Effect of posttranslational modifications on enzyme function and assembly.

The detailed examination of enzyme molecules by mass spectrometry and other techniques continues to identify hundreds of distinct PTMs. Recently, global analyses of enzymes using methods of contemporary proteomics revealed widespread distribution of PTMs on many key enzymes distributed in all cellular compartments. Critically, patterns of multiple enzymatic and nonenzymatic PTMs within a single enzyme are now functionally evaluated providing a holistic picture of a macromolecule interacting with low molecular mass compounds, some of them being substrates, enzyme regulators, or activated precursors for enzymatic and nonenzymatic PTMs.

Offline and online capillary electrophoresis enzyme assays of β-N-acetylhexosaminidase.

Enzyme assays of β-N-acetylhexosaminidase from Aspergillus oryzae using capillary electrophoresis in the offline and online setup have been developed. The pH value and concentration of the borate-based background electrolyte were optimized in order to achieve baseline separation of N,N',N″-triacetylchitotriose, N,N'-diacetylchitobiose, and N-acetyl-D-glucosamine. The optimized method using 25 mM tetraborate buffer, pH 10.

Native red electrophoresis--a new method suitable for separation of native proteins.

A new type of native electrophoresis was developed to separate and characterize proteins. In this modification of the native blue electrophoresis, the dye Ponceau Red S is used instead of Coomassie Brilliant Blue to impose uniform negative charge on proteins to enable their electrophoretic separation according to their relative molecular masses. As Ponceau Red S binds less tightly to proteins, in comparison with Coomassie Blue, it can be easily removed after the electrophoretic separation and a further investigation of protein properties is made possible (e.

Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase.

Fungal β-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group better and has some other unusual catalytic properties.

What can enzymes of C₄ photosynthesis do for C₃ plants under stress?

Phosphoenolpyruvate carboxylase (PEPC), NADP-malic enzyme (NADP-ME), and pyruvate, phosphate dikinase (PPDK) participate in the process of concentrating CO₂ in C₄ photosynthesis. Non-photosynthetic counterparts of these enzymes, which are present in all plants, play important roles in the maintenance of pH and replenishment of Krebs cycle intermediates, thereby contributing to the biosynthesis of amino acids and other compounds and providing NADPH for biosynthesis and the antioxidant system. Enhanced activities of PEPC and/or NADP-ME and/or PPDK were found in plants under various types of abiotic stress, such as drought, high salt concentration, ozone, the absence of phosphate and iron or the presence of heavy metals in the soil.

Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: properties of phosphorylated and dephosphorylated forms.

Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.

Effect of Potato virus Y on the NADP-malic enzyme from Nicotiana tabacum L.: mRNA, expressed protein and activity.

The effect of biotic stress induced by viral infection (Potato virus Y, strain NTN and O) on NADP-malic enzyme (EC 1.1.1.

Regulation of phosphoenolpyruvate carboxylase in PVY(NTN)-infected tobacco plants.

The effect of viral infection on the regulation of phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.