EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.5.1 | expressed in Escherichia coli strain DW35 | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.5.1 | H71C | role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Mutant H71C results in a protein that retains penta-coordinated heme b indicating that Cys is not able to provide coordination for the heme in Escherichia coli SQR even in its optimal structural position. Km (ubiquinone): 0.012 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. Mutant H71C retains 43% of ubiquinone reductase activity compared to wild-type SQR, quinone reductase activity is impaired to a greater extent than its succinate-oxidase activity measured with phenazine ethosulfate | Escherichia coli |
1.3.5.1 | H71Y | mutant lacks heme. Km (ubiquinone): 0.01 mM compared to 0.0025 mM wild-type, lower ubiquinone or phenazine ethosulfate reductase activity compared to mutant H71C or double mutant H71Y/A72C | Escherichia coli |
1.3.5.1 | H71Y/A72C | role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Double mutant assembles within the membrane but without heme, and it retains the ability to reduce quinone. Km (ubiquinone): 0.013 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. The Y71C72 double mutant shows significant improvement in its activity compared to H71Y or H71C | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.3.5.1 | 0.0025 | - |
ubiquinone | wild-type SQR | Escherichia coli | |
1.3.5.1 | 0.01 | - |
ubiquinone | mutant H71Y | Escherichia coli | |
1.3.5.1 | 0.012 | - |
ubiquinone | mutant H71Y | Escherichia coli | |
1.3.5.1 | 0.013 | - |
ubiquinone | mutant H71Y/A72C | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.5.1 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.5.1 | succinate + phenazine ethosulfate | - |
Escherichia coli | fumarate + reduced phenazine ethosulfate | - |
? | |
1.3.5.1 | succinate + ubiquinone | - |
Escherichia coli | fumarate + ubiquinol | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.5.1 | SdhD | succinate dehydrogenase subunit that also coordinate the low spin hexa-coordinated heme b | Escherichia coli |
1.3.5.1 | SQR | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.3.5.1 | 30 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.3.5.1 | 8 | - |
assay at | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.5.1 | flavin adenine dinucleotide | - |
Escherichia coli |