Table 1. Kinetic parameters of Trx-like protein-dependent oxidation in CF1-γ SpeciesConditionsΔμH+S1/2 (nM)Significance by condition (p < 0.05)|R|t1/2 (s)Significance by condition (p < 0.05)|R| TrxL2.1 Light, − FCCP Formed 7.1 ± 2.5 a 0.993 9.4 + 1.1 a 0.986 Light, + ...
In fact, the increase of positive charges on the surface of EcTRX (E30K/L94K) enhances the affinity for other substrates like chloroplast fructose-1,6-bisphosphatase, and also increases specific activity. Remarkably, these effects can be shielded by ionic strength; i.e., high concentrations ...
The protein disulfide reductase thioredoxin (Trx) maintains thiol groups in a reduced form through thiol-disulfide exchange reactions involving a redox-active WCXXC motif. Trx also provides reducing equivalents to enzymes like ribonucleotide reductase, peroxiredoxins and methionine sulfoxide reductase1. The...
Protein disulfide isomerases typically consist of two catalytic thioredoxin-like domains (a and a′) that each contain an active-site redox motif which are separated by two non-catalytic thioredoxin-like domains (b and b′). However, some protein disulfide isomerases, such as ERp18 (43) and...
S. pombe strains (Table S1) were grown under standard conditions. Analysis of Protein Oxidation 3.75–7.5 × 106 cells were grown to mid-log phase and harvested before or after exposure to hydrogen peroxide. Proteins were prepared using the trichloroacetic acid (TCA) method (Delaunay et al., ...
(Fig. 1andSupplemental Fig. S1). Trx-like domains are common to members of the protein disulfide isomerase (PDI) family, which are responsible for assisting protein folding in the ER29. Most PDI family members are multidomain proteins containing both redox-active and -inactive Trx-like domains...
lysates. We then used a combination of ELISA-based assay and purification strategies to show that deCoAlation is an enzyme-driven mechanism. Using mass-spectrometry and deCoAlation assays, we identifiedB. subtilisYtpP (thioredoxin-like protein) and thioredoxin A (TrxA) as enzymes that can remove...
Contact hot spots, together with their close energy neighbors, defined three major interacting (or contact) areas for protein ligands: a corner-like exposed area including the active site involved exclusively in covalent interactions, a neighboring extended area for covalent and strong non-covalent ...