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benzylsuccinate = toluene + fumarate
benzylsuccinate = toluene + fumarate
mechanism
-
benzylsuccinate = toluene + fumarate
stereospecific radical addition of toluene to fumarate, enzyme carries a stable organic free radical, most probably located on glycine residue 828
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benzylsuccinate = toluene + fumarate
substrate binding stabilizing the active site and reaction mechanism via glycyl radical, detailed overview. Syn addition of toluene to fumaric acid and facilitation of a mechanism that retains the hydrogen abstracted from the methyl group of toluene within the succinyl moiety. The stability of substrates at the active site and the occurrence of feasible radical transfer distances between the thiyl radical, substrates, and the active site glycine indicate a substrate-assisted radical transfer pathway governing fumarate addition
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
benzylsuccinate = toluene + fumarate
benzylsuccinate synthase (BSS) catalyzes the formation of a C-C bond between toluene and fumarate by a radical mechanism. BSS binds substrates in a buried active site and uses conformational changes to gate access. The C-C bond-forming reaction performed by BSS requires an oxygen-sensitive radical cofactor. BSS contains a backbone glycyl radical in its activated form. The two substrates adopt orientations that appear ideal for radical-mediated C-C bond formation, the methyl group of toluene is positioned between fumarate and a cysteine that forms a thiyl radical during catalysis, which is in turn adjacent to the glycine that serves as a radical storage residue. Toluene is held in place by fumarate on one face and tight packing by hydrophobic residues on the other face and sides. These hydrophobic residues appear to become ordered, thus encapsulating toluene, only in the presence of BSSbeta, a small protein subunit that forms a tight complex with BSSalpha, the catalytic subunit. Substrates can enter the active site through a channel, which can be blocked by subunit beta, BSSbeta plays a role in gating active site accessibility
benzylsuccinate = toluene + fumarate
DFT model of the reaction mechanism of BSS, mechanistic modeling
-
benzylsuccinate = toluene + fumarate
DFT model of the reaction mechanism of BSS, mechanistic modeling
benzylsuccinate = toluene + fumarate
DFT model of the reaction mechanism of BSS, mechanistic modeling
benzylsuccinate = toluene + fumarate
reaction mechanism of enzymatic radical C-C coupling by benzylsuccinate synthase, molecular dynamics (MD) simulations and quantum mechanics (QM) modeling, detailed overview. 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, and this reaction represents the general mechanism of toluene degradation in all known anaerobic degraders. The enantiospecificity of the enzyme seems to be enforced by a thermodynamic preference for binding of fumarate in the pro-(R)-orientation and reverse preference of benzyl radical attack on fumarate in pro-(S)-pathway which results with prohibitively high energy barrier of the radical quenching
benzylsuccinate = toluene + fumarate
stereospecific radical addition of toluene to fumarate, enzyme carries a stable organic free radical, most probably located on glycine residue 828
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benzylsuccinate = toluene + fumarate
DFT model of the reaction mechanism of BSS, mechanistic modeling
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benzylsuccinate = toluene + fumarate
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2-fluorotoluene + fumarate
(2-fluorobenzyl)succinate
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?
3-fluorotoluene + fumarate
(3-fluorobenzyl)succinate
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?
4-fluorotoluene + fumarate
(4-fluorobenzyl)succinate
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?
benzaldehyde + fumarate
benzoylsuccinate
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?
benzylsuccinate
toluene + fumarate
m-cresol + fumarate
(3-hydroxybenzyl)succinic acid
m-xylene + fumarate
(3-methylbenzyl)succinic acid
m-xylene-d6 + fumarate
(3-methylbenzyl)succinate-d6
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?
o-cresol + fumarate
(2-hydroxybenzyl)succinic acid
o-xylene + fumarate
(2-methylbenzyl)succinic acid
o-xylene-d10 + fumarate
(2-methylbenzyl)succinate-d10
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?
p-cresol + fumarate
(4-hydroxybenzyl)succinic acid
p-xylene + fumarate
(4-methylbenzyl)succinic acid
p-xylene-d10 + fumarate
(4-methylbenzyl)succinate-d10
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?
toluene + fumarate
benzylsuccinate
toluene + maleate
benzylsuccinate
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?
