Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Equilibrium constants (K) of the complex formation of adenosine-5'-phosphate with phenylalanine (27 l/mol) and tryptophan (67 l/mol) in water (D2O, pD 9.9) have been determined. The comparison of the equilibrium constant values allowed to find the sequence of probabilities of the approach of aromatic amino acids to adenosine-5'-phosphate (tryptophan greater than tyrosine greater than phenylalanine). It has been shown that the dependence of lg K on l/T in the system phenylalanine-adenosine-5'-phosphate is non-linear. The ranges of the positive values of enthalpy (deltaH) and entropy (deltaS) changes of the complex phenylalanine-adenosine-5'-phosphate formation in the temperature interval 28-65 degrees have been found (deltaH = 0.2-1.5 kcal/mol, delta S = 14-50 e.u.). The conclusion about the hydrophobic interaction of aromatic cycles of nucleotide and amino acids has been deduced from the received data.
Mol Biol (Mosk)
PMID:[Intermolecular interaction of adenosine-5'-phosphate with phenylalanine and tryptophan by nuclear magnetic resonance]. 105 79

The DNA dependent synthesis of proteins was studied with a system composed of DNA, washed ribosomes, centrifuged (150,000 X g) bacterial extract from Escherichia coli and purified initiation factors IF-1 and IF-2. Synthesis of active enzymes encoded by the tryptophan (trp)-operon of E. coli was found to depend strongly on the addition of IF-3, with the same IF-3 dependency for all 5 gene-products of this operon, irrespective of the presence of the promotor proximal gene trpE. Synthesis of T7 RNA polymerase with T7 DNA as a template, however, was completely independent of the addition of IF-3. The same difference in IF-3 requirement was found when we compared the overall protein synthesis directed by these templates. This difference could be related to the effect of IF-3 on the formation of initiation complexes with the in vitro prepared mRNA: initiation complexes are readily formed with T7 mRNA also in the absence of IF-3, whereas the formation of these complexes with phi80trp mRNA almost completely depends on the presence of this factor.
Mol Gen Genet 1975 Sep 08
PMID:The role of IF-3 in the translation of T7- and phi80trp messenger RNA. 110 44

50-S ribosomal subunits from the extreme halophilic bacterium, Halobacterium cutirubrum, contain an alanine-rich acidic "A" protein which resembles the L7--L12 multimer (Kaltschmidt and Wittmann, 1970) found in the 50-S ribosomal subunit of Escherichia coli cells. The protein contains 24 mole % alanine and is devoid of histidine, tryptophan and cysteine. Unlike E. coli which has two forms of the "A" protein distinguished solely by the acetylation state of the serine amino terminus. H. cutirubrum 50-S subunits contain only one unsubstituted form of the "A" protein in vivo. However, during purification of ribosomes from cells grown between 25 and 37 degrees C the latter "A" protein undergoes rapid, specific, in vitro enzymatic alteration at its carboxy-terminal end. When the halophile is grown in the temperature range of 40 to 42 degrees C the cleaving enzyme is not active and only one form of the "A" protein is found on the ribosomes.
Mol Gen Genet 1975 Sep 15
PMID:Temperature related alterations in the acidic alanine-rich "A" protein from the 50S ribosomal particle of the extreme halophile, Halobacterium cutirubrum. 110 49

The photoreversibility of UV-induced mutations to Trp+ in strain Escherichia coli WP2 uvrA trp (unable to excise pyrimidine dimers) was lost at different rates during incubation in different media. In Casamino acids medium after a short initial lag, photoreversibility was lost over about one generation time; in minimal medium with tryptophan, photoreversibility persisted for more than two generations; in Casamino acids medium with pantoyl lactone photoreversibility was lost extremely slowly. The rate of loss of photoreversibility was unaffected by UV dose in either Casamino acids medium or in minimal medium. The same eventual number of induced mutants was obtained when cells were incubated for two generations in any of the three media before being transferred to selective plates supplemented with Casamino acids. Thus in each the proportion of cells capable of giving rise to a mutant was the same and only the rate at which these cells did so during post-irradiation growth varied, suggesting that there might be a specific fraction of pyrimidine dimers at a given site capable of initiating a mutagenic repair event, and that the size of this fraction is dose dependent. Segregation experiments have shown that error-prone repair appears to occur once only and is not repeated in subsequent replication cycles, in contrast to (presumed error-free) recombination repair. The results are discussed in the light of current models of UV mutagenesis.
Mol Gen Genet 1975 Oct 03
PMID:Mutagenic DNA repair in Escherichia coli. II. Factors affecting loss of photoreversibility of UV induced mutations. 110 95

