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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
Q9Z4P0, FRD2_SHEFNP00363, FRDA_ECOLIP44894, FRDA_HAEIN
Q9ZMP0, FRDA_HELPJO06913, FRDA_HELPYP64175, FRDA_MYCBO
P9WN90, FRDA_MYCTOP9WN91, FRDA_MYCTUP20922, FRDA_PROVU
V3TQ67, FRDA_SERS3Q07WU7, FRDA_SHEFNP0C278, FRDA_SHEFR
P83223, FRDA_SHEONP17412, FRDA_WOLSUP0AC49, FRDB_ECO57
P0AC48, FRDB_ECOL6P0AC47, FRDB_ECOLIP44893, FRDB_HAEIN
Q9ZMP1, FRDB_HELPJO06914, FRDB_HELPYP9WN88, FRDB_MYCTO
P9WN89, FRDB_MYCTUP20921, FRDB_PROVUP0AC50, FRDB_SHIFL
P17596, FRDB_WOLSUO82663, SDHA1_ARATHQ33862, SDHA1_ASCSU
Q9ZPX5, SDHA2_ARATHQ8WSR3, SDHA2_ASCSUQ6PA58, SDHAA_XENLA
Q801S2, SDHAB_XENLAP08065, SDHA_BACSUP31039, SDHA_BOVIN
Q09508, SDHA_CAEELQ9YHT1, SDHA_CHICKP51054, SDHA_COXBU
Q7ZVF3, SDHA_DANREQ9U3X4, SDHA_DICDIQ94523, SDHA_DROME
P0AC43, SDHA_ECO57P0AC42, SDHA_ECOL6P0AC41, SDHA_ECOLI
P31040, SDHA_HUMANQ8HXW3, SDHA_MACFAQ0QF17, SDHA_MESAU
Q8K2B3, SDHA_MOUSEQ6ZDY8, SDHA_ORYSJQ59661, SDHA_PARDE
Q0QF01, SDHA_PIGQ5R616, SDHA_PONABQ920L2, SDHA_RAT
Q1RHB9, SDHA_RICBRQ92J97, SDHA_RICCNQ4UJM1, SDHA_RICFE
P31038, SDHA_RICPRQ68XN9, SDHA_RICTYQ8ZQU3, SDHA_SALTY
Q9UTJ7, SDHA_SCHPOG4V4G6, SDHA_SERS3Q28ED0, SDHA_XENTR
Q00711, SDHA_YEASTQ8LBZ7, SDHB1_ARATHQ9S827, SDHB1_ORYSJ
Q8LB02, SDHB2_ARATHQ6H4G3, SDHB2_ORYSJQ9FJP9, SDHB3_ARATH
O44074, SDHB_ASCSUP08066, SDHB_BACSUQ3T189, SDHB_BOVIN
A8WPF0, SDHB_CAEBRQ09545, SDHB_CAEELQ6FWS8, SDHB_CANGA
Q9YHT2, SDHB_CHICKP48932, SDHB_CHOCRP51053, SDHB_COXBU
P48933, SDHB_CYACAA5PL98, SDHB_DANREQ55CC2, SDHB_DICDI
P21914, SDHB_DROMEP07014, SDHB_ECOLIQ75CI4, SDHB_EREGS
P21912, SDHB_HUMANQ9CQA3, SDHB_MOUSEQ59662, SDHB_PARDE
Q007T0, SDHB_PIGP80477, SDHB_PORPUP21913, SDHB_RAT
P80480, SDHB_RECAMQ1RGP3, SDHB_RICBRQ92JJ8, SDHB_RICCN
Q4UN71, SDHB_RICFEQ9ZEA1, SDHB_RICPRQ68XS0, SDHB_RICTY
Q8ZQU2, SDHB_SALTYP21911, SDHB_SCHPOQ70KF8, SDHB_UROFA
P32420, SDHB_USTMAQ3B8J8, SDHB_XENLAB0BM36, SDHB_XENTR
P21801, SDHB_YEASTO42772, SDHB_ZYMTRP47052, SDHX_YEAST

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