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

This study was concerned with the course of DNA synthetic activity (3H-TdR-LI-method) in the buccal mucosa of adult male. Sprague Dawley rats over an incubation period of 5 h. Interest was focussed on the influences of different media and, in particular, on temoporary changes in the proliferative activity. 3H-LI were compared in specimens (a) kept in active (= i.e., 3H-thymidine containing) medium throughout their respective incubation period and (b) pre-incubated in inactive medium for varying, but clearly defined periods before being transferred into active medium for 30 min (actual 3H-LI). Independent of the medium used the rate of DNA synthesis was markedly lowered at 60 min, the reduction being more or less significant in the different media. This was due to a temporary inhibition of DNA synthesis, which was restored after 120-180 min. In contrast, the blockade of G2-phase and/or mitosis persisted up to the end of incubation, as indicated by the unchanged number of labelled mitotic figures after 120 min. Addition of glutamine to Mc Coy's 5A markedly enhanced the activity of 3H-thymidine incorporation, but could not prevent the temporary inhibition of DNA synthesis. The biochemical mechanisms relevant for cell proliferation have been reviewed and correlated to the present results.
Virchows Arch B Cell Pathol Incl Mol Pathol 1979
PMID:An autoradiographic analysis of the mode of proliferation in the buccal mucosa of rats incubated up to 5 hours. 4 1

As glutamine-dependent carbamoyl phasphate synthetase (CPS) activity in some organisms is composed of a glutaminase and an ammonium-dependent CPS, CPS- mutants in Neurospora crassa were examined for glutamine- and ammonium-dependent CPS activities. No evidence was found that the genetic location of these two functions were separable. This is discussed with reference to the close genetic proximity of the CPSpyr and aspartate carbamoyltransferase (ACT) structural gene (pyr-3) and the arg-2 gene which appears to specify a subunit responsible for glutamine utilisation in CPSarg.
Mol Gen Genet 1976 Dec 08
PMID:Glutamine utilization in both the arginine-specific and pyrimidine-specific carbamoyl phosphate synthase enzymes of eurospora crassa. 18 79

Mutants of Escherichia coli K12 requiring glutamine as a nitrogen source were isolated, and characterized as lacking glutamine synthetase activity. Temperature sensitive revertants of one of the mutants had a heat labile glutamine synthetase, while temperature insensitive revertants had a glutamine synthetase which was thermostable in vitro, indicating that the mutation was in the structural gene for the enzyme. All of the mutations mapped in the same region of the chromosome suggesting that they might all be in the same gene. The glutamine synthetase gene (gln) was located on the E. coli chromosome by conjugation and P1-mediated transduction at minute 77. The gln gene cotransduced with the genes for oleate degradation (old), and the genes for L-rhamnose utilization (rha). The most probable gene order is old-gln-rha.
Mol Gen Genet 1975
PMID:The isolation and characterization of glutamine-requiring strains of Escherichia coli K12. 24 28

The ribosomes of an Escherichia coli mutant, designated prm-2, can be methylated in vitro by an enzymatic fraction from wild-type. This enzyme is inactive on the ribosomes from another mutant, prm-1, is reported previously to be methyl group-deficient in protein L11. In vitro methylation of prm-2 ribosomes resulted in the incorporation of about one methyl group per molecule of protein L3. After acid hydrolysis, all the methyl groups were found in a very basic compound which was identified as methylamine. This compound could have been generated by acid hydrolysis of N-methylated amide-groups from glutamine or asparagine. Therefore, chemically-synthesized N4-methyl-asparagine and N5-methylglutamine were chromatographed together with an enzymatic hydrolysate of methylated prm-2 proteins. In all the chromatogrphic systems studied the methylated amino acid was found in the same position as N5'-methylglutamine. These results indicate that mutant prm-2 lacks one residue of N5-methylglutamine present in ribosomal protein L3 of wild type E. coli.
Mol Gen Genet 1977 Jul 20
PMID:Genetics of ribosomal protein methylation in Escherichia coli. II. A mutant lacking a new type of methylated amino acid, N5-methylglutamine, in protein L3. 33 Oct 83

Constitutivity for the synthesis of the urea amidolyase bienzymatic complex is obtained by durOh mutations located in the regulatory genetic region adjacent to the dur1, dur2 gene cluster. The durOh mutations act only in cis and are a new case of cis effect strongly cancelled in alpha/a diploid, similar to cargA+Oh mutation shown previously to lead to arginase constitutivity. Illegitimate diploids do not show such a cancellation of constitutivity. The constitutivity produced by durOh mutation comprises the process of induction and the release of the glutamine effect. It does not impair the NH+4 effect.
Mol Gen Genet 1978 Nov 09
PMID:The regulation of urea amidolyase of Saccharomyces cerevisiae: mating type influence on a constitutivity mutation acting in cis. 36 77

