Efficient synthesis of enantiopure amines from alcohols using resting cells and ammonia.

-Chiral amines are pivotal building blocks for chemical manufacturing. Stereoselective amination of alcohols is receiving increased interest due to its higher atom-efficiency and overall improved environmental footprint compared with other chemocatalytic and biocatalytic methods. We previously developed a hydrogen-borrowing amination by combining an alcohol dehydrogenase (ADH) with an amine dehydrogenase (AmDH) .

Lysosomes nor Mice Move Forward without Borcs7.

Lysosome function and position in the cytoplasm depends on the BORCS machinery, which tethers lysosomes to the kinesin microtubule motor. A recent paper of Snouwaert et al. in Cell Reports characterizes a mouse with a spontaneous mutation in the Borcs7 subunit, which causes axonal dystrophy and impaired motor function.

Concurrent presence of on- and off-pathway folding intermediates of apoflavodoxin at physiological ionic strength.

Flavodoxins have a protein topology that can be traced back to the universal ancestor of the three kingdoms of life. Proteins with this type of architecture tend to temporarily misfold during unassisted folding to their native state and form intermediates. Several of these intermediate species are molten globules (MGs), which are characterized by a substantial amount of secondary structure, yet without the tertiary side-chain packing of natively folded proteins.

Folding of proteins with a flavodoxin-like architecture.

The flavodoxin-like fold is a protein architecture that can be traced back to the universal ancestor of the three kingdoms of life. Many proteins share this α-β parallel topology and hence it is highly relevant to illuminate how they fold. Here, we review experiments and simulations concerning the folding of flavodoxins and CheY-like proteins, which share the flavodoxin-like fold.

The Ribosome Restrains Molten Globule Formation in Stalled Nascent Flavodoxin.

Folding of proteins usually involves intermediates, of which an important type is the molten globule (MG). MGs are ensembles of interconverting conformers that contain (non-)native secondary structure and lack the tightly packed tertiary structure of natively folded globular proteins. Whereas MGs of various purified proteins have been probed to date, no data are available on their presence and/or effect during protein synthesis.

Stalled flavodoxin binds its cofactor while fully exposed outside the ribosome.

Correct folding of proteins is crucial for cellular homeostasis. More than thirty percent of proteins contain one or more cofactors, but the impact of these cofactors on co-translational folding remains largely unknown. Here, we address the binding of flavin mononucleotide (FMN) to nascent flavodoxin, by generating ribosome-arrested nascent chains that expose either the entire protein or C-terminally truncated segments thereof.

Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase.

Enzyme mechanisms are often probed by structure-informed point mutations and measurement of their effects on enzymatic properties to test mechanistic hypotheses. In many cases, the challenge is to report on complex, often inter-linked elements of catalysis. Evidence for long-range effects on enzyme mechanism resulting from mutations remains sparse, limiting the design/redesign of synthetic catalysts in a predictable way.