Florian Hollfelder

TL;DR: A new member of this superfamily, a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum (R/PMH), is characterised both structurally and kinetically and represents a further example of conservation of the overall structure and mechanism within the alkaline phosphatase superfamily.

TL;DR: This review introduces the emerging approaches towards making biomimetic man-made compartments that are poised to be adapted by a wider circle of researchers.

TL;DR: In this paper, the importance of microdroplets in enabling new experiments in biology and chemistry is highlighted as well as the remaining technological challenges, and examples are presented to show how compartmentalization, monodispersity, single-molecule sensitivity, and high throughput have been exploited in experiments that would have been extremely difficult outside the microfluidics platform.

TL;DR: The limits and potential of substrate promiscuity of the adenylation domain of tyrocidine synthetase 1 were systematically explored and quantification of these factors provides ground rules for understanding and possibly evolving substrate specificity in this class of enzymes.

TL;DR: The evidence for widespread crosswise promiscuity amongst enzymes that catalyze phosphoryl transfer is reviewed, including several members of the alkaline phosphatase superfamily, where large rate accelerations between 10(6) and 10(17) are observed for both native and multiple promiscuous reactions.