reaction mechanism, residues Arg84, Asp88 and Gln246 side chains and the isoalloxazine ring of FAD define the enzymatic environment for the desulfination reaction. FAD is not involved in electron transfer during the reaction, essential role of Arg84 in catalysis. The enzymatic reaction might progress with hydrogen-bond formation and charge transfer between the guanidinium cation of Arg84 and 3-sulfinopropanoyl-CoA, which would favour nucleophilic attack of a water molecule on the S atom of the sulfino group
reaction mechanism, residues Arg84, Asp88 and Gln246 side chains and the isoalloxazine ring of FAD define the enzymatic environment for the desulfination reaction. FAD is not involved in electron transfer during the reaction, essential role of Arg84 in catalysis. The enzymatic reaction might progress with hydrogen-bond formation and charge transfer between the guanidinium cation of Arg84 and 3-sulfinopropanoyl-CoA, which would favour nucleophilic attack of a water molecule on the S atom of the sulfino group
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
shows high amino acid sequence similarity of acyl-CoA dehydrogenases, but no dehydrogenation activity of acyl-CoA thioesters (butyryl-CoA, isobutyryl-CoA, and valeryl-CoA) is observed
the enzyme is a tetramer with each subunit containing one flavin adenine dinucleotide (FAD) molecule, binding structure, overview. FAD is not involved in electron transfer during the reaction
the enzyme is responsilbe for the final defulfination step during catabolism of 3,3'-dithiopropionate, a sulfur-containing substrate for biosynthensis of polythioesters, the final reaction before propionyl-CoA enters the central metabolism on the level of the methylcitric acid cycle
the enzyme is responsilbe for the final defulfination step during catabolism of 3,3'-dithiopropionate, a sulfur-containing substrate for biosynthensis of polythioesters, the final reaction before propionyl-CoA enters the central metabolism on the level of the methylcitric acid cycle
Arg84 is a key residue in the desulfination reaction, the guanidinium group of the arginine is essential for desulfination, modelling of the enzyme-substrate complex, overview. Structure-function analysis and active site structure determination, modeling of substrate binding. The Arg84, Asp88 and Gln246 side chains and the isoalloxazine ring of FAD define the enzymatic environment for the desulfination reaction
Arg84 is a key residue in the desulfination reaction, the guanidinium group of the arginine is essential for desulfination, modelling of the enzyme-substrate complex, overview. Structure-function analysis and active site structure determination, modeling of substrate binding. The Arg84, Asp88 and Gln246 side chains and the isoalloxazine ring of FAD define the enzymatic environment for the desulfination reaction
Arg84 is a key residue in the desulfination reaction, the guanidinium group of the arginine is essential for desulfination, modelling of the enzyme-substrate complex, overview. Structure-function analysis and active site structure determination, modeling of substrate binding. The Arg84, Asp88 and Gln246 side chains and the isoalloxazine ring of FAD define the enzymatic environment for the desulfination reaction
gel filtration of the native protein, indicating a homotetrameric structure, in accordance with other members of the acyl-CoA dehydrogenase superfamily, in accordance to the theoretical molecular mass of 179200 Da
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant apoenzyme and enzyme in complex with the CoA moiety from the substrate analogue succinyl-CoA, hanging drop vapour diffusion, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.4, with 0.002 ml of reservoir solution containing 0.1 M Bis-Tris, pH 6.5, and 5-20% PEG 3350, in the absence or presence of 4 mM succinyl-CoA, X-ray diffraction structure determination and analysis at 1.89 A and 2.30 A resolution, respectively, molecular replacement using the monomer of an acyl-CoA dehydrogenase (Acd) from Thermus thermophilus HB8 as search model
the enzyme is part of the 3,3'-dithiopropionate degradation pathway. The elucidation of this pathway and the identification of the genes could provide an strategy to engineer strains suitable for biotechnological production of polythioesters
the enzyme is part of the 3,3'-dithiopropionate degradation pathway. The elucidation of this pathway and the identification of the genes could provide an strategy to engineer strains suitable for biotechnological production of polythioesters
Wuebbeler, J.H.; Bruland, N.; Kretschmer, K.; Steinbuechel, A.
Novel pathway for catabolism of the organic sulfur compound 3,3-dithiodipropionic acid via 3-mercaptopropionic acid and 3-Sulfinopropionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7
Schürmann, M.; Deters, A.; Wübbeler, J.H.; Steinbüchel, A.
A novel 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis strain DPN7T acting as a key enzyme during catabolism of 3,3'-dithiodipropionic acid is a member of the acyl-CoA dehydrogenase superfamily
Schuermann, M.; Meijers, R.; Schneider, T.R.; Steinbuechel, A.; Cianci, M.
3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold