Database : MEDLINE
Search on : Enzyme and Precursors [Words]
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[PMID]: 29514286
[Au] Autor:Zhang S; Gilbert ER; Noonan KJT; Saremi B; Wong EA
[Ad] Address:Department of Animal and Poultry Sciences, Virginia Tech, Blacksburg, VA 24061.
[Ti] Title:Gene expression and activity of methionine converting enzymes in broiler chickens fed methionine isomers or precursors.
[So] Source:Poult Sci;, 2018 Mar 05.
[Is] ISSN:1525-3171
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Common dietary supplemental methionine (Met) sources include DL-methionine (DL-Met) and the Met precursor DL-2-hydroxy-4-(methylthio) butanoic acid (DL-HMTBA). For bio-utilization, D-Met and DL-HMTBA are converted into L-Met through oxidation and transamination. The objective of this study was to determine the effect of different dietary supplemental Met sources on gene expression and enzyme activity of Met oxidases in male broiler chickens. Liver, muscle, duodenum, jejunum, and ileum were collected at days 10 (d 10), 21 (d 21), and 26 (d 26) post-hatch from male broiler chickens that were fed a basal diet deficient in sulfur amino acids (SAA) (control), or the control diet supplemented with DL-Met, L-Met, or DL-HMTBA to meet SAA requirements. The mRNA abundance of D-Met oxidase, L-HMTBA oxidase, and D-HMTBA oxidase was measured by real-time PCR, and oxidase activities were measured using colorimetric assays (n = 5). Liver expressed more D- and L-HMTBA oxidase mRNA, while breast muscle and liver expressed more D-Met oxidase mRNA than other tissues. In the liver, DL-HMTBA and L-Met supplementation were associated with greater mRNA abundance of L-HMTBA oxidase compared to the control diet-fed group at d 10 but not d 21 or d 26. DL-HMTBA supplementation, however, was not associated with changes in the mRNA abundance of D-HMTBA oxidase. The Met-deficient diet at d 26 was associated with greater hepatic abundance of DAO mRNA, which is responsible for oxidation of amino acids. Oxidase activities were similar among the Met deficient and Met-supplemented groups. In conclusion, dietary Met supplementation influenced the transcriptional regulation and activity of Met oxidases in a tissue and age-specific manner. Met oxidases may thus act as a determining factor in the bioefficacy of different dietary supplemental Met sources.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:Publisher
[do] DOI:10.3382/ps/pey037

  2 / 27614 MEDLINE  
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[PMID]: 29513045
[Au] Autor:Burcul F; Generalic Mekinic I; Radan M; Rollin P; Blazevic I
[Ad] Address:a Department of Analytical Chemistry, Faculty of Chemistry and Technology , University of Split , Split , Croatia.
[Ti] Title:Isothiocyanates: cholinesterase inhibiting, antioxidant, and anti-inflammatory activity.
[So] Source:J Enzyme Inhib Med Chem;33(1):577-582, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Finding a new type of cholinesterase inhibitor that would overcome the brain availability and pharmacokinetic parameters or hepatotoxic liability has been a focus of investigations dealing with the treatment of Alzheimer's disease. Isothiocyanates have not been previously investigated as potential cholinesterase inhibitors. These compounds can be naturally produced from their glucosinolate precursors, secondary metabolites widely distributed in our daily Brassica vegetables. Among 11 tested compounds, phenyl isothiocyanate and its derivatives showed the most promising inhibitory activity. 2-Methoxyphenyl ITC showed best inhibition on acetylcholinesterase with IC of 0.57 mM, while 3-methoxyphenyl ITC showed the best inhibition on butyrylcholinesterase having 49.2% at 1.14 mM. Assessment of the antioxidant efficacy using different methods led to a similar conclusion. The anti-inflammatory activity was also tested using human COX-2 enzyme, ranking phenyl isothiocyanate, and 3-methoxyphenyl isothiocyanate as most active, with ∼99% inhibition at 50 µM.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Process
[do] DOI:10.1080/14756366.2018.1442832

