Determination of the Quadrupole Splitting in Bulk n-GaAs by Warm-Up Spectroscopy

Semiconductors - We found bulk n-GaAs layers grown by liquid phase epitaxy to be irregularly stressed. Deformation created by this stress causes a small but detectable quadrupole splitting of...     

Steels for Bridge Structures

Metallurgist - We consider domestic and foreign standards for rolled metals used in bridge building. Domestic standards contain elevated requirements to the reliability of rolled metals in terms of...     

A Dynamic Inertial Weight Strategy in Micro PSO for Swarm Robots

Wireless Personal Communications - A relatively new area of research and development is Swarm Robotics. It is a part of the swarm intelligence field. In the proposed paper, we shall use swarm...     

Crossing the Border: From Keto- to Imine Reduction in Short-Chain Dehydrogenases/Reductases

The family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDRs) comprises numerous biocatalysts capable of C=O or C=C reduction. The highly homologous noroxomaritidine reductase (NR) from Narcissus sp. aff. pseudonarcissus and Zt_SDR from Zephyranthes treatiae, however, are SDRs with an extended imine substrate scope. Comparison with a similar SDR from Asparagus officinalis (Ao_SDR) exhibiting keto-reducing activity, yet negligible imine-reducing capability, and mining the Short-Chain Dehydrogenase/Reductase Engineering Database indicated that NR and Zt_SDR possess a unique active-site composition among SDRs. Adapting the active site of Ao_SDR accordingly improved its imine-reducing capability. By applying the same strategy, an unrelated SDR from Methylobacterium sp. 77 (M77_SDR) with distinct keto-reducing activity was engineered into a promiscuous enzyme with imine-reducing activity, thereby confirming that the ability to reduce imines can be rationally introduced into members of the “classical” SDR enzyme family. Thus, members of the SDR family could be a promising starting point for protein approaches to generate new imine-reducing enzymes.