[d3-methyl]toluene + fumarate
?
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deuterium is transferred from toluene to the C-3 pro-(S) position of benzylsuccinate, implying that the addition of toluene to the double bond of fumarate is syn
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?
[d3-methyl]toluene + maleate
?
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addition of toluene occurs in anti fashion. Formation of the C-3 radical of the benzylsuccinate as an intermediate, in which rotation about the C-2-C-3 bond can occur to relieve the sterically unfavorable cis conformation
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?
additional information
?
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benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
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?
benzylsuccinate
toluene + fumarate
enzyme-substrate interactions at the active site by molecular dynamics simulations, overview
involvement of Phe384, Leu390, Leu491, Tyr829, and Val708 in stabilizing toluene binding and Ser827, Glu509, and Gln706 in stabilizing fumaric acid binding
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?
m-cresol + fumarate
(3-hydroxybenzyl)succinic acid
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?
m-cresol + fumarate
(3-hydroxybenzyl)succinic acid
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?
m-cresol + fumarate
(3-hydroxybenzyl)succinic acid
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?
m-cresol + fumarate
(3-hydroxybenzyl)succinic acid
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?
m-xylene + fumarate
(3-methylbenzyl)succinic acid
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-
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?
m-xylene + fumarate
(3-methylbenzyl)succinic acid
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-
-
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?
m-xylene + fumarate
(3-methylbenzyl)succinic acid
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-
-
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?
m-xylene + fumarate
(3-methylbenzyl)succinic acid
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?
o-cresol + fumarate
(2-hydroxybenzyl)succinic acid
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-
-
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?
o-cresol + fumarate
(2-hydroxybenzyl)succinic acid
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-
-
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?
o-cresol + fumarate
(2-hydroxybenzyl)succinic acid
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-
-
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?
o-cresol + fumarate
(2-hydroxybenzyl)succinic acid
-
-
-
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?
o-xylene + fumarate
(2-methylbenzyl)succinic acid
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-
-
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?
o-xylene + fumarate
(2-methylbenzyl)succinic acid
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?
o-xylene + fumarate
(2-methylbenzyl)succinic acid
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-
-
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?
o-xylene + fumarate
(2-methylbenzyl)succinic acid
-
-
-
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?
p-cresol + fumarate
(4-hydroxybenzyl)succinic acid
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-
-
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?
p-cresol + fumarate
(4-hydroxybenzyl)succinic acid
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-
-
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?
p-xylene + fumarate
(4-methylbenzyl)succinic acid
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?
p-xylene + fumarate
(4-methylbenzyl)succinic acid
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
-
first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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on incubation of fresh sediments with (13)C(7)-toluene, the production of both sulfide and (13)CO(2) is coupled to the (13)C-labeling of DNA of microbes related to Desulfosporosinus spp. within the Peptococcaceae (Clostridia)
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
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highly stereospecific, enantiomer purity for (R-)-(+)-benzylsuccinate 99%
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?
toluene + fumarate
benzylsuccinate
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first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
-
first step in the anaerobic degradation pathway of toluene
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ir
toluene + fumarate
benzylsuccinate
benzylsuccinate synthase (BSS) catalyzes the formation of a C-C bond between toluene and fumarate by a radical mechanism. BSS binds substrates in a buried active site and uses conformational changes to gate access. Both substrates can bind to the BSSalphabetagamma complex
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?
toluene + fumarate
benzylsuccinate
the enzyme generates enantiospecifically (R)-benzylsuccinate from fumarate and toluene
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r
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
-
first step in the anaerobic degradation pathway of toluene
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?
toluene + fumarate
benzylsuccinate
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?
toluene + fumarate
benzylsuccinate
-
first step in the anaerobic degradation pathway of toluene
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?
additional information
?
