agreement between the sufficient intake and requirement of phenylalanine and tyrosine. The sufficient intake of isoleucine, leucine, and valine as judged from our study is lower than in former studies on requirement.

Amino Acids, Essential↗
PubMed1984

Leucine, isoleucine and valine requirements of immature beagle dogs.

Three experiments were conducted with growing beagle dogs fed crystalline L-amino acid diets, to determine the requirement for each of the branched-chain amino acids: leucine, isoleucine and valine. Requirements were taken as the minimum dietary concentrations required for optimal growth, feed efficiency and nitrogen retention. For each amino acid, the requirements estimated from each of these criteria were similar. Ten- to 12-week-old male beagle dogs were found to require 0.65% leucine, 0.40% isoleucine and 0.43% valine. These values correspond to 159 mg leucine, 98 mg isoleucine and 105 mg valine per 100 kcal dietary metabolizable energy. These branched-chain amino acid requirements of the growing dog are lower than those of weanling rats or pigs.

Animals↗
PubMed2000

Proton-symport of L-valine in plasma membrane vesicles isolated from leaves of the wild-type and the Val(r)-2 mutant of Nicotiana tabacum L.

Transport of amino acids across the plasma membranes of various cell types is a key process in controlling the nitrogen balance of leaves. We studied the transport of the neutral amino acid L-valine into plasma membrane vesicles obtained by aqueous polymer two-phase partitioning of a microsomal fraction isolated from leaves of the wild-type and the Val(r)-2 mutant of tobacco (Nicotiana tabacum L.). Initial influxes were determined after the imposition of a pH-gradient (DeltapH, inside alkaline) and/or an electrical gradient (Deltapsi, inside negative) across the vesicle membrane. The initial magnitudes of the imposed gradients were DeltapH=2 and Deltapsi=-68 mV. In vesicles from the wild-type, the DeltapH-dependent valine influx could be analysed into a high-affinity (Km approximately 20 microM) and a low-affinity (Km approximately 3 mM) component. The influx of valine by the low-affinity system was stimulated about twofold, and that by the high-affinity system more than sixfold by the imposition of Deltapsi. This strong stimulation of the high-affinity system may indicate that it transports 2H+/amino acid. In the Val(r)-2 mutant the high-affinity component appeared to be completely absent.

Adenosine Triphosphatases↗
PubMed1988

Valine dehydrogenase from Streptomyces fradiae: purification and properties.

Valine dehydrogenase (VDH) was purified to homogeneity from cell-free extract of Streptomyces fradiae, which produces tylosin. The enzyme was purified 1508-fold in a 17.7% yield using a combination of hydrophobic chromatography and ion-exchange fast protein liquid chromatography. The Mr of the native enzyme was determined to be 218,000 and 215,000, by equilibrium ultracentrifugation and size-exclusion high-performance liquid chromatography, respectively. The enzyme is composed of 12 subunits of Mr 18,000. Using analytical isoelectric focusing the isoelectric point of VDH was found to be 4.7. Oxidative deamination of L-valine was optimal at pH 10.6. Reductive amination of 2-oxoisovalerate was optimal at pH 8.8. The Michaelis constants (Km) were 1 mM for L-valine and 0.029 mM for NAD+. Km values for reductive amination were 0.80 mM for 2-oxoisovalerate, 0.050 mM for NADH and 22 mM for NH4+.

Amino Acid Oxidoreductases↗
PubMed1995

The tylosin producer, Streptomyces fradiae, contains a second valine dehydrogenase.

A second NAD-dependent valine dehydrogenase (VDH) of Streptomyces fradiae was detected and purified to homogeneity by affinity chromatography on Reactive-Blue 2 Sepharose followed by gel filtration and Mono Q fast protein liquid chromatography. The relative molecular masses of the native enzyme and its subunits were determined to be 80,000 and 41,000, respectively, indicating that the enzyme is a homodimer. The enzyme was the only active VDH in S. fradiae; its activity was significantly induced by L-valine, but was repressed by ammonia. Among branched- and straight-chain amino acids that serve as enzyme substrates, L-2-aminobutyrate and L-valine are preferred. Significant activities were found with deamino-NAD+ and 3-pyridinealdehyde-NAD+. The molecular and catalytic properties of the enzyme distinguish it from the enzyme previously purified, and thus indirectly indicate the existence of two VDHs in S. fradiae.

Amino Acid Oxidoreductases↗