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Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris.
Through three rounds of directed evolution by random point mutagenesis and screening, a 40-fold increase in total HRP activity is obtained in the S.cerevisiae culture supernatant compared with wild-type. Expand
Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae.
This work used random mutagenesis, recombination, and screening to identify HRP-C mutants that are more active and stable to incubation in hydrogen peroxide at 50 degrees C and a single mutation in the HRP active site was found to improve thermal stability. Expand
Repression of Acinetobacter vanillate demethylase synthesis by VanR, a member of the GntR family of transcriptional regulators.
Reverse transcriptase-polymerase chain reaction was used to demonstrate that control of vanAB was exerted at the level of transcription, and it was shown that vanillate is converted to protocatechuate by the action of vanillsate demethylase encoded by vanAB. Expand
2-Naphthoate catabolic pathway in Burkholderia strain JT 1500
The proposed pathway for the conversion of 2-naphthoate to 1 mol (each) of pyruvate, succinate, and acetyl coenzyme A and 2 mol of CO2 suggests that one of the other three diastereomers is not eliminated as a potential intermediate for a dehydration reaction. Expand
Stereochemical course of two arene-cis-diol dehydrogenases specifically induced in Pseudomonas putida
1H nuclear magnetic resonance experiments for two diol dehydrogenases induced during growth of Pseudomonas putida PaW1(TOL) and JT105 with p-xylene and p-toluate with unexpected lack of stereo- and regioselectivity was supported by kinetic isotope effect studies. Expand
Biohydroxylation of 2-naphthoic acid by Pseudomonas testosteroni: absolute configuration of (1R,2S)-2-carboxy-cis-1,2-dihydro-1,2-dihydroxynaphthalene
Abstract The absolute stereochemistry of the 2-carboxy-cis-1,2-dihydro-1,2-dihydroxynaphthalene, a diol produced by Pseudomonas testosteroni A3C, was shown by X-ray crystal analysis to be 1R,2S