FQR1 is a novel primary auxin-response gene that codes for a flavin mononucleotide-binding flavodoxin-like quinone reductase. Accumulation of FQR1 mRNA begins within 10 min of indole-3-acetic acid application and reaches a maximum of approximately 10-fold induction 30 min after treatment. This increase in FQR1 mRNA abundance is not diminished by the protein synthesis inhibitor cycloheximide, de...

The ene-reductases mediated bioreduction of a selection of open-chain α-alkyl-β-aryl enones afforded the corresponding saturated α-chiral ketones in high yield and optical purity in several cases. The stereo-electronic requirements of the reaction have been investigated, considering the nature and location of substituents on the aromatic ring as well as the steric hindrance at the α-position an...

From a single amethopterin-resistant organism, Streptococcus faecium var. durans strain A, two different dihydrofolate reductases have been obtained as essentially homogeneous proteins in good yield. One of the reductases has a similar substrate specificity and turnover number (about 8000 moles per min per mole of enzyme) to the single reductase found in the amethopterin-sensitive strain of S. ...

N-Substituted α-amino esters are widely used as chiral intermediates in a range of pharmaceuticals. Here we report the enantioselective biocatalyic synthesis N-substituted through direct reductive coupling α-ketoesters and amines employing sequence diverse metagenomic imine reductases (IREDs). Both enantiomers were obtained with high conversion excellent enantioselectivity under mild reaction c...

Preliminary evidence is presented that indicates that the dihydrofolate reductase activity of amethopterin-sensitive Streptococcus faecium var. durans ATCC 8043 is separable into two dihydrofolate reductases, one of which also reduces folate.

Streptomyces coelicolor is an obligate aerobic, filamentous soil-dwelling bacterium. Remarkably, the genome of S. coelicolor has three copies of the narGHJI operon that encodes respiratory nitrate reductase. This review summarizes our current views on the requirements for multiple nitrate reductases in S. coelicolor.

Nitrate analysis in water is one of the most frequently applied methods in environmental chemistry. Current methods for nitrate are generally based on toxic substances. Here, we show that a viable alternative method is to use the enzyme nitrate reductase. The key to applying this Green Chemistry solution for nitrate analysis is plentiful, inexpensive, analytical grade enzyme. We demonstrate tha...

We have reported the use of carboxylate-alumoxanes as efficient nucleating agents for isotactic polypropylene (iPP) with a possible structural correlation to the nucleation efficiency. The unique, butterfly-like structure of carboxylate-alumoxanes correlates well with the nucleation characteristics of iPP and, for the first time, the impact of a thermally induced, crystalline transition of carb...

The article reviews the state of knowledge on the biosynthesis of cardenolides in the genus Digitalis. It summarizes studies with labelled and unlabelled precursors leading to the formulation of the putative cardenolide pathway. Alternative pathways of cardenolide biosynthesis are discussed as well. Special emphasis is laid on enzymes involved in either pregnane metabolism or the modification o...

Development of artificial systems, capable of delivering electrons to metal-based catalysts for the reductive activation of dioxygen, has been proven very difficult for decades, constituting a major scientific lock for the elaboration of environmentally friendly oxidation processes. Here we demonstrate that the incorporation of a flavin mononucleotide (FMN) in a water-soluble polymer, bearing a...