  3 / 27614 MEDLINE  
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[PMID]: 29512899
[Au] Autor:Simithy J; Sidoli S; Garcia BA
[Ad] Address:Epigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
[Ti] Title:Integrating Proteomics and Targeted Metabolomics to Understand Global Changes in Histone Modifications.
[So] Source:Proteomics;, 2018 Mar 07.
[Is] ISSN:1615-9861
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:The chromatin fiber is the control panel of eukaryotic cells. Chromatin is mostly composed of DNA, which contains the genetic instruction for cell phenotype, and histone proteins, which provide the scaffold for chromatin folding and part of the epigenetic inheritance. Histone writers/erasers "flag" chromatin regions by catalyzing/removing covalent histone post-translational modifications (PTMs). Histone PTMs chemically contribute to chromatin relaxation or compaction and recruit histone readers to modulate DNA readout. The precursors of protein PTMs are mostly small metabolites. For instance, acetyl-CoA is used for acetylation, ATP for phosphorylation, and S-adenosyl methionine for methylation. Interestingly, PTMs such as acetylation can occur at neutral pH also without their respective enzyme when the precursor is sufficiently concentrated. Therefore, it is essential to differentially quantify the contribution of histone writers/erasers vs the effect of local concentration of metabolites to understand the primary regulation of histone PTM abundance. Aberrant phenotypes such as cancer cells have misregulated metabolism and thus the composition and the modulation of chromatin is not only driven by enzymatic tuning. In this review, we discuss the latest advances in mass spectrometry (MS) to analyze histone PTMs and the most adopted quantification methods for related metabolites, both necessary to understand PTM relative changes. This article is protected by copyright. All rights reserved.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:Publisher
[do] DOI:10.1002/pmic.201700309

  4 / 27614 MEDLINE  
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[PMID]: 29507322
[Au] Autor:Cova M; López-Gutiérrez B; Artigas-Jerónimo S; González-Díaz A; Bandini G; Maere S; Carretero-Paulet L; Izquierdo L
[Ad] Address:ISGlobal, Barcelona Ctr. Int. Health Res. (CRESIB), Hospital Clínic - Universitat de Barcelona, Barcelona, Spain.
[Ti] Title:The Apicomplexa-specific glucosamine-6-phosphate N-acetyltransferase gene family encodes a key enzyme for glycoconjugate synthesis with potential as therapeutic target.
[So] Source:Sci Rep;8(1):4005, 2018 Mar 05.
[Is] ISSN:2045-2322
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Apicomplexa form a phylum of obligate parasitic protozoa of great clinical and veterinary importance. These parasites synthesize glycoconjugates for their survival and infectivity, but the enzymatic steps required to generate the glycosylation precursors are not completely characterized. In particular, glucosamine-phosphate N-acetyltransferase (GNA1) activity, needed to produce the essential UDP-N-acetylglucosamine (UDP-GlcNAc) donor, has not been identified in any Apicomplexa. We scanned the genomes of Plasmodium falciparum and representatives from six additional main lineages of the phylum for proteins containing the Gcn5-related N-acetyltransferase (GNAT) domain. One family of GNAT-domain containing proteins, composed by a P. falciparum sequence and its six apicomplexan orthologs, rescued the growth of a yeast temperature-sensitive GNA1 mutant. Heterologous expression and in vitro assays confirmed the GNA1 enzymatic activity in all lineages. Sequence, phylogenetic and synteny analyses suggest an independent origin of the Apicomplexa-specific GNA1 family, parallel to the evolution of a different GNA1 family in other eukaryotes. The inability to disrupt an otherwise modifiable gene target suggests that the enzyme is essential for P. falciparum growth. The relevance of UDP-GlcNAc for parasite viability, together with the independent evolution and unique sequence features of Apicomplexa GNA1, highlights the potential of this enzyme as a selective therapeutic target against apicomplexans.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:In-Data-Review
[do] DOI:10.1038/s41598-018-22441-3

