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Literature summary extracted from

  • Gong, H.; Gao, Y.; Zhou, X.; Xiao, Y.; Wang, W.; Tang, Y.; Zhou, S.; Zhang, Y.; Ji, W.; Yu, L.; Tian, C.; Lam, S.; Shui, G.; Guddat, L.; Wong, L.; Wang, Q.; Rao, Z.
    Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF (2020), Nat. Commun., 11, 4245 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.1 gene MSMEG_1671, recombinant expression of C-terminally His10-tagged protein Sdh2D in Mycobacterium smegmatis mutant strain mc2 51 Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.1 0.0658
-
 succinate pH 7.4, 37°C, recombinant Sdh2 Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 succinate + a quinone Mycolicibacterium smegmatis
-
 fumarate + a quinol
-
 ?
1.3.5.1 succinate + a quinone Mycolicibacterium smegmatis ATCC 700084
-
 fumarate + a quinol
-
 ?
1.3.5.1 succinate + a quinone Mycolicibacterium smegmatis mc(2)155
-
 fumarate + a quinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Mycolicibacterium smegmatis A0QT08 AND A0QT07 AND A0QT10 AND A0QT09 SdhA, SdhB, SdhC, and SdhD proteins forming one subunit of the heterotrimeric enzyme
-
1.3.5.1 Mycolicibacterium smegmatis ATCC 700084 A0QT08 AND A0QT07 AND A0QT10 AND A0QT09 SdhA, SdhB, SdhC, and SdhD proteins forming one subunit of the heterotrimeric enzyme
-
1.3.5.1 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 (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1 recombinant His10-tagged protein Sdh2D from Mycobacterium smegmatis mutant strain mc2 51 by nickel affinity chromatography, digitonin treatment, and gel filtration Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 succinate + a quinone
-
 Mycolicibacterium smegmatis fumarate + a quinol
-
 ?
1.3.5.1 succinate + a quinone
-
 Mycolicibacterium smegmatis ATCC 700084 fumarate + a quinol
-
 ?
1.3.5.1 succinate + a quinone
-
 Mycolicibacterium smegmatis mc(2)155 fumarate + a quinol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 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

EC Number Synonyms Comment Organism
1.3.5.1 SDH
-
 Mycolicibacterium smegmatis
1.3.5.1 SDH2
-
 Mycolicibacterium smegmatis
1.3.5.1 SdhA catalytic FAD binding subunit Mycolicibacterium smegmatis
1.3.5.1 SdhD hydrophobic membrane anchor protein subunit Mycolicibacterium smegmatis
1.3.5.1 succinate dehydrogenase
-
 Mycolicibacterium smegmatis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.5.1 3.16
-
 succinate pH 7.4, 37°C, recombinant Sdh2 Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 FAD
-
 Mycolicibacterium smegmatis
1.3.5.1 Fe-S cluster three clusters Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
1.3.5.1 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
1.3.5.1 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