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)

It has been shown that 50S subunits of E. coli MRE-600 ribosomes catalyze the reaction of N-(formyl)-methionyl ester of adenosine 5'-phosphate acting as peptide donor, with Phe-tRNA or CACCA-Phe serving as a peptide acceptor. The reaction is stimulated by cytidine 5'phosphate and inhibited by lincomycin, puromycin and chloramphenicol. The obtained results show that the structure of the donor site of peptidyltransferase is completely assembled on the 50S subunit and 30S subunit is not required for its formation.
Mol Biol (Mosk)
PMID:[Fragment reaction catalyzed by E. coli ribosomes]. 37 8

50 S subunits of E. coli ribosomes catalyze the reaction of the 2'(3')-N-(formyl) methionine ester of adenosine 5'-phosphate and Phe-tRNA resulting in peptide bond synthesis. Cytidine 5'-phosphate stimulates this process on 50 S ribosomal subunits as well as on intact ribosomes. The obtained data show that the areas of the peptidyltransferase donor site which binds the 3'-terminal fragment of peptidyl-tRNA possess completely formed structures on 50 S ribosomal subunits.
Mol Biol Rep 1976 Nov
PMID:Catalysis of the peptide bond formation by 50 S subunits of E. coli ribosomes with N-(formyl) methionine ester of adenylic acid as peptide donor. 79 86

The mechanism of 5'-cytidilic acid stimulation of the reaction between 2'(3')-O-formylmethionine ester of 5'-adenylic acid and phenylalanyl-tRNA catalyzed by E. coli ribosomes has been studied. It has been shown that cytidilic acid binds to the donor site of the peptidyltransferase in the area which is usually occupied by the second nucleotide residue of the peptidyl-tRNA 3'-end. After the binding cytidilic acid stimulates effectively the donor activity of formylmethionine ester of adenylic acid. A number of compounds have been tested as possible stimulants. Both the chemical nature of stimulant and its conformation are important for the stimulating action. A hypothetic scheme is suggested explaining possible causative factors of peptidyl-tRNA translocation from the acceptor site to the donor site after peptide bond formation.
Mol Biol (Mosk)
PMID:[Donor site of E. coli ribosomal peptidyltransferase]. 80 87

The effect of spermine on the binding of AcPhe-tRNA to poly(U)-programmed ribosomes (step 1) and on the puromycin reaction (step 2) has been studied in a cell-free system, derived from E. coli. In the absence of ribosomal wash (FWR fraction) and at suboptimal concentration of Mg++ (6 mM), spermine stimulated the binding of AcPhe-tRNA at least five fold, while at 10 mM Mg++ there was a three fold stimulation. The above stimulatory effect was decreased at 6 mM Mg++, or was abolished at 10 mM Mg++ by the presence of FWR during the binding. Beside the stimulatory effect, spermine enhanced the stability of initiation complex AcPhe-tRNA-poly(U)-ribosome. In step 2, spermine affected the final degree of puromycin reaction and the activity status of peptidyltransferase. Both stimulatory and inhibitory effects have been observed, depending on the experimental conditions followed during the binding of the donor and during the peptide bond formation.
Mol Cell Biochem 1992 Sep 22
PMID:Effect of spermine on peptide-bond formation, catalyzed by ribosomal peptidyltransferase. 143 61

All tested members of genus Plasmodium contain tandemly arrayed, transcribed, extrachromosomal DNA with a unit length of 6.0 kb. This DNA contains two open reading frames with potential to encode cytochrome c oxidase subunit I (cox1) and cytochrome b (cob) as well as fragments of rRNA genes scattered on both strands. At least 10 discrete RNA molecules transcribed during erythrocytic stages of a rodent malarial parasite, Plasmodium yoelii, were recognized by the 6.0-kb DNA probes. The RNA molecules of 1.4 and 1.1 kb were identified as encoding cox1 and cob, respectively. Primer extension and RNA sequencing were used to locate and characterize 5' ends of these two RNAs, showing that an identical 12-nucleotide sequence, 5'-TATTTTT TGTTT-3', was present at these positions. This sequence may act as a promoter or as an RNA processing signal. A stem-loop structure signifying a possible transcription termination was present at the end of the cox1 open reading frame. At least six discrete RNA molecules of less than 250 nucleotides were recognized by different fractions of the 6.0-kb DNA. The largest of these, 200 nucleotides, was also characterized by primer extension and RNA sequencing. This molecule had a high homology to portions of the large-subunit rRNA domains IV and V. Other, small RNA molecules were recognized by regions of the 6.0-kb DNA that had homology to the highly conserved peptidyltransferase domain of large-subunit rRNA. These results show that the unusual compactly organized mitochondrionlike DNA of malarial parasites is transcribed in a complex pattern.
Mol Cell Biol 1990 Dec
PMID:Complex transcription from the extrachromosomal DNA encoding mitochondrial functions of Plasmodium yoelii. 170 Oct 17

