The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
the structure of the GDHDes-glutaconyl-CoA complex is completely compatible with the mechanism of the reductive half-reaction established for acyl-CoA dehydrogenases, which is characterized by the rupture of two kinetically stable C-H bonds. The substrate binds to the re side of the FAD ring, and the C2-C3 bond is sandwiched between the carboxylate group of Glu367 and the pyrimidine ring of FAD, mechanism, overview
The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
Substrates: GDHGeo contains highly conserved amino acid residues that are specifically involved in the decarboxylation of the intermediate glutaconyl-CoA Products: -
Substrates: GDHGeo contains highly conserved amino acid residues that are specifically involved in the decarboxylation of the intermediate glutaconyl-CoA Products: -
Substrates: the decarboxylating, EC 1.3.99.7, and nondecarboxylating capabilities are provided by complex structural changes around the glutaconyl carboxylate group, the key factor being a Tyr to Val exchange strictly conserved between the two GDH types, the interaction between the glutaconyl carboxylate and the guanidinium group of a conserved Arg is stronger in GDHDes than in the decarboxylating enzyme, molecular dynamics. The identified structural changes prevent decarboxylation 1. by strengthening the C4-C5 bond of glutaconyl-CoA, 2. by reducing the leaving group potential of CO2, and 3. by increasing the distance between the C4 atom, negatively charged in the dienolate transition state, and the adjacent glutamic acid Products: -
Substrates: GDHGeo contains highly conserved amino acid residues that are specifically involved in the decarboxylation of the intermediate glutaconyl-CoA Products: -
Substrates: GDHGeo contains highly conserved amino acid residues that are specifically involved in the decarboxylation of the intermediate glutaconyl-CoA Products: -
Substrates: the decarboxylating, EC 1.3.99.7, and nondecarboxylating capabilities are provided by complex structural changes around the glutaconyl carboxylate group, the key factor being a Tyr to Val exchange strictly conserved between the two GDH types, the interaction between the glutaconyl carboxylate and the guanidinium group of a conserved Arg is stronger in GDHDes than in the decarboxylating enzyme, molecular dynamics. The identified structural changes prevent decarboxylation 1. by strengthening the C4-C5 bond of glutaconyl-CoA, 2. by reducing the leaving group potential of CO2, and 3. by increasing the distance between the C4 atom, negatively charged in the dienolate transition state, and the adjacent glutamic acid Products: -
0.65 mol FAD/mol of enzyme, altered ratios of mutant enzymes, except for mutant V88S, overview. With the exception of V88S, all enzyme variants essentially loose the FAD cofactor
the organism conserves the free energy of decarboxylation by a Na+-pumping glutaconyl-CoA decarboxylase. Glutaconyl-Co A-forming GDH is a nondecarboxylating enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged GDHDes, hanging drop vapor diffusion method, 20 mg/ml protein in 10 mM MES, pH 6.0, 0.5 M KCl, 10% w/v glycerol, 1 mM DTT, 1 mM FAD, and 2 mM glutaryl-CoA are mixed with an equal volume of reservoir solution containing 50% v/v MPD, 0.1 M Tris-HCl, pH 8.5, and 0.2 M NH4H2PO4, at 4°C, X-ray diffraction structure determination and analysis
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The mutant enzyme shows a higher tetramer conformation than the wild-type
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The mutant enzyme shows a higher tetramer conformation than the wild-type
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The mutant enzyme shows a higher tetramer conformation than the wild-type
screening of a cosmid gene library, DNA and amino acid sequence determination and analysis, expression of His6-tagged GDHDes in Escherichia coli strain BL21(DE3)
show
top
