4.1.99.11: benzylsuccinate synthase
This is an abbreviated version!
For detailed information about benzylsuccinate synthase, go to the full flat file.
Word Map on EC 4.1.99.11
-
4.1.99.11
-
denitrifying
-
glycyl
-
thauera
-
aromatica
-
toluene-degrading
-
sulfate-reducing
-
aquifer
-
benzoyl-coa
-
azoarcus
-
ethylbenzene
-
geobacter
-
r-benzylsuccinate
-
hydrocarbon-degrading
-
plume
-
m-xylene
-
formate-lyase
-
environmental protection
-
iron-reducing
-
2-methylnaphthalene
-
hydrocarbon-contaminated
-
feiii-reducing
-
toluene-induced
-
desulfobulbaceae
-
nitrate-reducing
-
alkylbenzenes
-
toluene-grown
-
compound-specific
-
magnetospirillum
-
alkylsuccinate
- 4.1.99.11
-
denitrifying
-
glycyl
- thauera
- aromatica
-
toluene-degrading
-
sulfate-reducing
-
aquifer
- benzoyl-coa
- azoarcus
- ethylbenzene
- geobacter
-
r-benzylsuccinate
-
hydrocarbon-degrading
-
plume
- m-xylene
- formate-lyase
- environmental protection
-
iron-reducing
- 2-methylnaphthalene
-
hydrocarbon-contaminated
-
feiii-reducing
-
toluene-induced
- desulfobulbaceae
-
nitrate-reducing
-
alkylbenzenes
-
toluene-grown
-
compound-specific
- magnetospirillum
-
alkylsuccinate
Reaction
Synonyms
(R)-benzylsuccinate synthase, benzylsuccinate synthase, benzylsuccinate synthase A, BSS, BSSA, toluene-activating enzyme
ECTree
Advanced search results
General Information
General Information on EC 4.1.99.11 - benzylsuccinate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
metabolism
physiological function
additional information
evolution
enzyme BSS is a member of the glycyl radical enzyme (GRE) family
evolution
-
enzyme BSS is a member of the glycyl radical enzyme (GRE) family. Structure and function of benzylsuccinate synthase and related fumarate-adding glycyl radical enzymes, phylogenetic analysis, overview
evolution
enzyme BSS is a member of the glycyl radical enzyme (GRE) family. Structure and function of benzylsuccinate synthase and related fumarate-adding glycyl radical enzymes, phylogenetic analysis, overview
evolution
enzyme BSS is a member of the glycyl radical enzyme (GRE) family. Structure and function of benzylsuccinate synthase and related fumarate-adding glycyl radical enzymes, phylogenetic analysis, overview
evolution
-
enzyme BSS is a member of the glycyl radical enzyme (GRE) family. Structure and function of benzylsuccinate synthase and related fumarate-adding glycyl radical enzymes, phylogenetic analysis, overview
-
-
BSSA gene encoding the alpha-subunit of Bss from a novel taxon of the Betaproteobacteria catalyzes the first step in anaerobic toluene degradation
metabolism
-
BSSA gene encoding the alpha-subunit of Bss from a novel taxon of the Betaproteobacteria catalyzes the first step in anaerobic toluene degradation
-
-
a novel benzylsuccinate synthase alpha-subunit (bssA) sequence type in sedimentary microbial community originating from a tar-oil-contaminated aquifer at a former coal gasification plant
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
physiological function
the enzyme is a glycyl radical enzyme that catalyzes the enantiospecific fumarate addition to toluene initiating its anaerobic metabolism in the denitrifying bacterium Thauera aromatica
the catalytic subunit has the putative radical sites located on Cys492 and Gly828, induced-fit product docking approach and substrate-bound molecular dynamics simulations based on the refined active site topology, three-dimensional structure homology modeling, overview
additional information
-
enzyme structure and structure-based mechanistic models, overview. The QM cluster model contains whole or fragmented side chains of nine active site amino acids surrounding the bound substrates, Glu189, Tyr197, Ser199, Ile384, Leu391, Leu492, Cys493, Arg508, and Val709
additional information
enzyme structure and structure-based mechanistic models, overview. The QM cluster model contains whole or fragmented side chains of nine active site amino acids surrounding the bound substrates, Glu189, Tyr197, Ser199, Ile384, Leu391, Leu492, Cys493, Arg508, and Val709
additional information
enzyme structure and structure-based mechanistic models, overview. The QM cluster model contains whole or fragmented side chains of nine active site amino acids surrounding the bound substrates, Glu189, Tyr197, Ser199, Ile384, Leu391, Leu492, Cys493, Arg508, and Val709
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
additional information
the C-C bond-forming reaction performed by BSS and its relatives requires an oxygen-sensitive radical cofactor. BSS is a member of the glycyl radical enzyme (GRE) family and contains a backbone glycyl radical in its activated form
additional information
-
enzyme structure and structure-based mechanistic models, overview. The QM cluster model contains whole or fragmented side chains of nine active site amino acids surrounding the bound substrates, Glu189, Tyr197, Ser199, Ile384, Leu391, Leu492, Cys493, Arg508, and Val709
-