The cytosolic aminotransferase VAS1 coordinates aromatic amino acid biosynthesis and metabolism.

The aromatic amino acids (AAAs) phenylalanine, tyrosine, and tryptophan are basic protein units and precursors of diverse specialized metabolites that are essential for plant growth. Despite their significance, the mechanisms that regulate AAA homeostasis remain elusive. Here, we identified a cytosolic aromatic aminotransferase, REVERSAL OF SAV3 PHENOTYPE 1 (VAS1), as a suppressor of () in Arabidopsis ().

Rational design of GDP‑D‑mannose mannosyl hydrolase for microbial L‑fucose production.

Background: L‑Fucose is a rare sugar that has beneficial biological activities, and its industrial production is mainly achieved with brown algae through acidic/enzymatic fucoidan hydrolysis and a cumbersome purification process. Fucoidan is synthesized through the condensation of a key substance, guanosine 5'‑diphosphate (GDP)‑L‑fucose. Therefore, a more direct approach for biomanufacturing L‑fucose could be the enzymatic degradation of GDP‑L‑fucose.

A widespread pathway for substitution of adenine by diaminopurine in phage genomes.

DNA modifications vary in form and function but generally do not alter Watson-Crick base pairing. Diaminopurine (Z) is an exception because it completely replaces adenine and forms three hydrogen bonds with thymine in cyanophage S-2L genomic DNA. However, the biosynthesis, prevalence, and importance of Z genomes remain unexplored.

A Cost-Effective Method for Preparing Robust and Conductive Superhydrophobic Coatings Based on Asphalt.

The wide application of superhydrophobic materials is mainly hindered by the poor mechanical robustness and complicated preparation method. To overcome these problems, we tried to make a combination of hierarchical and self-similar structure by the means of a simple spraying method. By adding nanofiller (carbon nanotube) and microfiller (graphite powder and expanded graphite), the hierarchical structure was constructed.

Programmable adenine deamination in bacteria using a Cas9-adenine-deaminase fusion.

Precise genetic manipulation is vital to studying bacterial physiology, but is difficult to achieve in some bacterial species due to the weak intrinsic homologous recombination (HR) capacity and lack of a compatible exogenous HR system. Here we report the establishment of a rapid and efficient method for directly converting adenine to guanine in bacterial genomes using the fusion of an adenine deaminase and a Cas9 nickase. The method achieves the conversion of adenine to guanine an enzymatic deamination reaction and a subsequent DNA replication process rather than HR, which is utilized in conventional bacterial genetic manipulation methods, thereby substantially simplifying the genome editing process.

Purification, characterization, and application of a high activity 3-ketosteroid-Δ-dehydrogenase from Mycobacterium neoaurum DSM 1381.

Δ-Dehydrogenation is one of the most important reactions for steroid drug modification. Numerous 3-ketosteroid-Δ-dehydrogenases (KstDs) catalyzing this reaction were observed in various organisms. However, only a few have been characterized and used for substrate conversion.