Literature summary extracted from
Funk, M.A.; Judd, E.T.; Marsh, E.N.; Elliott, S.J.; Drennan, C.L.
Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity (2014), Proc. Natl. Acad. Sci. USA, 111, 10161-10166 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.99.11 |
recombinant enzyme expression in Escherichia coli strain BL21(DE3) |
Thauera aromatica |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.1.99.11 |
Fe2+ |
one [4Fe4S]-cluster is located in the small subunit beta |
Thauera aromatica |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.1.99.11 |
toluene + fumarate |
Thauera aromatica |
- |
benzylsuccinate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.99.11 |
Thauera aromatica |
O87943 AND O87944 AND O87942 |
alpha-, beta-, and gamma-subunit |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.99.11 |
recombinant enzyme from Escherichia coli strain BL21(DE3) |
Thauera aromatica |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
4.1.99.11 |
benzylsuccinate = toluene + fumarate |
benzylsuccinate synthase (BSS) catalyzes the formation of a C-C bond between toluene and fumarate by a radical mechanism, overview. An enzyme-bound glycyl radical cofactor transiently forms a catalytically essential enzyme-bound thiyl (Cys) radical |
Thauera aromatica |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.1.99.11 |
toluene + fumarate |
- |
Thauera aromatica |
benzylsuccinate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.1.99.11 |
heterotrimer |
1 * 100000 + 1 * 8500 + 1 * 6500, the enzyme consists of three subunits encoded by three different genes and of very different sizes: the large subunit of circa 100 kDa contains the glycyl radical in the active site and carries out the catalysis |
Thauera aromatica |
4.1.99.11 |
More |
analysis of BSSalpha-BSSgamma subunit interactions and of BSSalpha-BSSbeta subunit interactions, detailed overview |
Thauera aromatica |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.99.11 |
BSS |
- |
Thauera aromatica |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.1.99.11 |
glycyl radical |
an enzyme-bound glycyl radical cofactor transiently forms a catalytically essential enzyme-bound thiyl (Cys) radical |
Thauera aromatica |
|
4.1.99.11 |
additional information |
the BSS small subunits resemble high potential iron-sulfur proteins |
Thauera aromatica |
|
4.1.99.11 |
[4Fe-4S] cluster |
a [4Fe4S]-cluster is located in the small subunit beta, while there is no bound [4Fe-4S] cluster observable in the electron density of subunit BSSgamma |
Thauera aromatica |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
4.1.99.11 |
evolution |
enzyme BSS is a member of the glycyl radical enzyme (GRE) family |
Thauera aromatica |
4.1.99.11 |
additional information |
subunit BSSalpha adopts a conserved Gly radical enzyme fold. The beta subunit BSSbeta adopts a fold similar to that of a high potential iron-sulfur protein HiPIP. Subunit gamma, BSSgamma, is only 19% identical to BSSbeta, but they share the basic HiPIP fold along with the extended beta-sheet and hairpin loop. Analysis of BSSalpha-BSSgamma subunit interactions and of BSSalpha-BSSbeta subunit interactions, global structural changes in the BSSalpha-BSSgamma complex, influence of BSSbeta on the structure and flexibility of BSSalpha, overview |
Thauera aromatica |
4.1.99.11 |
physiological function |
benzylsuccinate synthase (BSS) catalyzes the first step in anaerobic toluene degradation, the generation of (R)-benzylsuccinate from toluene and fumarate. This unusual reaction is thought to proceed through radical mediated C-C bond formation, with the radical source being an enzyme-bound glycyl radical cofactor that transiently forms a catalytically essential enzyme-bound thiyl (Cys) radical |
Thauera aromatica |