Cloned (Comment) | Organism |
---|---|
gene MSMEG_1671, recombinant expression of C-terminally His10-tagged protein Sdh2D in Mycobacterium smegmatis mutant strain mc2 51 | Mycolicibacterium smegmatis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0658 | - |
succinate | pH 7.4, 37°C, recombinant Sdh2 | Mycolicibacterium smegmatis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate + a quinone | Mycolicibacterium smegmatis | - |
fumarate + a quinol | - |
? | |
succinate + a quinone | Mycolicibacterium smegmatis ATCC 700084 | - |
fumarate + a quinol | - |
? | |
succinate + a quinone | Mycolicibacterium smegmatis mc(2)155 | - |
fumarate + a quinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | A0QT08 AND A0QT07 AND A0QT10 AND A0QT09 | SdhA, SdhB, SdhC, and SdhD proteins forming one subunit of the heterotrimeric enzyme | - |
Mycolicibacterium smegmatis ATCC 700084 | A0QT08 AND A0QT07 AND A0QT10 AND A0QT09 | SdhA, SdhB, SdhC, and SdhD proteins forming one subunit of the heterotrimeric enzyme | - |
Mycolicibacterium smegmatis mc(2)155 | A0QT08 AND A0QT07 AND A0QT10 AND A0QT09 | SdhA, SdhB, SdhC, and SdhD proteins forming one subunit of the heterotrimeric enzyme | - |
Purification (Comment) | Organism |
---|---|
recombinant His10-tagged protein Sdh2D from Mycobacterium smegmatis mutant strain mc2 51 by nickel affinity chromatography, digitonin treatment, and gel filtration | Mycolicibacterium smegmatis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate + a quinone | - |
Mycolicibacterium smegmatis | fumarate + a quinol | - |
? | |
succinate + a quinone | - |
Mycolicibacterium smegmatis ATCC 700084 | fumarate + a quinol | - |
? | |
succinate + a quinone | - |
Mycolicibacterium smegmatis mc(2)155 | fumarate + a quinol | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotrimer | determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices | Mycolicibacterium smegmatis |
Synonyms | Comment | Organism |
---|---|---|
SDH | - |
Mycolicibacterium smegmatis |
SDH2 | - |
Mycolicibacterium smegmatis |
SdhA | catalytic FAD binding subunit | Mycolicibacterium smegmatis |
SdhD | hydrophobic membrane anchor protein subunit | Mycolicibacterium smegmatis |
succinate dehydrogenase | - |
Mycolicibacterium smegmatis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.16 | - |
succinate | pH 7.4, 37°C, recombinant Sdh2 | Mycolicibacterium smegmatis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Mycolicibacterium smegmatis | |
Fe-S cluster | three clusters | Mycolicibacterium smegmatis |
General Information | Comment | Organism |
---|---|---|
additional information | the membrane-anchored SdhF is a subunit of the enzyme complex II (Sdh2). The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Location and interaction of SdhF subunit in Sdh2 protein. Two distal quinone-binding sites with bound quinones are identified, one distal binding site is formed by neighboring subunits of the complex. Major redox centers in the complex are FAD, three iron-sulfur clusters, and a transiently bound semiquinone. The purified recombinant Sdh2 is a functioning complex that couples succinate oxidation to menadione reduction. Enzyme structure analysis, overview | Mycolicibacterium smegmatis |
physiological function | succinate dehydrogenase (SDH) is a protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, overview | Mycolicibacterium smegmatis |