-
docking of the substrates into the relaxed active site and structure of the enzyme-product complex, overview. The active site cavity contains two hydrophobic regions, which are involved in interacting with the benzene ring and the protonated carboxyl group, respectively. On the other hand, a hydrophilic portion of the active site cavity binds the deprotonated carboxylic group by a strong electrostatic interaction towards Arg508 and a range of hydrogen bonds. Kinetic isotope effect of 4.0 for [2H] substituents at the methyl group of toluene
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?
additional information
?
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docking of the substrates into the relaxed active site and structure of the enzyme-product complex, overview. The active site cavity contains two hydrophobic regions, which are involved in interacting with the benzene ring and the protonated carboxyl group, respectively. On the other hand, a hydrophilic portion of the active site cavity binds the deprotonated carboxylic group by a strong electrostatic interaction towards Arg508 and a range of hydrogen bonds. Kinetic isotope effect of 4.0 for [2H] substituents at the methyl group of toluene
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?
additional information
?
-
substrate-bound structures of benzylsuccinate synthase, fumarate is secured at the bottom of a long active site cavity with toluene bound directly above it. The two substrates adopt orientations that appear ideal for radical-mediated C-C bond formation, the methyl group of toluene is positioned between fumarate and a cysteine that forms a thiyl radical during catalysis, which is in turn adjacent to the glycine that serves as a radical storage residue. Toluene is held in place by fumarate on one face and tight packing by hydrophobic residues on the other face and sides. These hydrophobic residues appear to become ordered, thus encapsulating toluene, only in the presence of BSSbeta, a small protein subunit that forms a tight complex with BSSalpha, the catalytic subunit. Toluene is activated in anaerobic hydrocarbon degradation, overview. Fumarate binding stabilizes a partially closed conformation in the dimeric BSSalphagamma
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?
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evolution
the enzyme belongs to the glycyl radical enzyme family
evolution
enzyme BSS is a member of the glycyl radical enzyme (GRE) family
evolution
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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
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metabolism
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BSSA gene encoding the alpha-subunit of Bss from a novel taxon of the Betaproteobacteria catalyzes the first step in anaerobic toluene degradation
metabolism
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BSSA gene encoding the alpha-subunit of Bss from a novel taxon of the Betaproteobacteria catalyzes the first step in anaerobic toluene degradation
-
physiological function
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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
additional information
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
structure homology modeling
additional information
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structure homology modeling
additional information
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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
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?
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98000, SDS-PAGE of the alpha subunit
heterotrimer
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alpha, beta and gamma subunit
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
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 presumably carries out the catalysis, whereas the two small subunits of 8.5 and 6.5 kDa each contain a low-potential [4Fe4S]-cluster
hexamer
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alpha2 beta2 gamma2, three subunits encoded by the genes tutF, tutD, and tutG
hexamer
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the structural model for benzylsuccinate synthase proposes an alpha2beta2gamma2-complex
hexamer
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alpha2 beta2 gamma2, three subunits encoded by the genes tutF, tutD, and tutG
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tetramer
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alpha, alpha', beta, gamma, 1 * 97000 + 1 * 97000 + 1 * 14500 + 1 * 6500, SDS-PAGE
tetramer
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alpha, alpha', beta, gamma, 1 * 94000 + 1 * 90000 + 1 * 12000 + 1 * 10000, SDS-PAGE
additional information
the enzyme has a trimeric structure of alpha-, beta- and gamma subunits. Structure comparisons of BSS enzymes and BSS-like fumarate-adding enzymes (FAEs)
additional information
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the enzyme has a trimeric structure of alpha-, beta- and gamma subunits. Structure comparisons of BSS enzymes and BSS-like fumarate-adding enzymes (FAEs)
additional information
analysis of BSSalpha-BSSgamma subunit interactions and of BSSalpha-BSSbeta subunit interactions, detailed overview
additional information
the enzyme has a trimeric structure of alpha-, beta- and gamma subunits. Structure comparisons of BSS enzymes and BSS-like fumarate-adding enzymes (FAEs)
additional information
-
the enzyme has a trimeric structure of alpha-, beta- and gamma subunits. Structure comparisons of BSS enzymes and BSS-like fumarate-adding enzymes (FAEs)
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Krieger, C.J.; Rosebooms, W.; Albrachts, P.J.; Spormann, A.M.
