High-Affinity Fluorogenic Substrate for Tissue Transglutaminase Reveals Enzymatic Hysteresis.

Transglutaminases (TGases) are a family of calcium-dependent enzymes primarily known for their ability to cross-link proteins. Transglutaminase 2 (TG2) is one isozyme in this family whose role is multifaceted. TG2 can act not only as a typical transamidase through its catalytic core but also as a G-protein via its GTP binding site.

Electrospun nanofibers of cellulose acetate/metal organic framework-third generation PAMAM dendrimer for the removal of methylene blue from aqueous media.

In this research, magnetic metal-organic framework nanofibers were produced by the electrospinning method. The nanocomposite was functionalized by third generation hyperbranched poly(amidoamine) dendrimer (PAMAM) to improve its dye adsorption efficiency from aqueous media. The characteristics of the synthesized magnetic nanocomposite was determined by Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), energy-dispersive X-ray spectroscopy (EDS) along with elemental mapping analysis and scanning electron microscopy (SEM).

The reactivity of lactyl-oxythiamin implies the role of the amino-pyrimidine in thiamin catalyzed decarboxylation.

It has previously been established that the deprotonated amino substituent of the pyrimidine of thiamin diphosphate (ThDP) acts as an internal base to accept the C2H of the thiazolium in ThDP-dependent enzymes. The amino group has also been implicated in assisting the departure of the aldehydic product formed after loss of CO from ketoacid substrates. However, the potential role for the pyrimidine amino group in the key decarboxylation step has not been assessed.