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nitriles (22) 22
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Catalysis Science and Technology, ISSN 2044-4753, 2019, Volume 9, Issue 3, pp. 842 - 853
Enzymatic transformations of the nitrile group are important in biology as well as in synthetic chemistry. The enzyme QueF catalyses the conversion of... 
STRUCTURAL INSIGHTS | SITE | MECHANISM | TETRAMER BINDING | BIOSYNTHESIS | OXIDOREDUCTASE | CHEMISTRY, PHYSICAL | CONVERTING ENZYMES | TRANSFER-RNA | AROMATIC NITRILES | REVEALS
Journal Article
ACS Catalysis, ISSN 2155-5435, 06/2015, Volume 5, Issue 6, pp. 3740 - 3751
The NADPH-dependent QueF nitrile reductases catalyze the unprecedented four-electron reduction of nitrile to amine. QueF nitrile reductases can be found in the... 
covalent intermediate | enzyme catalysis | transition state | biocatalyst | nitrile reductase | SITE | MOLECULAR-ORBITAL METHODS | CHEMISTRY, PHYSICAL | DEHYDROGENASE | ONIOM | BIOSYNTHESIS | HYDRATASE | BASIS-SETS | SIMULATIONS | EXPRESSION
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 10, pp. 3720 - 3733
Journal Article
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 01/2017, Volume 85, Issue 1, pp. 103 - 116
ABSTRACT The tunneling‐fold (T‐fold) structural superfamily has emerged as a versatile protein scaffold of diverse catalytic activities. This is especially... 
7‐cyano‐7‐deazaguanine | 7‐deazaguanosine | thioimide | T‐fold | amidinotransferase | transfer‐RNA | modified nucleoside | QueF‐L | preQ0 | tunneling‐fold enzyme | RECRUITMENT | 7-deazaguanosine | MECHANISM | tunneling-fold enzyme | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | NUCLEOSIDE-Q | transfer-RNA | ENZYMATIC-SYNTHESIS | QUEUOSINE | BASE | BIOPHYSICS | BIOSYNTHESIS | GUANINE TRANSGLYCOSYLASE | preQ | T-fold | ARCHAEAL TRANSFER-RNA | QueF-L | 7-cyano-7-deazaguanine | Protein Multimerization | RNA, Archaeal - chemistry | Archaeal Proteins - chemistry | Substrate Specificity | Amidinotransferases - genetics | Crystallography, X-Ray | Pyrimidinones - metabolism | Protein Subunits - metabolism | Pyrimidinones - chemistry | Guanosine - chemistry | Cloning, Molecular | Escherichia coli - metabolism | RNA, Transfer - genetics | Archaeal Proteins - genetics | Protein Interaction Domains and Motifs | Amidinotransferases - chemistry | RNA, Archaeal - genetics | RNA, Transfer - chemistry | Protein Subunits - genetics | Archaeal Proteins - metabolism | Guanosine - analogs & derivatives | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Pyrroles - metabolism | Catalytic Domain | Gene Expression | RNA Processing, Post-Transcriptional | Pyrobaculum - enzymology | RNA, Transfer - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Guanosine - metabolism | Amidinotransferases - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | RNA, Archaeal - metabolism | Protein Binding | Pyrroles - chemistry | Molecular Docking Simulation | Protein Subunits - chemistry | Pyrobaculum - genetics | Enzymes | Cysteine | Analysis | Crystals | Physiological aspects | Nitriles | Phylogeny | Structure | Transfer RNA | Tunneling-fold enzyme
Journal Article
ChemBioChem, ISSN 1439-4227, 05/2020, Volume 21, Issue 10, pp. 1534 - 1543
The nitrile reductase QueF catalyzes NADPH‐dependent reduction of the nitrile group of preQ0 (7‐cyano‐7‐deazaguanine) into the primary amine of preQ1... 
NADPH | nitrile reductases | cofactors | C=C double bond hydration | hydration | Reductases | Reduction | NADH | Hydration | Mutagenesis | E coli | Nicotinamide adenine dinucleotide | Protonation | Biosynthesis | NADP | Substrates | Reductase | Index Medicus
Journal Article
Chemistry - A European Journal, ISSN 0947-6539, 05/2013, Volume 19, Issue 22, pp. 7007 - 7012
Nitrile reductase QueF catalyzes the reduction of 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one (preQ0) to 2-amino-5-aminomethylpyrrolo[2,3-d]pyrimidin-4-one... 
amines | enzyme catalysis | active site model | biocatalysis | nitrile reductase | CATALYZED SYNTHESIS | OXIDOREDUCTASE | CHEMISTRY, MULTIDISCIPLINARY | DISCOVERY | PRECISION | BIOTRANSFORMATION | (S)-OXYNITRILASE | FORCE-FIELD | HYDRATASE | SIMULATIONS | EXPRESSION | Enzymes | Bacteriology | Binding | Reductases | Residues | Reduction | Amines | Nitriles | Amino acids
Journal Article
ChemBioChem, ISSN 1439-4227, 03/2018, Volume 19, Issue 5, pp. 521 - 526
Journal Article
Catalysis Science & Technology, ISSN 2044-4753, 06/2016, Volume 6, Issue 20, pp. 7391 - 7397
Nitrile reductases catalyse a two-step reduction of nitriles to amines. This requires the binding of two NADPH molecules during one catalytic cycle. For the... 
Journal Article
Catalysis Science and Technology, ISSN 2044-4753, 2016, Volume 6, Issue 20, pp. 7391 - 7397
Nitrile reductases catalyse a two-step reduction of nitriles to amines. This requires the binding of two NADPH molecules during one catalytic cycle. For the... 
CHEMISTRY, PHYSICAL | QUEF | ENZYME | HYDROGENATION | MECHANISM | INSIGHT | Binding | Reductases | Catalysts | Pocket | Nitriles | Catalysis | Mass spectrometry | Substrates
Journal Article
Journal of Molecular Catalysis. B, Enzymatic, ISSN 1381-1177, 09/2016, Volume 131, pp. 47 - 54
[Display omitted] •A new nitrile reductase with a specific activity three times of the highest value was cloned from Pectobacterium carotovorum.•The enzyme was... 
Biochemical properties | Nitriles | Nitrile reductase | Biocatalysis | Genome data mining | FOLD | QUEF | MECHANISM | RNA | OXIDOREDUCTASE | CHEMISTRY, PHYSICAL | INSIGHT | QUEUOSINE | BIOSYNTHESIS
Journal Article
Catalysis Science and Technology, ISSN 2044-4753, 8/2014, Volume 4, Issue 9, pp. 2871 - 2876
Nitrile-containing compounds are widely manufactured and extensively used in the chemical and pharmaceutical industries as synthetic intermediates or... 
FOLD | ANGSTROM RESOLUTION | COMPUTATIONAL ENZYME DESIGN | QUEF | GTP CYCLOHYDROLASE-I | ALDEHYDE DEHYDROGENASE | CRYSTAL-STRUCTURE | REACTION-MECHANISM | CHEMISTRY, PHYSICAL | HYDRATASE | QUEUOSINE-BIOSYNTHESIS
Journal Article