  5 / 27614 MEDLINE  
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[PMID]: 29506985
[Au] Autor:Vignali D; Cantarelli E; Bordignon C; Canu A; Citro A; Annoni A; Piemonti L; Monti P
[Ad] Address:San Raffaele Diabetes Research Institute, IRCCS San Raffaele Scientific Institute, Milan, Italy.
[Ti] Title:Detection and Characterization of CD8+ Autoreactive Memory Stem T Cells in Patients with Type 1 Diabetes.
[So] Source:Diabetes;, 2018 Mar 05.
[Is] ISSN:1939-327X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Stem memory T cells (Tscm) constitute the earliest developmental stage of memory T cells, displaying stem cell-like properties such as self-renewal capacity. Their superior immune reconstitution potential has sparked interest in cancer immune-therapy, vaccine development and immune reconstitution, whereas their role in autoimmunity is largely unexplored. Here we show that autoreactive CD8+ Tscm specific for ß cell antigens GAD65, insulin and IGRP are present in patients with type 1 diabetes (T1D). generation of autoreactive Tscm from naïve precursors required the presence of the homeostatic cytokine interleukin-7 (IL-7). IL-7 promotes glucose uptake via overexpression of the glucose transporter GLUT-1 and up-regulation of the glycolytic enzyme hexokinase II. Even though metabolism depends on glucose uptake, the subsequent oxidation of pyruvate in the mitochondria was necessary for Tscm generation from naïve precursors. In patients with T1D, high expression of GLUT1 was a hallmark of circulating Tscm and targeting glucose uptake via GLUT-1 using the selective inhibitor WZB117 resulted in inhibition of Tscm generation and expansion. Our results suggest that autoreactive Tscm are present in patients with T1D and can be selectively targeted by inhibition of glucose metabolism.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:Publisher

  6 / 27614 MEDLINE  
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[PMID]: 29413944
[Au] Autor:Ghosh S; Ahmad R; Gautam VK; Khare SK
[Ad] Address:Enzyme and Microbial Biochemistry Laboratory, Department of Chemistry, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India.
[Ti] Title:Cholesterol-oxidase-magnetic nanobioconjugates for the production of 4-cholesten-3-one and 4-cholesten-3, 7-dione.
[So] Source:Bioresour Technol;254:91-96, 2018 Apr.
[Is] ISSN:1873-2976
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Cholesterol oxidase(ChOx) enzyme isolated from Pseudomonas aeruginosa PseA(ChOxP) and Rhodococcus erythropolis MTCC 3951(ChOxR) strains as well as a commercial variant produced by Streptomyces sp.(ChOxS) were immobilized on silane modified iron(II, III)oxide magnetic nanoparticles(MNP) by covalent coupling methods. The nanobiocatalysts in case of ChOxP, ChOxR and ChOxS, retained 71, 91 and 86% of cholesterol oxidase activity respectively, as compared to their soluble counterparts. The catalytic efficiency of the immobilized enzymes on nanoparticles was more than 2.0 times higher than the free enzyme. They also showed enhanced pH and thermal stability. After 10 cycles of operation, the MNP-bioconjugates retained 50, 52 and 51% of residual activity in case of ChOxP, ChOxR and ChOxS respectively. The presence of enzyme on nanoparticles was confirmed by FTIR, SEM and TEM. The nanobiocatalysts were used for the biotransformation of cholesterol and 7-ketocholesterol to 4-cholesten-3-one and 4-cholesten-3, 7-dione respectively, which are industrially and medically important steroid precursors.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[St] Status:In-Process

  7 / 27614 MEDLINE  
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[PMID]: 29340834
[Au] Autor:Smiljanic K; Todorovic S; Mladenovic Djordjevic A; Vanmierlo T; Lütjohann D; Ivkovic S; Kanazir S
[Ad] Address:Department of Neurobiology, Institute for Biological Research "Sinisa Stankovic", University of Belgrade, Belgrade, Serbia.
[Ti] Title:Limited daily feeding and intermittent feeding have different effects on regional brain energy homeostasis during aging.
[So] Source:Biogerontology;19(2):121-132, 2018 Apr.
[Is] ISSN:1573-6768
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Albeit aging is an inevitable process, the rate of aging is susceptible to modifications. Dietary restriction (DR) is a vigorous nongenetic and nonpharmacological intervention that is known to delay aging and increase healthspan in diverse species. This study aimed to compare the impact of different restricting feeding regimes such as limited daily feeding (LDF, 60% AL) and intermittent feeding (IF) on brain energy homeostasis during aging. The analysis was focused on the key molecules in glucose and cholesterol metabolism in the cortex and hippocampus of middle-aged (12-month-old) and aged (24-month-old) male Wistar rats. We measured the impact of different DRs on the expression levels of AMPK, glucose transporters (GLUT1, GLUT3, GLUT4), and the rate-limiting enzyme in the cholesterol synthesis pathway (HMGCR). Additionally, we assessed the changes in the amounts of cholesterol, its metabolite, and precursors following LDF and IF. IF decreased the levels of AMPK and pAMPK in the cortex while the increased levels were detected in the hippocampus. Glucose metabolism was more affected in the cortex, while cholesterol metabolism was more influenced in the hippocampus. Overall, the hippocampus was more resilient to the DRs, with fewer changes compared to the cortex. We showed that LDF and IF differently affected the brain energy homeostasis during aging and that specific brain regions exhibited distinct vulnerabilities towards DRs. Consequently, special attention should be paid to the DR application among elderly as different phases of aging do not respond equally to altered nutritional regimes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180303
[Lr] Last revision date:180303
[St] Status:In-Data-Review
[do] DOI:10.1007/s10522-018-9743-y

