Correction to Kinetic Study of the Effect of pH on the Trypsin-Catalyzed Hydrolysis of -α-benzyloxycarbonyl-l-lysine--nitroanilide: Mechanism of Trypsin Catalysis.

[This corrects the article DOI: 10.1021/acsomega.9b03750.

Kinetic Studies of the Effect of pH on the Trypsin-Catalyzed Hydrolysis of -α-benzyloxycarbonyl-l-lysine--nitroanilide: Mechanism of Trypsin Catalysis.

The pH dependence of the trypsin-catalyzed hydrolysis of -α-benzyloxycarbonyl-l-lysine -nitroanilide has been studied at 25 °C. / was maximal at alkaline pH values but decreased with decreasing pH. / was dependent on free enzyme p values of 6.

A new lysine derived glyoxal inhibitor of trypsin, its properties and utilization for studying the stabilization of tetrahedral adducts by trypsin.

New trypsin inhibitors Z-Lys-COCHO and Z-Lys-H have been synthesised. values for Z-Lys-COCHO, Z-Lys-COOH, Z-Lys-H and Z-Arg-COOH have been determined. The glyoxal group (-COCHO) of Z-Lys-COCHO increases binding ~300 fold compared to Z-Lys-H.

Structural and biochemical properties of LuxF from Photobacterium leiognathi.

The lux-operon of bioluminescent bacteria contains the genes coding for the enzymes required for light emission. Some species of Photobacteria feature an additional gene, luxF, which shows similarity to luxA and luxB, the genes encoding the heterodimeric luciferase. Isolated dimeric LuxF binds four molecules of an unusually derivatized flavin, i.

Quantifying tetrahedral adduct formation and stabilization in the cysteine and the serine proteases.

Two new papain inhibitors have been synthesized where the terminal α-carboxyl groups of Z-Phe-Ala-COOH and Ac-Phe-Gly-COOH have been replaced by a proton to give Z-Phe-Ala-H and Ac-Phe-Gly-H. We show that for papain, replacing the terminal carboxylate group of a peptide inhibitor with a hydrogen atom decreases binding 3-4 fold while replacing an aldehyde or glyoxal group with a hydrogen atom decreases binding by 300,000-1,000,000 fold. Thiohemiacetal formation by papain with aldehyde or glyoxal inhibitors is shown to be ~10,000 times more effective than hemiacetal or hemiketal formation with chymotrypsin.