Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT02079 (lysine)
 58,762 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Feeding of rice diet reduced the food consumption and growth of rats. Hepatic Cytochrome P-450, NADPH Cytochrome c reductase and the activity of cytochrome P-450 dependent enzymes (Aniline hydroxylase, aminopyrine N-demethylase, p-nitroanisole O-demethylase) were also decreased by feeding rice diet. Supplementation of lysine and threonine to rice diet improved the activity of these enzymes. NADPH regeneration and microsomal phosphatidylcholine were reduced by feeding rice diet. The phenobarbitone induced sleeping time was decreased by supplementing rice diet with lysine and threonine. The effect of protein is probably partly attributed to changes in membrane phosphatidylcholine content and NADPH regeneration rate.
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PMID:Mixed function oxidases in response to quality and quantity of dietary protein. 314 73

1. Effects of repeated administration of N2-[(N-acetylmuramoyl)-L-alanyl-D-isoglutaminyl]-N6-stearoyl-L-lysine (MDP-Lys (L18), muroctasin) to female rats on the activities of drug metabolizing enzymes in liver microsomes were examined. The in vitro effects of the compound on the activities of drug metabolizing enzymes in liver microsomes from male rats were also investigated. 2. The subcutaneous administration of MDP-Lys (L18) at a dose of 1 mg/kg (high dose) caused slight but significant decrease in the contents of cytochrome P-450 and cytochrome b5. The daily subcutaneous injection at a dose of 0.1 mg/kg (middle dose) resulted in the induction of aminopyrine N-demethylase, aniline hydroxylase and 7-ethoxycoumarin O-deethylase. Such induction of the enzymes was seen only when calculated on the basis of microsomal protein but not wet weight of livers. The changes were relatively small as compared with those caused by phenobarbital. 3. At one week after the last injection of the high dose of MDP-Lys (L18), slightly higher levels of the contents of cytochrome P-450 and cytochrome b5 and the activity of NADPH-cytochrome c reductase were noted. The cessation of the administration tended to increase the activities of drug metabolizing enzymes in rats treated with the high dose of the drug. These changes were seen only when the activities were calculated on the basis of mg of microsomal protein. 4. MDP-Lys (L18) inhibited drug metabolizing enzymes in vitro to various extents depending on the substrate used.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of muroctasin on the activities of drug metabolizing enzymes in liver microsomes of rats. 326 67

Fluorescein isothiocyanate (FITC) has been selectively bound to the epsilon-amino group of lysine-382 in cytochrome P-450 LM2 (RH, reduced-flavoprotein: oxygen oxidoreductase (RH-hydroxylating), EC 1.14.14.1) at pH 8.15. Benzphetamine N-demethylase activity of the reconstituted FITC-modified cytochrome P-450 LM2 was inhibited by 25%. This inhibition has been shown to be due to an impaired electron transfer from the NADPH-cytochrome P-450 reductase (NADPH: ferricytochrome oxidoreductase, EC 1.6.2.4) to the haemoprotein. The data indicate that cytochrome P-450 interacts with the flavoprotein via electrostatic interactions.
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PMID:Selective chemical modification of a functionally linked lysine in cytochrome P-450 LM2. 642 89

Fluorescein isothiocyanate was selectively bound to the epsilon-amino group of a lysine residue of cytochrome P-450 LM2 at rho H 8.15. The decrease in the N-demethylase activity after modification evidences the functional importance of the modified group. After tryptic digestion the FITC-labeled peptide was isolated by means of HPLC and its amino acid composition determined. It was shown that the FITC-peptide can be attributed to the sequence Gly (379)- Arg (400) and that the label is selectively bound to Lys (384).
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PMID:Identification of lysine (384) in cytochrome P-450 LM2 as functionally linked residue. 644 64

It has been demonstrated that the deficiency of 3 essential amino acids (lysine, threonine and methionine) combined with polyhypovitaminosis A, C and E for 2 months leads to a decrease in the para-hydroxylase and N-demethylase activity in rat liver microsomes. The content of cytochromes P-450 and b5 was also reduced as compared to that in animals given balanced nutrition. However, in such a polynutrient deficiency, the activity of microsomal enzymes was induced by phenobarbital to a greater degree than in balanced nutrition. It is suggested that in polynutrient deficiency, the lacking essential factors mobilized from other organs and tissues are involved in the process of induction of microsomal enzymes.
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PMID:[Effect of lysine, threonine, methionine and vitamin A, C and E deficiency on the liver microsome enzyme system responsible for metabolizing foreign compounds in the rat]. 671 Sep 59

