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Results 1 - 10 of 33 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2evolution DsbA is a periplasmic thiol-disulfide oxidoreductase that belongs to the thioredoxin family of proteins with a CxxC conserved domain -, 764747
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2evolution homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA -, 765006
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2evolution the oxidoreductase MdbA identified from Corynebacterium matruchotii is highly homologous to the Corynebacterium diphtheriae thiol-disulfide oxidoreductase MdbA (MdbACd). The disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbACm is a major thiol-disulfide oxidoreductase, which likely mediates posttranslocational protein folding in Corynebacterium matruchotii by a mechanism that is conserved in Actinobacteria, the enzyme is essential in the organism. Corynebacterium matruchotii MdbA can replace Corynebacterium diphtheriae MdbA in mutants to maintain normal cell growth and morphology, toxin production, and pilus assembly. The protein active site closely resembles active sites of other MdbA/DsbA enzymes. The superposition of Corynebacterium matruchotii and Corynebacterium diphtheriae MdbA active sites does not show notable changes of active-site arrangement, overview -, 765004
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2malfunction gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo -, 765006
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2malfunction SpeA in the culture supernatant remains reduced when gene sdbA is inactivated and restored to the oxidized state when a functional copy of sdbA is returned to the sdbA-knockout mutant. Complementation of sdbA deletion restores SpeA to an oxidized state. The enzyme mutant SdbAC49A forms a mixed disulfide with substrate mutant SpeAC87A. No reactions between SdbAC49A and SpeAC98A, SdbAC46A and SpeAC87A, or SdbAC46A and SpeAC98A 765010
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2malfunction the purple non-sulfur bacterium Rhodobacter capsulatus mutants lacking DsbA show severe temperature-sensitive and medium-dependent respiratory growth defects. Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase (cbb3-Cox) biogenesis in Rhodobacter capsulatus. Absence of DsbA, besides impairing the maturation of the c-type cytochrome subunits, also affects the incorporation of Cu into the catalytic subunit of cbb3-Cox. Defective high affinity Cu acquisition pathway, which includes the MFS-type Cu importer CcoA, and lower production of the c-type cytochrome subunits lead together to improper assembly and degradation of cbb3-Cox. DsbA- and several cbb3-Cox biogenesis mutants exhibit similar phenotypes. Mutational analysis of enzyme function, overview -, 764747
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2malfunction the truncation mutation (E87X) clearly disrupts the CHCH domain by removing a large portion of the protein from helix 2 onward. The other two mutations, W59C and W66R, are found within the first helix of COA6, where the side chains of each tryptophan face the bulk solvent, suggesting that these residues may facilitate interactions with their client proteins. Overexpression of the wild-type and mutant alleles of COA6 in control and COA6 patient fibroblasts shows that the W66R variant fails to rescue CcO activity. In contrast, expression of the W59C mutant leads to a partial recovery of CcO activity and COX2 levels. It seems that in most cell types residual levels of the partially functional W59C allele are not sufficient to support CcO assembly and mitochondrial respiration because coa6DELTA cells expressing the W59C variant do not exhibit respiratory growth. The human patient with the W59C mutation exhibits a severe CcO deficiency in cardiac tissue 764441
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2metabolism enzyme reacts with glutathionylated substrates in a GSH-dependent ping pong mechanism. The pKa of GrxS12 catalytic Cys29 is very low (3.9) and makes GrxS12 itself sensitive to oxidation by H2O2 and to direct glutathionylation by nitrosoglutathione. Glutathionylated-GrxS12 is temporarily inactive until it is deglutathionylated by GSH 762613
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2metabolism identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii -, 765006
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2metabolism posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by membrane-bound thiol-disulfide oxidoreductase, MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon. Reoxidation of MdbA involves a bacterial vitamin K epoxide reductase (VKOR)-like protein that contains four cysteine residues, C93/C101 and C175/C178, with the latter forming a canonical CXXC thioredoxin-like motif. Topological view of the Actinomyces oris membrane-spanning protein VKOR with these four exoplasmic cysteine residues that participate in MdbA reoxidation. Like deletion of the VKOR gene, alanine replacement of individual cysteine residues abrogates polymicrobial interactions and biofilm formation, concomitant with the failure to form adhesive pili on the bacterial surface. Mutational analysis of VKOR function, overview. The C93 residue of VKOR is postulated to form a mixed disulfide bond with MdbA 745224
Results 1 - 10 of 33 > >>