EC Number   |
General Information |
Reference |
|---|
   1.8.4.2 | metabolism |
the actinobacterium Corynebacterium matruchotii has been implicated in nucleation of oral microbial consortia leading to biofilm formation |
-, 765004 |
| 1.8.4.2 | metabolism |
the enzyme affects multiple phenotypes in Streptococcus gordonii and is required for production of disulfide-bonded proteins like Anti-CR1 scFv |
725524 |
| 1.8.4.2 | more |
the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices. The conserved catalytic CHYC motif (residues 91 to 94) forms the active site together with a conserved cis-Pro loop (residues S221 and P222). Structure modeling and structure comparisons, overview |
-, 765004 |
| 1.8.4.2 | more |
the solution structure of COA6 reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. COA6 structure analysis by NMR spectroscopy, overview |
-, 764441 |
| 1.8.4.2 | more |
the solution structure of COA6 reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. COA6 structure analysis by NMR spectroscopy, overview. The conserved tryptophans W59 and W66 are critical for COA6 stability and possibly for their interactions with client proteins |
764441 |
| 1.8.4.2 | more |
VKOR-mediated reactivation of MdbA appears to be conserved in the Actinobacteria. Formation of the MdbA-VKOR mixed disulfide complex requires C93. The signal of this MdbA-VKOR complex is greatly diminished when the sample is treated with 2-mercaptoethanol. The complex is not found when both C93 and C101 are mutated to alanine. The results suggest that when C101 is mutated, VKOR forms a complex with MdbA via the VKOR C93 residue |
745224 |
| 1.8.4.2 | physiological function |
a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant |
-, 742200 |
| 1.8.4.2 | physiological function |
CGFS-type GRX is not reduced by GSH and has an atypically low redox potential (-323 mV at pH 7.9). GRX3 can be reduced in the light by photoreduced ferredoxin and ferredoxin-thioredoxin reductase |
763241 |
| 1.8.4.2 | physiological function |
gene deletion results in a severe growth defect at 37°C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30°C. At 37°C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production |
-, 743311 |
| 1.8.4.2 | physiological function |
in eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6. COA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidase. COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO, overview. COA6 acts as a disulfide reductase of SCO and COX2 proteins |
-, 764441 |