A stable organic free radical in anaerobic benzylsuccinate synthase of Azoarcus sp. strain T
J. Biol. Chem.
276
12924-12927
2001
Azoarcus sp., Azoarcus sp. T
brenda
Beller, H.R.; Edwards, E.A.
Anaerobic toluene activation by benzylsuccinate synthase in a highly enriched methanogenic culture
Appl. Environ. Microbiol.
66
5503-5505
2000
Desulfotomaculum, Methanothrix sp., Methanospirillum sp.
brenda
Beller, H.R.; Spormann, A.M.
Substrate range of benzylsuccinate synthase from Azoarcus sp. strain T
FEMS Microbiol. Lett.
178
147-153
1999
Azoarcus sp.
brenda
Leutwein, C.; Heider, J.
Anaerobic toluene-catabolic pathway in denitrifying Thauera aromatica: activation and beta-oxidation of the first intermediate, (R)-(+)-benzylsuccinate
Microbiology
145
3265-3271
1999
Thauera aromatica
brenda
Beller, H.R.; Spormann, A.M.
Analysis of the novel benzylsuccinate synthase reaction for anaerobic toluene activation based on structural studies of the product
J. Bacteriol.
180
5454-5457
1998
Azoarcus sp.
brenda
Leuthner, B.; Leutwein, C.; Schultz,H.; Hrth, P.; Haehnel, W.; Schiltz, E.; Schgger, H.; Heider, J.
Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalaysing the first step in anaerobic toluene metabolism
Mol. Microbiol.
28
615-628
1998
Thauera aromatica
brenda
Verfrth, K.; Pierik, A.J.; Leutwein, C.; Zorn, S.; Heider, J.
Substrate specificities and electron paramagnetic resonance properties of benzylsuccinate synthases in anaerobic toluene and m-xylene metabolism
Arch. Microbiol.
181
155-162
2004
Azoarcus sp., Azoarcus sp. T, Thauera aromatica, Thauera aromatica K172
brenda
Qiao, C.; Marsh, E.N.G.
Mechanism of benzylsuccinate synthase: Stereochemistry of toluene addition to fumarate and maleate
J. Am. Chem. Soc.
127
8608-8609
2005
Thauera aromatica
brenda
Bhandare, R.; Calabro, M.; Coschigano, P.W.
Site-directed mutagenesis of the Thauera aromatica strain T1 tutE tutFDGH gene cluster
Biochem. Biophys. Res. Commun.
346
992-998
2006
Thauera aromatica, Thauera aromatica T1
brenda
Li, L.; Marsh, E.N.
Deuterium isotope effects in the unusual addition of toluene to fumarate catalyzed by benzylsuccinate synthase
Biochemistry
45
13932-13938
2006
Thauera aromatica
brenda
Winderl, C.; Schaefer, S.; Lueders, T.
Detection of anaerobic toluene and hydrocarbon degraders in contaminated aquifers using benzylsuccinate synthase (bssA) genes as a functional marker
Environ. Microbiol.
9
1035-1046
2007
Azoarcus sp., Thauera aromatica, Desulfotomaculum sp., Desulfobacula toluolica, Geobacter grbiciae, Geobacter sp., Desulfosarcina cetonica, Desulfotomaculum sp. OX39, Geobacter sp. TMJ1, Azoarcus sp. T, Thauera aromatica K172
brenda
Li, L.; Patterson, D.P.; Fox, C.C.; Lin, B.; Coschigano, P.W.; Marsh, E.N.
Subunit structure of benzylsuccinate synthase (dagger)
Biochemistry
48
1284-1292
2009
Thauera aromatica
brenda
Musat, F.; Galushko, A.; Jacob, J.; Widdel, F.; Kube, M.; Reinhardt, R.; Wilkes, H.; Schink, B.; Rabus, R.
Anaerobic degradation of naphthalene and 2-methylnaphthalene by strains of marine sulfate-reducing bacteria
Environ. Microbiol.
