Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium - Wikidata - awgldk - TriplyDB

Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium

Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium

http://www.wikidata.org/entity/Q24561818

about

Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea Type 3 lodothyronine deiodinase: cloning, in vitro expression, and functional analysis of the placental selenoenzyme Thioredoxin reductase Reconsidering the evolution of eukaryotic selenoproteins: a novel nonmammalian family with scattered phylogenetic distribution.Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases The molecular biology of selenocysteine Regulation of the extracellular antioxidant selenoprotein plasma glutathione peroxidase (GPx-3) in mammalian cells Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis Selective selC-independent selenocysteine incorporation into formate dehydrogenases Efficient CO2-reducing activity of NAD-dependent formate dehydrogenase from Thiobacillus sp. KNK65MA for formate production from CO2 gas Identification of a protein component of a mammalian tRNA(Sec) complex implicated in the decoding of UGA as selenocysteine.Selenium in chemistry and biochemistry in comparison to sulfur.Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.Selenocysteine inserting tRNAs: an overview.Genes for selenium dependent and independent formate dehydrogenase in the gut microbial communities of three lower, wood-feeding termites and a wood-feeding roach.The mononuclear molybdenum enzymes.A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family Trends in selenium biochemistry.Evolution of the metabolic and regulatory networks associated with oxygen availability in two phytopathogenic enterobacteria.Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis.A selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production.Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli.Genetic analysis of selenocysteine biosynthesis in the archaeon Methanococcus maripaludis Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli SelenoDB 1.0 : a database of selenoprotein genes, proteins and SECIS elements Genetic code flexibility in microorganisms: novel mechanisms and impact on physiology.Seleno-independent glutathione peroxidases. More than simple antioxidant scavengers.Facile Recoding of Selenocysteine in Nature Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase.[Facile Recoding of Selenocysteine in Nature].Spectroscopic and density functional theory studies of the blue-copper site in M121SeM and C112SeC azurin: Cu-Se versus Cu-S bonding.Genome-wide effects of selenium and translational uncoupling on transcription in the termite gut symbiont Treponema primitia.Translational recoding in archaea.Peptide ligation chemistry at selenol amino acids.The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.Molybdenum and tungsten-dependent formate dehydrogenases.

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P2860

Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium

http://www.wikidata.org/entity/Q24561818

description

1991 nî lūn-bûn

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1991 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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1991 թվականի հոտեմբերին հրատարակված գիտական հոդված

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1991年の論文

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1991年学术文章

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1991年学术文章

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1991年学术文章

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1991年学术文章

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1991年学术文章

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1991年學術文章

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name

Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Catalytic properties of an Esc ...... which sulfur replaces selenium

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Catalytic properties of an Esc ...... which sulfur replaces selenium

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P2093

A Böck

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M J Axley

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P2860

Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety

Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon

Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli

Type I iodothyronine deiodinase is a selenocysteine-containing enzyme

Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine.

Formic dehydrogenase and the hydrogenlyase enzyme complex in coli-aerogenes bacteria

Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component.

Escherichia coli genes whose products are involved in selenium metabolism.

Metalloselenonein, the selenium analogue of metallothionein: synthesis and characterization of its complex with copper ions.

Selenium biochemistry.

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scholarly article

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3121778

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19

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Thressa Stadtman

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Escherichia coli

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