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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
BRENDA1.3.5.1
EC2PDB1.3.5.1
ExplorEnz1.3.5.1
PRIAM enzyme-specific profiles1.3.5.1
KEGG Ligand Database for Enzyme Nomenclature1.3.5.1
IUBMB Enzyme Nomenclature1.3.5.1
IntEnz1.3.5.1
MEDLINEFind literature relating to 1.3.5.1
MetaCyc1.3.5.1
Rhea expert-curated reactions1.3.5.1
UniProtKB/Swiss-Prot
P00363, FRDA_ECOLIP44894, FRDA_HAEINQ9ZMP0, FRDA_HELPJ
O06913, FRDA_HELPYP64175, FRDA_MYCBOP9WN90, FRDA_MYCTO
P9WN91, FRDA_MYCTUP20922, FRDA_PROVUV3TQ67, FRDA_SERS3
P17412, FRDA_WOLSUP0AC49, FRDB_ECO57P0AC48, FRDB_ECOL6
P0AC47, FRDB_ECOLIP44893, FRDB_HAEINQ9ZMP1, FRDB_HELPJ
O06914, FRDB_HELPYP9WN88, FRDB_MYCTOP9WN89, FRDB_MYCTU
P20921, FRDB_PROVUP0AC50, FRDB_SHIFLP17596, FRDB_WOLSU
O82663, SDHA1_ARATHQ33862, SDHA1_ASCSUQ9ZPX5, SDHA2_ARATH
Q8WSR3, SDHA2_ASCSUQ6PA58, SDHAA_XENLAQ801S2, SDHAB_XENLA
P08065, SDHA_BACSUP31039, SDHA_BOVINQ09508, SDHA_CAEEL
Q9YHT1, SDHA_CHICKP51054, SDHA_COXBUQ7ZVF3, SDHA_DANRE
Q9U3X4, SDHA_DICDIQ94523, SDHA_DROMEP0AC43, SDHA_ECO57
P0AC42, SDHA_ECOL6P0AC41, SDHA_ECOLIP31040, SDHA_HUMAN
Q8HXW3, SDHA_MACFAQ0QF17, SDHA_MESAUQ8K2B3, SDHA_MOUSE
Q6ZDY8, SDHA_ORYSJQ59661, SDHA_PARDEQ0QF01, SDHA_PIG
Q5R616, SDHA_PONABQ920L2, SDHA_RATQ1RHB9, SDHA_RICBR
Q92J97, SDHA_RICCNQ4UJM1, SDHA_RICFEP31038, SDHA_RICPR
Q68XN9, SDHA_RICTYQ8ZQU3, SDHA_SALTYQ9UTJ7, SDHA_SCHPO
G4V4G6, SDHA_SERS3Q28ED0, SDHA_XENTRQ00711, SDHA_YEAST
Q8LBZ7, SDHB1_ARATHQ9S827, SDHB1_ORYSJQ8LB02, SDHB2_ARATH
Q6H4G3, SDHB2_ORYSJQ9FJP9, SDHB3_ARATHO44074, SDHB_ASCSU
P08066, SDHB_BACSUQ3T189, SDHB_BOVINA8WPF0, SDHB_CAEBR
Q09545, SDHB_CAEELQ6FWS8, SDHB_CANGAQ9YHT2, SDHB_CHICK
P48932, SDHB_CHOCRP51053, SDHB_COXBUP48933, SDHB_CYACA
A5PL98, SDHB_DANREQ55CC2, SDHB_DICDIP21914, SDHB_DROME
P07014, SDHB_ECOLIQ75CI4, SDHB_EREGSP21912, SDHB_HUMAN
Q9CQA3, SDHB_MOUSEQ59662, SDHB_PARDEQ007T0, SDHB_PIG
P80477, SDHB_PORPUP21913, SDHB_RATP80480, SDHB_RECAM
Q1RGP3, SDHB_RICBRQ92JJ8, SDHB_RICCNQ4UN71, SDHB_RICFE
Q9ZEA1, SDHB_RICPRQ68XS0, SDHB_RICTYQ8ZQU2, SDHB_SALTY
P21911, SDHB_SCHPOQ70KF8, SDHB_UROFAP32420, SDHB_USTMA
Q3B8J8, SDHB_XENLAB0BM36, SDHB_XENTRP21801, SDHB_YEAST
O42772, SDHB_ZYMTRP47052, SDHX_YEAST

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