The effect of hyperammonemia of varying degree and duration on the gamma-glutamyl-transpeptidase (GGT) activity was studied in the homogenates and capillaries of different brain regions of the rat. "Acute" hyperammonemia (750 and 600 mg of ammonium acetate per kg b.w. were injected i.p. at 30 min interval, and the animals were decapitated immediately), in which blood ammonia was increased 14-fold, and brain ammonia six-fold above the control level, produced a 20% increase of the enzyme activity in cerebellum, and a 17% decrease in gyrus dentatus, but had no effect in the frontal cortex and the CA1 and CA3 regions of hippocampus. "Subchronic" hyperammonemia (two injections of 600 mg ammonium acetate/kg were given at 24 h intervals, and tissue samples were removed 24 h later), that was accompanied by only a 60% increase of blood or brain ammonia, increased the activity in cerebellum to 38% above control, but produced no effect in the other brain regions. "Chronic" hyperammonemia (three injections of 600 mg ammonium acetate/kg at 24 h intervals and excision of tissue samples 30 min after the last injection), in which blood and brain ammonia were, respectively, 60 and 100% higher than in control animals, elevated the GGT activity in the cerebellum by 57%, in CA1 by 15%, and in CA3 by 21%, but produced no effect in the frontal cortex or gyrus dentatus. By contrast, "chronic" hyperammonemia produced a 30% increase of GGT activity in cerebral cortical capillaries, but only a 10% increase in hippocampal capillaries, and no change in cerebellar capillaries. The results suggest that, hyperammonemia of relatively long duration may contribute to the enhancement of brain GGT activity observed in chronic forms of hepatic encephalopathy. However, ammonia does not appear to activate the enzyme directly.
Mol Chem Neuropathol
PMID:The effect of acute and repeated hyperammonemia on gamma-glutamyl transpeptidase in homogenates and capillaries of various rat brain regions. 198 79

Effects of Cephalotaxus alkaloids (homoharringtonine and cephalotaxine) on the translation of endogenous mRNA in a cell-free system of rabbit reticulocyte lysate and on poly(U)-directed poly(Phe) synthesis on human placenta ribosomes was studied. The effect of the alkaloids on the activity of human placenta ribosomes in a template-dependent aminoacyl-tRNA binding, N-acetyl-phenylalanyl-puromycin and diphenylalanine formation was also studied. Homoharringtonine was shown to have little effect of codon-dependent Phe-tRNA(Phe) binding but the alkaloid strongly inhibited (Phe)2 formation as well as N-Ac-Phe-puromycin synthesis from the complex N-Ac-Phe-tRNA(Phe).poly(U).80S ribosomes. It was concluded that the site of homoharringtonine binding overlaps or coincides with the acceptor site of the ribosomal peptidyltransferase center. The association constant of homoharringtonine to the ribosomes was estimated to be (4.8 +/- 1.0) x 10(7) M-1. Cephalotaxine had no effect on the elongation steps.
Mol Biol (Mosk)
PMID:[The effect of Cephalotaxus group alkaloids on elongation of the polypeptide chain in human ribosomes]. 209 16

