1-5-dihydro-fad and 5-methylindole

1-5-dihydro-fad has been researched along with 5-methylindole* in 1 studies

Other Studies

1 other study(ies) available for 1-5-dihydro-fad and 5-methylindole

Article	Year
Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination. Science (New York, N.Y.), 2005, Sep-30, Volume: 309, Issue:5744 Chlorinated natural products include vancomycin and cryptophycin A. Their biosynthesis involves regioselective chlorination by flavin-dependent halogenases. We report the structural characterization of tryptophan 7-halogenase (PrnA), which regioselectively chlorinates tryptophan. Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10 angstrom-long tunnel and bound by distinct enzyme modules. The FAD module is conserved in halogenases and is related to flavin-dependent monooxygenases. On the basis of biochemical studies, crystal structures, and by analogy with monooxygenases, we predict that FADH2 reacts with O2 to make peroxyflavin, which is decomposed by Cl-. The resulting HOCl is guided through the tunnel to tryptophan, where it is activated to participate in electrophilic aromatic substitution. Topics: Amino Acid Sequence; Binding Sites; Chlorides; Crystallography, X-Ray; Dimerization; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Hypochlorous Acid; Indoles; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Pseudomonas fluorescens; Tryptophan	2005

Article

Year

Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination.

Science (New York, N.Y.), 2005, Sep-30, Volume: 309, Issue:5744

Chlorinated natural products include vancomycin and cryptophycin A. Their biosynthesis involves regioselective chlorination by flavin-dependent halogenases. We report the structural characterization of tryptophan 7-halogenase (PrnA), which regioselectively chlorinates tryptophan. Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10 angstrom-long tunnel and bound by distinct enzyme modules. The FAD module is conserved in halogenases and is related to flavin-dependent monooxygenases. On the basis of biochemical studies, crystal structures, and by analogy with monooxygenases, we predict that FADH2 reacts with O2 to make peroxyflavin, which is decomposed by Cl-. The resulting HOCl is guided through the tunnel to tryptophan, where it is activated to participate in electrophilic aromatic substitution.

Topics: Amino Acid Sequence; Binding Sites; Chlorides; Crystallography, X-Ray; Dimerization; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Hypochlorous Acid; Indoles; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Pseudomonas fluorescens; Tryptophan

2005