Toward Modular and Flexible Open RAN Implementations in 6G Networks: Traffic Steering Use Case and O-RAN xApps.

The development of cellular wireless systems has entered the phase when 5G networks are being deployed and the foundations of 6G solutions are being identified. However, in parallel to this, another technological breakthrough is observed, as the concept of open radio access networks is coming into play. Together with advancing network virtualization and programmability, this may reshape the way the functionalities and services related to radio access are designed, leading to modular and flexible implementations.

Catalysis of dehydrogenation of 4-trans-(N,N-dimethylamino)cinnamaldehyde by aldehyde dehydrogenase.

4-trans-(N,N-dimethylamino)cinnamaldehyde (DACA) is a chromophoric and fluorogenic substrate of aldehyde dehydrogenase. Fluorescence of DACA is enhanced by binding to aldehyde dehydrogenase in the absence of catalysis both in the presence and absence of the coenzyme analogue 5'AMP. DACA binds to aldehyde dehydrogenase with a dissociation constant of 1-3 microM and stoichiometry of 2 mol mol(-1) enzyme.

Binding and incorporation of 4-trans-(N,N-dimethylamino) cinnamaldehyde by aldehyde dehydrogenase.

4-trans-(N,N-Dimethylamino)cinnamaldehyde (DACA) is a chromophoric substrate of aldehyde dehydrogenase (EC 1.2.1.

Mechanism of inhibition of aldehyde dehydrogenase by citral, a retinoid antagonist.

Low concentrations of citral (3,7-dimethyl-2,6-octadienal), an inhibitor of retinoic acid biosynthesis, inhibited E1, E2 and E3 isozymes of human aldehyde dehydrogenase (EC1.2.1.

N-tosyl-L-phenylalanine chloromethyl ketone, a serine protease inhibitor, identifies glutamate 398 at the coenzyme-binding site of human aldehyde dehydrogenase. Evidence for a second "naked anion" at the active site.

Human aldehyde dehydrogenase isozymes were inactivated by N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), an inhibitor of chymotrypsin. The inactivation was a first-order process that followed saturation kinetics. NAD and chloral when used together protected against inactivation.

Haloenol lactones as inactivators and substrates of aldehyde dehydrogenase.

Human aldehyde dehydrogenase (EC 1.2.1.

Aspartic proteinase from Penicillium camemberti: purification, properties, and substrate specificity.

An acid proteinase from the culture filtrate of Penicillium camemberti was isolated in a two-step purification procedure by cation exchange chromatography and gel filtration. The enzyme is an aspartic proteinase inhibited by pepstatin, DAN, and EPNP, with a molecular mass determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 33.5 kDa.

Inactivation of the Enterobacter cloacae P99 beta-lactamase by a fluorescent phosphonate: direct detection of ligand binding at the second site.

The synthesis of a fluorescent beta-lactamase inhibitor, p-nitrophenyl [(dansylamido)methyl]-phosphonate is described. The compound inactivated the class C beta-lactamase of Enterobacter cloacae P99 with stoichiometric release of p-nitrophenol, presumably, as with other phosphonate inhibitors, by phosphonylation of the active site serine. The inhibited enzyme exhibited typical dansyl fluorescence emission at 533 nm with excitation maxima at 345 and 283 nm; the latter excitation peak probably arises from radiationless energy transfer to the dansyl group from aromatic chromophores on the protein-inspection of the crystal structure shows that the closest are tyrosines.

Steady-state kinetics of the binding of beta-lactams and penicilloates to the second binding site of the Enterobacter cloacae P99 beta-lactamase.

Previous research has shown that the class C beta-lactamase of Enterobacter cloacae P99 is able to catalyze the hydrolysis and aminolysis of acyclic depsipeptides. The steady kinetics of these reactions are complicated by the presence of an additional (depsi)peptide binding site in addition to the active site [Pazhanisamy, S., & Pratt, R.

Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 2. Limited proteolysis of Curcurbita maxima trypsin inhibitor I by pepsin.

Porcine pepsin hydrolyzes the Leu7-Met8 (P2'-P3') peptide bond in Cucurbita maxima trypsin inhibitor I (CMTI I) in the pH range 2.0-4.8.

Metallo-proteinase from the seedlings of kale (Brassica oleracea L. var. sabellica): : Preparation, partial characterization and substrate specificity.

Metallo-proteinase from 8-d-old seedlings of kale was isolated. The enzyme was extracted with 1% NaCl, concentrated by ammonium sulfate and finally purified by high-performance liquid chromatography. The isolated enzyme had a molecular weight of 22.

Serine proteinase from Cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I).

A proteinase was purified from resting seeds of Cucurbita ficifolia by ammonium sulfate fractionation and successive chromatography on CM-cellulose, Sephacryl S-300 and TSK DEAE-2SW (HPLC) columns. Inhibition by DFP and PMSF suggests that the enzyme is a serine proteinase. The apparent molecular mass of this enzyme is ca.

Serine proteinase from Cucurbita ficifolia seeds.

A new serine proteinase was isolated from Cucurbita ficifolia seeds by the purification procedure, which includes: extraction, salting out with ammonium sulphate, chromatography on CM-cellulose. Sephacryl S-300 gel filtration and h.p.