Young adult Sprague-Dawley rats were partially hepatectomized (two-thirds organ removal) and administered a basal diet supplemented with various animal- and plant-derived enzymes (trypsin, alpha-chymotrypsin, pepsin, lipase, alpha-amylase, malt diastase, ficin and bromelain) over a post-operative period of up to 10 days. Porcine or bovine dialyzed and lyophilized crystalline trypsin products containing 2400-3200 NF u/mg in addition to enteric-coated tablets with trypsin to chymotrypsin in a ratio of 6:1, were tested at supplementary levels of up to 4980 u/g ration. With the weight of tissue regenerated or the liver increment as indicator, trypsin in excess of 1000-1200 u/g ration proved inhibitory. This effect did not extend to alpha-chymotrypsin (levels of up to 4000 u/g diet) and the remaining 6 enzyme products specified above, nor to the s.c. injection of trypsin daily at 12,860 u/rat for the 1st 7 days. The last route promoted little change in increment with soy bean trypsin inhibitor (8.0 mg/rat daily for days 1 to 9). When a portion of the group fed a trypsin supplement of 2000 u/g was injected with phenobarbital i.p. at 80 mg/kg daily on each of the last 3 days, the resulting liver increment rose to the control range. As with lysine and arginine, acids of pertinence in tryptic proteolysis, no significant change was elicited by feeding a diet supplemented with peptone from tryptic digestion of casein. The enzyme-containing diets fed to sham-operated rats over a similar interval, did not affect the wet- or dry-liver weight per 100 g body weight. Microsomal parameters as total protein, cytochrome P-450 and the enzymes, aminopyrine demethylase and benzo[a]pyrene hydroxylase of livers from the partially hepatectomized or sham-operated rats fed trypsin and the other enzyme diets, presented no significant changes in the respective levels. The possible action of dietary trypsin in conjunction with inhibitors and growth factors controlling liver regeneration is discussed.
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PMID:Liver regeneration in trypsin-fed partially hepatectomized rats. 843 34

Histone lysine methylation is regarded as a very stable modification with important functions in epigenetic gene control and for organizing chromatin domains. While more robust modifications of the chromatin template are essential to stabilize epigenetic information, there is now the first evidence for a histone lysine demethylase that reverts an activating methyl mark to the unmodified state (Shi et al., 2004 [this issue of Cell]).
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PMID:A crack in histone lysine methylation. 1562 Mar 53

Histone modifications mediate changes in gene expression by altering the underlying chromatin structure or by serving as a binding platform to recruit other proteins. One such modification, histone methylation, was thought to be irreversible until last year when Shi and co-workers broke new ground with their discovery of a lysine-specific histone demethylase (LSD 1). They showed that LSD 1, a nuclear amine oxidase homolog, is a bona fide histone H3 lysine 4 demethylase (Shi et al., 2004). Now, a new study from published in a recent issue of Molecular Cell, together with two studies recently published by and in Nature, reveal that LSD 1's specificity and activity is in fact regulated by associated protein cofactors.
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PMID:Taking LSD 1 to a new high. 1562 Mar 53

Covalent modification of histones has an important role in regulating chromatin dynamics and transcription. Whereas most covalent histone modifications are reversible, until recently it was unknown whether methyl groups could be actively removed from histones. Using a biochemical assay coupled with chromatography, we have purified a novel JmjC domain-containing protein, JHDM1 (JmjC domain-containing histone demethylase 1), that specifically demethylates histone H3 at lysine 36 (H3-K36). In the presence of Fe(ii) and alpha-ketoglutarate, JHDM1 demethylates H3-methyl-K36 and generates formaldehyde and succinate. Overexpression of JHDM1 reduced the level of dimethyl-H3-K36 (H3K36me2) in vivo. The demethylase activity of the JmjC domain-containing proteins is conserved, as a JHDM1 homologue in Saccharomyces cerevisiae also has H3-K36 demethylase activity. Thus, we identify the JmjC domain as a novel demethylase signature motif and uncover a protein demethylation mechanism that is conserved from yeast to human.
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PMID:Histone demethylation by a family of JmjC domain-containing proteins. 1636 57

Histone methylation is unique among post-translational histone modifications by virtue of its stability. It is thought to be a relatively stable and heritable epigenetic mark for gene-specific regulation. In this study, we use quantitative in situ approaches to investigate the cell cycle dynamics of methylated isoforms of histone H3 lysine 9. Contrary to the expected stability of trimethylated lysines, our results for trimethylated lysine 9 (tMeK9) of H3 demonstrate that the genomic content of this methylation undergoes significant changes as cells progress through mitosis. Unexpectedly, there is a loss of tMeK9 that appears to reflect a robust demethylase activity that is active during the period between anaphase and cytokinesis. Subsequent investigations of mitoses in tMeK9-deficient cells revealed defects in chromosome congression and segregation that are distinct from the increased cohesion at centromeres previously reported in association with the loss of tMeK9. Collectively, these results identify a mitosis-specific trimethylation of Lys9 in pericentromeric heterochromatin that functions in the faithful segregation of chromosomes.
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PMID:Dynamic changes in histone H3 lysine 9 methylations: identification of a mitosis-specific function for dynamic methylation in chromosome congression and segregation. 1637 53


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