11
209-219
2009
uncultured delta proteobacterium
brenda
Vogt, C.; Cyrus, E.; Herklotz, I.; Schlosser, D.; Bahr, A.; Herrmann, S.; Richnow, H.H.; Fischer, A.
Evaluation of toluene degradation pathways by two-dimensional stable isotope fractionation
Environ. Sci. Technol.
42
7793-7800
2008
Azoarcus sp., Thauera aromatica, Desulfosarcina cetonica, Blastochloris sulfoviridis, Azoarcus sp. T
brenda
Salinero, K.; Keller, K.; Feil, W.; Feil, H.; Trong, S.; Di Bartolo, G.; Lapidus, A.
Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: Indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation
BMC Genomics
10
351
2009
no activity in Dechloromonas aromatica RCB
brenda
Weelink, S.A.; van Doesburg, W.; Saia, F.T.; Rijpstra, W.I.; Roeling, W.F.; Smidt, H.; Stams, A.J.
A strictly anaerobic betaproteobacterium Georgfuchsia toluolica gen. nov., sp. nov. degrades aromatic compounds with Fe(III), Mn(IV) or nitrate as an electron acceptor
FEMS Microbiol. Ecol.
70
575-585
2009
Georgfuchsia toluolica, Georgfuchsia toluolica G5G6
brenda
Winderl, C.; Penning, H.; Netzer, F.V.; Meckenstock, R.U.; Lueders, T.
DNA-SIP identifies sulfate-reducing Clostridia as important toluene degraders in tar-oil-contaminated aquifer sediment
ISME J.
4
1314-1325
2010
Clostridia
brenda
Hilberg, M.; Pierik, A.J.; Bill, E.; Friedrich, T.; Lippert, M.L.; Heider, J.
Identification of FeS clusters in the glycyl-radical enzyme benzylsuccinate synthase via EPR and Moessbauer spectroscopy
J. Biol. Inorg. Chem.
17
49-56
2012
Escherichia coli
brenda
Bharadwaj, V.S.; Dean, A.M.; Maupin, C.M.
Insights into the glycyl radical enzyme active site of benzylsuccinate synthase: a computational study
J. Am. Chem. Soc.
135
12279-12288
2013
Thauera sp. DNT-1 (Q8L1A3)
brenda
Kuemmel, S.; Kuntze, K.; Vogt, C.; Boll, M.; Heider, J.; Richnow, H.H.
Evidence for benzylsuccinate synthase subtypes obtained by using stable isotope tools
J. Bacteriol.
195
4660-4667
2013
Desulfosarcina cetonica (A2TBP7), Thauera aromatica (O87943), Geobacter metallireducens (Q39VF1), Azoarcus sp. (Q8VPT7), Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210 (Q39VF1), Desulfosarcina cetonica DSM 7267 (A2TBP7), Azoarcus sp. T (Q8VPT7), Thauera aromatica K172 (O87943)
brenda
Szaleniec, M.; Heider, J.
Modeling of the reaction mechanism of enzymatic radical C-C coupling by benzylsuccinate synthase
Int. J. Mol. Sci.
17
514
2016
Thauera aromatica (O87943 AND O87944 AND O87942), Thauera aromatica
brenda
Funk, M.A.; Marsh, E.N.; Drennan, C.L.
Substrate-bound structures of benzylsuccinate synthase reveal how toluene is activated in anaerobic hydrocarbon degradation
J. Biol. Chem.
290
22398-22408
2015
Thauera aromatica (O87943 AND O87944 AND O87942)
brenda
Heider, J.; Szaleniec, M.; Martins, B.M.; Seyhan, D.; Buckel, W.; Golding, B.T.
Structure and function of benzylsuccinate synthase and related fumarate-adding glycyl radical enzymes
J. Mol. Microbiol. Biotechnol.
26
29-44
2016
Desulfosarcina cetonica, Azoarcus sp. CIB (I6LHT8), Thauera aromatica (O87943 AND O87944 AND O87942), Thauera aromatica K172 (O87943 AND O87944 AND O87942)
brenda
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
Proc. Natl. Acad. Sci. USA
111
10161-10166
2014
Thauera aromatica (O87943 AND O87944 AND O87942)
brenda