indigo-carmine and 4-chloroindole

indigo-carmine has been researched along with 4-chloroindole* in 1 studies

Other Studies

1 other study(ies) available for indigo-carmine and 4-chloroindole

Article	Year
Identification of amino acid residues involved in 4-chloroindole 3-hydroxylation by cytochrome P450 2A6 using screening of random libraries. Journal of biotechnology, 2009, Jan-01, Volume: 139, Issue:1 Cytochrome P450 (P450) 2A6 is able to catalyze indole hydroxylation to form the blue dye indigo. The wild-type P450 2A6 enzyme was randomly mutated throughout the whole open reading frame and screened using 4-chloroindole hydroxylation, a substituted indole selected from 30 indole compounds for enhanced color development. Mutants with up to 5-fold increases of catalytic efficiency (k(cat)/K(m)) and 2-fold increases in k(cat) were selected after two rounds of screening. Important residues located both in (e.g., Thr305) and outside the active site (e.g., Ser224) were identified. The study utilized a better substrate for "indigo assay" to obtain new information on the structure-functional relationship of P450 2A6 that was not revealed by previous mutagenesis studies with this enzyme. Topics: Aryl Hydrocarbon Hydroxylases; Cytochrome P-450 CYP2A6; Databases, Protein; Escherichia coli; Humans; Hydroxylation; Indigo Carmine; Indoles; Kinetics; Membranes; Models, Chemical; Models, Molecular; Mutagenesis; Sequence Analysis, Protein	2009

Article

Year

Identification of amino acid residues involved in 4-chloroindole 3-hydroxylation by cytochrome P450 2A6 using screening of random libraries.

Journal of biotechnology, 2009, Jan-01, Volume: 139, Issue:1

Cytochrome P450 (P450) 2A6 is able to catalyze indole hydroxylation to form the blue dye indigo. The wild-type P450 2A6 enzyme was randomly mutated throughout the whole open reading frame and screened using 4-chloroindole hydroxylation, a substituted indole selected from 30 indole compounds for enhanced color development. Mutants with up to 5-fold increases of catalytic efficiency (k(cat)/K(m)) and 2-fold increases in k(cat) were selected after two rounds of screening. Important residues located both in (e.g., Thr305) and outside the active site (e.g., Ser224) were identified. The study utilized a better substrate for "indigo assay" to obtain new information on the structure-functional relationship of P450 2A6 that was not revealed by previous mutagenesis studies with this enzyme.

Topics: Aryl Hydrocarbon Hydroxylases; Cytochrome P-450 CYP2A6; Databases, Protein; Escherichia coli; Humans; Hydroxylation; Indigo Carmine; Indoles; Kinetics; Membranes; Models, Chemical; Models, Molecular; Mutagenesis; Sequence Analysis, Protein

2009