Bis-Chelated Pd(II)-Amino Acid Complexes: Substitution Reactions of cis-Dichlorobis(benzonitrile)Palladium(II) with Amino Acids
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Abstract:
The substitution reactions of the benzonitrile (PhCN) complex cis-[Pd(PhCN)2C12] with the sodium salts of some amino acids, namely L-tyrosine (tyrH), L-phenylalanine (pheH), L-glutamic acid (gluH), L-glutamine (glnH), L-cysteine (cysH), and glycine (glyH) have been investigated. The isolated complexes [Pd(tyr)2].0.5H2O, [Pd(phe)2].H2O, [Pd(glu)2], [Pd(gln)2].H2O, Na2[Pd(cys)2].0.5Me2CO, and [Pd(gly)2].0.5H2O have been characterized by elemental analysis, conductivity measurements, IR, electronic absorption, and 1H- and 13C-NMR spectra. Based on these data, all amino acid anions are found to behave as bidentates through the ‒NH2 and ‒COO− groups except the cysteinate ion which bonds to Pd(II) through ‒NH2 and ‒S− groups.Keywords:
Benzonitrile
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Phenylalanine hydroxylase
Tyrosine aminotransferase
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A purified crystalline amino acid diet was used to study the phenylalanine tyrosine interrelationship in young chicks. Dietary phenylalanine and tyrosine requirements for maximal growth were observed to be 0.50±.07% and 0.37±.05%, respectively. Tyrosine was thus capable of furnishing up to 42.5% of the total requirement for aromatic amino acids. Under dietary conditions of phenylalanine adequacy and tyrosine deficiency, phenylalanine was found to be equal in efficacy to tyrosine in providing the limiting nutrient, tyrosine. Efficient molar conversion of phenylalanine to tyrosine was observed.
Limiting
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In the brains of newborn rats, about half of the tubulin molecules are modified posttranslationally by the addition of an aromatic amino acid at the carboxyl terminus of the alpha chain. Of the added residues, 96 percent are tyrosine and 4 percent are phenylalanine. After induction of hyperphenylalaninemia, the proportion of tubulin molecules containing carboxyl terminal phenylalanine increases up to eightfold and the pool of tyrosine-containing molecules decreases by an equivalent amount.
Hyperphenylalaninemia
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Nitrogen balance
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Hydroxylation
Phenylalanine hydroxylase
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The addition of 1% dl-phenylalanine and 1% l(-) tyrosine to a purified diet containing 10% casein produced growth retardation and external lesions. Phenylalanine is converted to tyrosine in the animal and so may add to the effect of the tyrosine. The addition of relatively large amounts of nicotinic acid or l(-)tryptophane will appre ciably alleviate the deleterious effects of these amino acids.
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Hydroxylation
Phenylalanine hydroxylase
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Abstract The kinetics of the incorporation into protein of [ 3 H]phenylalanine, [ 3 H]tyrosine and [ 3 H]tryptophan were studied with homogenates prepared from whole brain of 1‐, 7‐, 21‐ and 60‐day‐old rats. The maximal velocities ( V max )of incorporation of phenylalanine and tyrosine decreased and the apparent Michaelis‐constants ( K m ) for all three amino acids increased with increasing age of the rats. Tyrosine had the smallest and tryptophan the largest K m values in all age groups. Phenylalanine competitively inhibited the incorporation of tyrosine, but tyrosine inhibited non‐competitively the incorporation of phenylalanine. Tryptophan inhibited competitively the incorporation of phenylalanine, but at least partially non‐competitively the incorporation of tyrosine. Phenylalanine and tyrosine did not significantly affect the incorporation of tryptophan in homogenates from 60‐day‐old rats. In 1‐day‐old rats only a very large excess of phenylalanine or tyrosine inhibited detectably. The K i for phenylalanine in the incorporation of tyrosine was significantly smaller in 1‐ than in 60‐day‐old rats. In every case the inhibition presumably occurred at a single rate‐limiting step in the complicated process of incorporation of amino acids into protein.
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Seventeen structurally related compounds were tested for their ability to substitute for phenylalanine or tyrosine in the nutrition of chick embryo heart fragments. DL-Alanyl-DL-phenylalanine replaced phenylalanine. All other compounds had negligible effects, and most were toxic at high concentrations. β-Phenylserine, a phenylalanine antagonist, actually prolonged the survival of chick heart cells but only if both phenylalanine and tyrosine were present. Similarly, optimal reversal of β-phenylserine toxicity was dependent on the presence of both amino acids. Although phenylalanine and tyrosine are not interconvertible in the present system, it has been shown that three phenylalanine antagonists, p-fluorophenylalanine, β-2-thienylalanine, and β-phenylserine, can be identified by their relationship to tyrosine, rather than to phenylalanine.
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