Interaction of highly purified E. coli glutamate decarboxylase with a number substrate analogs was studied. Decarboxylation of the following amino acids was demonstrated: gamma-methylene glutamate, threo-beta-hydroxyglutamate, allo-gamma-hydroxyglutamate, threo-beta-methylglutamate, homocysteate, aminoadipate and cysteinesulfinate. The Km and either Ki or I50 values were determined for these compounds. The final products of the interaction of glutamate decarboxylase with these analogs have the same absorption spectra and capacity for reactivation by pyridoxal-P, as has the pyridoxamine-P form of the enzyme. Thus, decarboxylation of all the amino acids, mentioned above, was probably associated with the side reaction of transamination to coenzyme in the active center. Binding of aliphatic dicarboxylic acids or of valeric acid by glutamate decarboxylase leads to a slight shift of absorption spectra and of circular dichroism spectra from 420 to 423--425 nm. The following compounds fail to be bound and decarboxylated by the enzyme: gamma-aminobutyrate, D-glutamate, L-glutamine, 3,3-dimethylglutarate, methioninesulfone, methioninesulfoxide, norvaline, gamma-hydroxy-gamma-methylglutamate, erytro-beta-methylglutamate and erythro-beta-hydroxyglutamate.
Mol Biol (Mosk)
PMID:[Substrate specificity of E. coli glutamate decarboxylase]. 37 98

The production of some nonproteinous, and lack of production of other proteinous, amino acids in model prebiotic synthesis, along with the instability of glutamine and asparagine, suggest that not all of the 20 present day proteinous amino acids gained entry into proteins directly from the primordial soup. Instead, a process of active co-evolution of the genetic code and its constituent amino acids would have to precede the final selection of these proteinous amono acids.
J Mol Evol 1979 Jul 18
PMID:Inadequacy of prebiotic synthesis as origin of proteinous amino acids. 48 Mar 69

The diazomethyl ketones of z-Phe-Phe inactivate papain by a stoichiometric reaction at the active-center thiol. Since the reagents are stable in mercaptoethanol, their reaction with papain is judged to be the result of complex formation characteristic of affinity-labeling reagents. The diazomethyl ketones react by a mechanism different from that of chloromethyl ketones, since the pH dependence of their inactivation of papain is different, the rate increasing with decreasing pH. This relationship has been observed in other cases, such as in the reaction of azaserine with glutamine amidotransferases [Buchanan, J. M. (1973), Adv. Enzmol. Relat. Areas Mol. Biol. 39, 91], and is interpreted as an indication of reaction with a thiol group in its protonated form.
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PMID:Diazomethyl ketone substrate derivatives as active-site-directed inhibitors of thiol proteases. Papain. 58 60

1. Arterial concentration and arterial-venous differences of glutamine across the kidney, forearm, hepato-splanchnic bed and brain were measured in patients with chronic renal insufficiency and in patients with normally functioning kidneys before and during chronic ammonium chloride acidosis. 2. In chronic renal insufficiency and in chronic metabolic acidosis there is a rise in glutamine release from the muscles and a suppression of glutamine uptake by the hepato-splanchnic bed and the brain. 3. In chronic renal insufficiency arterial glutamine concentrations is significantly increased in comparison with subjects with normal renal function and either normal acid-base balance or chronic metabolic acidosis. 4. In patients with chronic renal insufficiency the kidney extracts negligible amounts of glutamine, which cannot account for the renal ammonia production measured in the same patients.
Clin Sci Mol Med 1978 Oct
PMID:Effects of chronic renal insufficiency and metabolic acidosis on glutamine metabolism in man. 71 53

1. The effects of acute acid-base alterations on renal ammonia production and glutamine metabolism were studied in anaesthetized dogs. 2. Plasma glutamine rose with acidosis and also when both PCO2 and plasma HCO-3 were raised isohydrically. 3. Blood urea fell when acidosis was induced with hydrochloric acid. 4. The renal production of ammonia per ml of renal blood flow was increased in acidosis, but this was independent of the amount of glutamine delivered to the kidney. 5. The results indicate that acute acidosis affects production of urea and glutamine and increases the capacity of the renal cells to extract glutamine from blood.
Clin Sci Mol Med 1978 May
PMID:Effects of acute acid--base alterations on glutamine metabolism and renal ammoniagenesis in the dog. 75 Jan 52


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