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ENZYME

ENZYME entry: EC 1.3.5.1

Accepted Name
succinate dehydrogenase
Alternative Name(s)
fumarate reductase (menaquinone)
succinate dehydrogenase (menaquinone)
succinate dehydrogenase (quinone)
succinate dehydrogenase (ubiquinone)
succinic dehydrogenase
Reaction catalysed
a quinone + succinate <=> a quinol + fumarate
Comment(s)
  • A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively.
  • Under aerobic conditions the enzyme catalyzes succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II).
  • Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor.
  • The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit.
  • These enzymes catalyze an electrogenic reaction and are thus classified as EC 7.1.1.12.
  • Formerly EC 1.3.5.4.
Cross-references
BRENDA 1.3.5.1
EC2PDB 1.3.5.1
ExplorEnz 1.3.5.1
PRIAM enzyme-specific profiles 1.3.5.1
KEGG Ligand Database for Enzyme Nomenclature 1.3.5.1
IUBMB Enzyme Nomenclature 1.3.5.1
IntEnz 1.3.5.1
MEDLINE Find literature relating to 1.3.5.1
MetaCyc 1.3.5.1
Rhea expert-curated reactions 1.3.5.1
UniProtKB/Swiss-Prot
Q9Z4P0, FRD2_SHEFN P00363, FRDA_ECOLI P44894, FRDA_HAEIN
Q9ZMP0, FRDA_HELPJ O06913, FRDA_HELPY P64175, FRDA_MYCBO
P9WN90, FRDA_MYCTO P9WN91, FRDA_MYCTU P20922, FRDA_PROVU
V3TQ67, FRDA_SERS3 Q07WU7, FRDA_SHEFN P0C278, FRDA_SHEFR
P83223, FRDA_SHEON P17412, FRDA_WOLSU P0AC49, FRDB_ECO57
P0AC48, FRDB_ECOL6 P0AC47, FRDB_ECOLI P44893, FRDB_HAEIN
Q9ZMP1, FRDB_HELPJ O06914, FRDB_HELPY P9WN88, FRDB_MYCTO
P9WN89, FRDB_MYCTU P20921, FRDB_PROVU P0AC50, FRDB_SHIFL
P17596, FRDB_WOLSU O82663, SDHA1_ARATH Q33862, SDHA1_ASCSU
Q9ZPX5, SDHA2_ARATH Q8WSR3, SDHA2_ASCSU Q6PA58, SDHAA_XENLA
Q801S2, SDHAB_XENLA P08065, SDHA_BACSU P31039, SDHA_BOVIN
Q09508, SDHA_CAEEL Q9YHT1, SDHA_CHICK P51054, SDHA_COXBU
Q7ZVF3, SDHA_DANRE Q9U3X4, SDHA_DICDI Q94523, SDHA_DROME
P0AC43, SDHA_ECO57 P0AC42, SDHA_ECOL6 P0AC41, SDHA_ECOLI
P31040, SDHA_HUMAN Q8HXW3, SDHA_MACFA Q0QF17, SDHA_MESAU
Q8K2B3, SDHA_MOUSE Q6ZDY8, SDHA_ORYSJ Q59661, SDHA_PARDE
Q0QF01, SDHA_PIG Q5R616, SDHA_PONAB Q920L2, SDHA_RAT
Q1RHB9, SDHA_RICBR Q92J97, SDHA_RICCN Q4UJM1, SDHA_RICFE
P31038, SDHA_RICPR Q68XN9, SDHA_RICTY Q8ZQU3, SDHA_SALTY
Q9UTJ7, SDHA_SCHPO G4V4G6, SDHA_SERS3 Q28ED0, SDHA_XENTR
Q00711, SDHA_YEAST Q8LBZ7, SDHB1_ARATH Q9S827, SDHB1_ORYSJ
Q8LB02, SDHB2_ARATH Q6H4G3, SDHB2_ORYSJ Q9FJP9, SDHB3_ARATH
O44074, SDHB_ASCSU P08066, SDHB_BACSU Q3T189, SDHB_BOVIN
A8WPF0, SDHB_CAEBR Q09545, SDHB_CAEEL Q6FWS8, SDHB_CANGA
Q9YHT2, SDHB_CHICK P48932, SDHB_CHOCR P51053, SDHB_COXBU
P48933, SDHB_CYACA A5PL98, SDHB_DANRE Q55CC2, SDHB_DICDI
P21914, SDHB_DROME P07014, SDHB_ECOLI Q75CI4, SDHB_EREGS
P21912, SDHB_HUMAN Q9CQA3, SDHB_MOUSE Q59662, SDHB_PARDE
Q007T0, SDHB_PIG P80477, SDHB_PORPU P21913, SDHB_RAT
P80480, SDHB_RECAM Q1RGP3, SDHB_RICBR Q92JJ8, SDHB_RICCN
Q4UN71, SDHB_RICFE Q9ZEA1, SDHB_RICPR Q68XS0, SDHB_RICTY
Q8ZQU2, SDHB_SALTY P21911, SDHB_SCHPO Q70KF8, SDHB_UROFA
P32420, SDHB_USTMA Q3B8J8, SDHB_XENLA B0BM36, SDHB_XENTR
P21801, SDHB_YEAST O42772, SDHB_ZYMTR P47052, SDHX_YEAST

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