The molecular structure of the hexagonal crystal form of porcine pepsin (EC 3.4.23.1), an aspartic proteinase from the gastric mucosa, has been determined by molecular replacement using the fungal enzyme, penicillopepsin (EC 3.4.23.6), as the search model. This defined the space group as P6522 and refinement led to an R-factor of 0.190 at 2.3 A resolution. The positions of 2425 non-hydrogen protein atoms in 326 residues have been determined and the model contains 371 water molecules. The structure is bilobal, consisting of two predominantly beta-sheet lobes which, as in other aspartic proteinases, are related by a pseudo 2-fold axis. The strands of the mixed beta-sheets (1N and 1C) of each lobe are related by an intra-lobe topological 2-fold symmetry. Two further beta-sheets, 2N and 2C, are each composed of two topologically related beta-hairpins folded below the 1N and 1C sheets. A further six-stranded sheet (3) spans the two lobes and forms a structure resembling an arch upon which the four other sheets reside. The interface between sheets 1N and 1C forms the catalytic centre consisting of absolutely conserved aspartate residues 32 and 215, which are shielded from solvent by a beta-hairpin loop (75 to 78). The crystal structure of a mammalian aspartic proteinase indicates that interactions with substrate may be more extensive on the prime side of the active site cleft than in the fungal enzymes and involve Tyr189 and the loop 290 to 295, perhaps contributing to the transpeptidase activity of pepsin and the specificity of the renins. Comparison with the high-resolution structure of pepsinogen gives a root-mean-square deviation of 0.9 A and reveals that, in addition to local rearrangement at the active site, there appears to be a rigid group movement of part of the C-terminal lobe of pepsin towards the cleft on activation. A large proportion of the absolutely conserved residues in aspartic proteinases are polar and buried. An examination of the pepsin structure reveals that these side-chains are involved in hydrogen-bond interactions with either the main chain of the protein or other conserved side-chains of the enzyme or propart.
J Mol Biol 1990 Jul 05
PMID:X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution. 211 88

Human lysosomal cathepsin G (cat G) appears to be an important mediator of non-oxidative killing of Neisseria gonorrhoeae ingested by human polymorphonuclear leucocytes (PMNLs). Nearly isogenic strains of gonococci having variations in the structure of penicillin-binding protein 2 (PBP2) also exhibit different levels of susceptibility to the lethal action of cat G in vitro. Accordingly, we examined the relationship between gonococcal susceptibility to cat G and PBP2 structure. The results of this study suggest that cat G has the capacity to interact with PBP2, as evidenced by its ability to inhibit binding of [3H]-benzylpenicillin to PBP2. We also found that changes in the amino acid sequence within the transpeptidase domain of PBP2, because of certain penA mutations, modulated such interactions. We propose that PBP2 is an intracellular target for cat G and that levels of gonococcal susceptibility to cat G may be related to PBP2 structure and/or intracellular availability.
Mol Microbiol 1990 Aug
PMID:Molecular mechanism for the antigonococcal action of lysosomal cathepsin G. 212 24

The nucleotide sequences of the 3' halves of the mitochondrial 16S rRNA genes from four independent mouse chloramphenicol-resistant (CAP-R) mutants were determined. Each contained a different, single base change that encodes the mutational phenotype. The mitochondrial rRNA gene from the SVA31 CAP-R mutant contains a G-to-A transition at nucleotide 2161 of the noncoding strand; the SVIS CAP-R mutant, a G-to-A transition at position 2375; the LA9 CAP-R mutant, an A-to-T transversion at position 2379; and the SVT2 CAP-R mutant, a T-to-C transition at position 2433. Three of these CAP-R mutants appear to be heteroplasmic as the mtDNA populations contain both wild-type and mutant copies of the rRNA gene. The SVIS CAP-R mutation has not been observed in other mammalian CAP-R mutants, although it occurs at a site homologous to one of the yeast mitochondrial CAP-R mutations. Based upon the locations of the mutated sites within the 16S rRNA, and their proximity to previously analyzed sites of mutations conferring increased inhibitor resistance, all these mutations occur within the ribosomal RNA peptidyltransferase domain. These results provide an explanation for the pleiotropic nature of mitochondrial CAP-R mutations in mammalian cells, particularly the observations that some of the mutant lines are partially respiration deficient.
Somat Cell Mol Genet 1989 May
PMID:Sequence analysis of mouse mitochondrial chloramphenicol-resistant mutants. 247 Dec 79


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