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- DsbA abstract "DsbA is a bacterial disulfide oxidoreductase. DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA forms intrachain disulfide bonds as peptides emerge into the cell's periplasm.Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. Like other thioredoxin-based enzymes, DsbA's catalytic site is a CXXC motif (CPHC in E. coli DsbA). The pair of cysteines may be oxidized (forming an internal disulfide) or reduced (as free thiols), and thus allows for oxidoreductase activity by serving as an electron pair donor or acceptor, depending on oxidation state. This reaction generally proceeds through a mixed-disulfide intermediate, in which a cysteine from the enzyme forms a bond to a cysteine on the substrate. DsbA is responsible for introducing disulfide bonds into nascent proteins. In equivalent terms, it catalyzes the oxidation of a pair of cysteine residues on the substrate protein. Most of the substrates for DsbA are eventually secreted, and include important toxins, virulence factors, adhesion machinery, and motility structures DsbA is localized in the periplasm, and is more common in Gram-negative bacteria than in Gram-positive bacteria. Within the thioredoxin family, DsbA is the most strongly oxidizing. Using glutathione oxidation as a metric, DsbA is ten times more oxidizing than protein disulfide-isomerase (the eukaryotic equivalent of DsbA). The extremely oxidizing nature of DsbA is due to an increase in stability upon reduction of DsbA, thereby imparting a decrease in energy of the enzyme when it oxidizes substrate. This feature is incredibly rare among proteins, as nearly all proteins are stabilized by the formation of disulfide bonds. DsbA's highly oxidizing nature is a result of hydrogen bond, electrostatic and helix-dipole interactions that favour the thiolate over the disulfide at the active site.After donating its disulfide bond, DsbA is regenerated by the membrane-bound protein DsbB.".
- DsbA entrezgene "948353".
- DsbA pdb "1A2M".
- DsbA symbol "DSBA".
- DsbA symbol "DsbA".
- DsbA thumbnail Ecoli_DsbA_1A2M.png?width=300.
- DsbA uniprot "P0AEG4".
- DsbA wikiPageID "29200295".
- DsbA wikiPageRevisionID "591069758".
- DsbA caption "Crystal structure of E. coli DsbA.".
- DsbA entrezgene "948353".
- DsbA hasPhotoCollection DsbA.
- DsbA interpro "IPR001853".
- DsbA name "DSBA oxidoreductase".
- DsbA name "DsbA".
- DsbA pdb "1".
- DsbA pfam "PF01323".
- DsbA symbol "DSBA".
- DsbA symbol "DsbA".
- DsbA uniprot "P0AEG4".
- DsbA subject Category:Enzymes.
- DsbA type Abstraction100002137.
- DsbA type Chemical114806838.
- DsbA type Compound114818238.
- DsbA type Macromolecule114944888.
- DsbA type Material114580897.
- DsbA type Matter100020827.
- DsbA type Molecule114682133.
- DsbA type OrganicCompound114727670.
- DsbA type Part113809207.
- DsbA type PhysicalEntity100001930.
- DsbA type Protein114728724.
- DsbA type Relation100031921.
- DsbA type Substance100019613.
- DsbA type Thing100002452.
- DsbA type Unit109465459.
- DsbA type Biomolecule.
- DsbA type Protein.
- DsbA type BiologicalObject.
- DsbA comment "DsbA is a bacterial disulfide oxidoreductase. DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA forms intrachain disulfide bonds as peptides emerge into the cell's periplasm.Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. Like other thioredoxin-based enzymes, DsbA's catalytic site is a CXXC motif (CPHC in E. coli DsbA).".
- DsbA label "DsbA".
- DsbA sameAs m.0dln3y2.
- DsbA sameAs Q5309954.
- DsbA sameAs Q5309954.
- DsbA sameAs DsbA.
- DsbA wasDerivedFrom DsbA?oldid=591069758.
- DsbA depiction Ecoli_DsbA_1A2M.png.
- DsbA isPrimaryTopicOf DsbA.
- DsbA name "DsbA".