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Literature summary for 1.3.5.1 extracted from

  • Janssen, S.; Schafer, G.; Anemuller, S.; Moll, R.
    A succinate dehydrogenase with novel structure and properties from the hyperthermophilic archaeon Sulfolobus acidocaldarius: genetic and biophysical characterization (1997), J. Bacteriol., 179, 5560-5569.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14080
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases Sulfolobus acidocaldarius
32205
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases Sulfolobus acidocaldarius
36471
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases Sulfolobus acidocaldarius
63075
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius P77943 and P77944 and P77945 and P77946 P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, P77946: subunit sdhD
-
Sulfolobus acidocaldarius DSM 639 P77943 and P77944 and P77945 and P77946 P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, P77946: subunit sdhD
-

Subunits

Subunits Comment Organism
? x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases Sulfolobus acidocaldarius

Synonyms

Synonyms Comment Organism
succinate dehydrogenase ambiguous Sulfolobus acidocaldarius

General Information

General Information Comment Organism
physiological function the enzyme is involved in electron transfer via the respiratory chain Sulfolobus acidocaldarius