  8 / 27614 MEDLINE  
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[PMID]: 29180590
[Au] Autor:Wellner K; Czech A; Ignatova Z; Betat H; Mörl M
[Ad] Address:Institute for Biochemistry, Leipzig University, Leipzig 04103, Germany.
[Ti] Title:Examining tRNA 3'-ends in : teamwork between CCA-adding enzyme, RNase T, and RNase R.
[So] Source:RNA;24(3):361-370, 2018 Mar.
[Is] ISSN:1469-9001
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:tRNA maturation and quality control are crucial for proper functioning of these transcripts in translation. In several organisms, defective tRNAs were shown to be tagged by poly(A) or CCACCA tails and subsequently degraded by 3'-exonucleases. In a deep-sequencing analysis of tRNA 3'-ends, we detected the CCACCA tag also in However, this tag closely resembles several 3'-trailers of tRNA precursors targeted for maturation and not for degradation. Here, we investigate the ability of two important exonucleases, RNase R and RNase T, to distinguish tRNA precursors with a native 3'-trailer from tRNAs with a CCACCA tag. Our results show that the degrading enzyme RNase R breaks down both tRNAs primed for degradation as well as precursor transcripts, indicating that it is a rather nonspecific RNase. RNase T, a main processing exonuclease involved in trimming of 3'-trailers, is very inefficient in converting the CCACCA-tagged tRNA into a mature transcript. Hence, while both RNases compete for trailer-containing tRNA precursors, the inability of RNase T to process CCACCA tails ensures that defective tRNAs cannot reenter the functional tRNA pool, representing a safeguard to avoid detrimental effects of tRNAs with erroneous integrity on protein synthesis. Furthermore, these data indicate that the RNase T-mediated end turnover of the CCA sequence represents a means to deliver a tRNA to a repeated quality control performed by the CCA-adding enzyme. Hence, originally described as a futile side reaction, the tRNA end turnover seems to fulfill an important function in the maintenance of the tRNA pool in the cell.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 180301
[Lr] Last revision date:180301
[St] Status:In-Data-Review
[do] DOI:10.1261/rna.064436.117