Upon preincubation with urea, various 3- or 4-substituted N-methylpyridinium salts form charge-transfer complexes with tryptophan containing proteins such as, L-chymotrypsin and lysozyme. The complexes were studied by using the difference spectrophotometric technique. The fluorescence examination showed that tryptophyl residues in protein molecules are engaged in the complex formation process. The complex formation reactions proceed at a considerable rate. The stopped-flow method was used to determine the pseudo first order rate constants. A linear dependence of the pseudo first order rate constants with the donor concentration was found. The second order rate constants were obtained by dividing the mean value of the pseudo first order rate constants by the initial donor concentration for each run. The linear dependence of second order rate constants with the electron affinity of the acceptors can serve as a criterion for the formation of charge-transfer complexes.
Mol Biol Rep 1975 Dec
PMID:The kinetics of complex formation of tryptophan containing proteins with pyridinium salts. 121 82

The parameters of fluorescence spectra of myosin and its subunits in Tris-HCl-buffer (pH 7.2) were studied. Analysis of the experimental results of myosin fluorescence quenching with I-ions and the quantum yield of the fluorescence at the excitation wavelength 296 nm shows that the greater part of the tryptophan residues (21 out of 28) is located in the hydrophylic environment. Concentrated solutions of NaCl and KCl do not affect myosin fluorescence, while LiCl, which changes the quaternary structure of the protein, brings about a change in the parameters of the myosin fluorescence spectra. This may be linked with structural changes accompanying the dissociation of the ligh subunits of myosin in the presence of LiCl.
Mol Biol (Mosk)
PMID:[Fluorescence of myosin and its subunits in concentrated salt solutions]. 121 99

Nucleotidyl-(5' leads to N)-amino acids containing different heterocycle bases: adenine, guanine, hypoxanthine, cytosine, uracyl, and aromatic amino acids: phenylalanine, tyrosine and tryptophan, have been investigated by proton magnetic resonance and circular dichroism. For all the compounds studied folded conformation have been shown stabilized by hydrophobic interaction in aqueous solution. The comparison of the results of the studied nucleotidyl-(5' leads to N)-amino acids unable us to build four secondary structure types in these very compounds. Phenylalanine and tyrosine derivatives of purine nucleotides can be regarded as the first type, tryptophan derivatives of purine nucleotides as the second type, phenylalanine and tyrosine derivatives of pyrimidine nucleotides as the third type and tryptophan derivatives of pyrimidine nucleotides as the fourth type. For each group of these compounds conformational models have been built. In all these compounds the anti-conformation has been proved to exist.
Mol Biol (Mosk)
PMID:[The secondary structure of nucleotidyl-(5' bound to N)-amino acids containing different heterocyclic bases and amino acids]. 121 5

1. Gluconeogenesis from lactate or from glutamine is inhibited by 90-100% by sodium quinolinate (1 mmol/l) or 3-mercaptopicolinate (150 nmol/l) in the perfused rat kidney. L-Tryptophan is not metabolized and is without effect. 2. Lactate uptake and glucose production are inhibited to the same degree by 3-mercaptopicolinate in the kidneys of well-fed or starved rats. 3. Inhibition of gluconeogenesis from glutamine (1 mmol/l) by 3-mercaptopicolinate is accompanied by 50% inhibition of ammonia production, and 34% inhibition of glutamine uptake, in the kidneys of acidotic rats. Ammonia production from glutamine was not inhibited in kidneys from non-acidotic rats. 4. It is concluded that the increased rate of gluconeogenesis from glutamine which occurs in acidotic rats is an essential and primary event regulating all of the increase in ammonia formation.
Clin Sci Mol Med 1976 Jun
PMID:Effect of inhibition of gluconeogenesis on ammonia production in the perfused rat kidney. 127 56

The rules defining the Asp-Asp domain of RNA-dependent polymerases deduced by Argos (1988) were tested in a set of 53 putative reverse transcriptases (RTs) sequences. Since it was found that some of these rules are not followed by RTs coded by bacteria, group II introns, and non-LTR retrotransposons, we present here a more strict definition of the Asp-Asp domain.
J Mol Evol 1992 Dec
PMID:A redefinition of the Asp-Asp domain of reverse transcriptases. 128 62

The mutants of Azospirillum brasilense Sp245 altered in the production of anthranilic (Ant) and indolyl-3-acetic (IAA) acids were selected after the chemical or transposon facilitated mutagenesis and divided into the following three classes: Ant+IAA+, Ant+IAA- and Ant-IAA-. A hypothesis on the existence of a pattern for tryptophan conversion to anthranilate that is different from the classic pattern, and on the connection of the indolyl-3-acetic synthesis with this process is suggested.
Mol Gen Mikrobiol Virusol
PMID:[Azospirillum brasilense SP245 mutants in production of anthranilic and indolyl-3-acetic acids]. 129 84


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>