  9 / 27614 MEDLINE  
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[PMID]: 28451635
[Au] Autor:Moyon S; Ma D; Huynh JL; Coutts DJC; Zhao C; Casaccia P; Franklin RJM
[Ad] Address:Department of Neuroscience, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
[Ti] Title:Efficient Remyelination Requires DNA Methylation.
[So] Source:eNeuro;4(2), 2017 Mar-Apr.
[Is] ISSN:2373-2822
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Oligodendrocyte progenitor cells (OPCs) are the principal source of new myelin in the central nervous system. A better understanding of how they mature into myelin-forming cells is of high relevance for remyelination. It has recently been demonstrated that during developmental myelination, the DNA methyltransferase 1 (DNMT1), but not DNMT3A, is critical for regulating proliferation and differentiation of OPCs into myelinating oligodendrocytes (OLs). However, it remains to be determined whether DNA methylation is also critical for the differentiation of adult OPCs during remyelination. After lysolecithin-induced demyelination in the ventrolateral spinal cord white matter of adult mice of either sex, we detected increased levels of DNA methylation and higher expression levels of the DNA methyltransferase DNMT3A and lower levels of DNMT1 in differentiating adult OLs. To functionally assess the role of DNMT1 and DNMT3 in adult OPCs, we used mice with inducible and lineage-specific ablation of and/or (i.e., , ). Upon lysolecithin injection in the spinal cord of these transgenic mice, we detected defective OPC differentiation and inefficient remyelination in the null and null mice, but not in the null mice. Taken together with previous results in the developing spinal cord, these data suggest an age-dependent role of distinct DNA methyltransferases in the oligodendrocyte lineage, with a dominant role for DNMT1 in neonatal OPCs and for DNMT3A in adult OPCs.
[Mh] MeSH terms primary: DNA (Cytosine-5-)-Methyltransferase 1/metabolism
DNA (Cytosine-5-)-Methyltransferases/metabolism
DNA Methylation
Oligodendrocyte Precursor Cells/metabolism
Remyelination
Spinal Cord/metabolism
[Mh] MeSH terms secundary: Animals
DNA (Cytosine-5-)-Methyltransferase 1/genetics
DNA (Cytosine-5-)-Methyltransferases/genetics
Demyelinating Diseases/chemically induced
Demyelinating Diseases/metabolism
Female
Lysophosphatidylcholines/administration & dosage
Male
Mice, Inbred C57BL
Mice, Knockout
Oligodendrocyte Precursor Cells/ultrastructure
White Matter/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Lysophosphatidylcholines); EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferase 1); EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferases); EC 2.1.1.37 (DNA methyltransferase 3A); EC 2.1.1.37 (Dnmt1 protein, mouse)
[Em] Entry month:1801
[Cu] Class update date: 180228
[Lr] Last revision date:180228
[Js] Journal subset:IM
[Da] Date of entry for processing:170429
[St] Status:MEDLINE

  10 / 27614 MEDLINE  
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[PMID]: 29338056
[Au] Autor:Tien C; Huang L; Watanabe SM; Speidel JT; Carter CA; Chen C
[Ad] Address:Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado, United States of America.
[Ti] Title:Context-dependent autoprocessing of human immunodeficiency virus type 1 protease precursors.
[So] Source:PLoS One;13(1):e0191372, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:HIV-1 protease autoprocessing is responsible for liberation of free mature protease (PR) from the Gag-Pol polyprotein precursor. A cell-based model system was previously developed to examine the autoprocessing mechanism of fusion precursors carrying the p6*-PR miniprecursor sandwiched between various proteins or epitopes. We here report that precursor autoprocessing is context-dependent as its activity and outcomes can be modulated by sequences upstream of p6*-PR. This was exemplified by the 26aa maltose binding protein (MBP) signal peptide (SigP) when placed at the N-terminus of a fusion precursor. The mature PRs released from SigP-carrying precursors are resistant to self-degradation whereas those released from SigP-lacking fusion precursors are prone to self-degradation. A H69D mutation in PR abolished autoprocessing of SigP-containing fusion precursors whereas it only partially suppressed autoprocessing of fusion precursors lacking SigP. An autoprocessing deficient GFP fusion precursor with SigP exhibited a subcellular distribution pattern distinct from the one without it in transfected HeLa cells. Furthermore, a SigP fusion precursor carrying a substitution at the P1 position released the mature PR and PR-containing fragments that were different from those released from the precursor carrying the same mutation but lacking SigP. We also examined autoprocessing outcomes in viral particles produced by a NL4-3 derived proviral construct and demonstrated the existence of several PR-containing fragments along with the mature PR. Some of these resembled the SigP precursor autoprocessing outcomes. This finding of context-dependent modulation reveals the complexity of precursor autoprocessing regulation that most likely accompanies sequence variation imposed by the evolution of the upstream Gag moiety.
[Mh] MeSH terms primary: Enzyme Precursors/metabolism
HIV Protease/metabolism
HIV-1/enzymology
[Mh] MeSH terms secundary: Amino Acid Sequence
Enzyme Precursors/chemistry
Enzyme Precursors/genetics
HEK293 Cells
HIV Protease/chemistry
HIV Protease/genetics
Humans
Mutation
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Name of substance:0 (Enzyme Precursors); EC 3.4.23.- (HIV Protease); EC 3.4.23.- (p16 protease, Human immunodeficiency virus 1)
[Em] Entry month:1802
[Cu] Class update date: 180226
[Lr] Last revision date:180226
[Js] Journal subset:IM
[Da] Date of entry for processing:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191372


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