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3-Sulfinopropionyl coenzyme A (3SP-CoA) desulfinase (AcdDPN7 ) is a new desulfinase that catalyzes the sulfur abstraction from 3SP-CoA in the betaproteobacteriumAdvenella mimigardefordensis strain DPN7T . During investigation of a Tn5 ::mob -induced mutant defective in growth on 3,3′-dithiodipropionate (DTDP) and also 3-sulfinopropionate (3SP), the transposon insertion was mapped to an open reading frame with the highest homology to an acyl-CoA dehydrogenase (Acd) fromBurkholderia phenoliruptrix strain BR3459a (83% identical and 91% similar amino acids). AnA. mimigardefordensis Δacd mutant was generated and verified the observed phenotype of the Tn5 ::mob -induced mutant. For enzymatic studies, AcdDPN7 was heterologously expressed inEscherichia coli BL21(DE3)/pLysS by using pET23a::acd DPN7 . The purified protein is yellow and contains a noncovalently bound flavin adenine dinucleotide (FAD) cofactor, as verified by high-performance liquid chromatography–electrospray ionization mass spectrometry (HPLC-ESI-MS) analyses. Size-exclusion chromatography revealed a native molecular mass of about 173 kDa, indicating a homotetrameric structure (theoretically 179 kDa), which is in accordance with other members of the acyl-CoA dehydrogenase superfamily.In vitro assays unequivocally demonstrated that the purified enzyme converted 3SP-CoA into propionyl-CoA and sulfite (SO3 2− ). Kinetic studies of AcdDPN7 revealed aV max of 4.19 μmol min−1 mg−1 , an apparentKm of 0.013 mM, and ak cat /Km of 240.8 s−1 mM−1 for 3SP-CoA. However, AcdDPN7 is unable to perform a dehydrogenation, which is the usual reaction catalyzed by members of the acyl-CoA dehydrogenase superfamily. Comparison to other known desulfinases showed a comparably high catalytic efficiency of AcdDPN7 and indicated a novel reaction mechanism. Hence, AcdDPN7 encodes a new desulfinase based on an acyl-CoA dehydrogenase (EC 1.3.8.x) scaffold. Concomitantly, we identified the gene product that is responsible for the final desulfination step during catabolism of 3,3′-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioesters.

journal of bacteriology

A Novel 3-Sulfinopropionyl Coenzyme A (3SP-CoA) Desulfinase from Advenella mimigardefordensis Strain DPN7 <sup>T</sup> Acting as a Key Enzyme during Catabolism of 3,3′-Dithiodipropionic Acid Is a Member of the Acyl-CoA Dehydrogenase Superfamily

A Novel 3-Sulfinopropionyl Coenzyme A (3SP-CoA) Desulfinase from Advenella mimigardefordensis Strain DPN7 T Acting as a Key Enzyme during Catabolism of 3,3′-Dithiodipropionic Acid Is a Member of the Acyl-CoA Dehydrogenase Superfamily

A Novel 3-Sulfinopropionyl Coenzyme A (3SP-CoA) Desulfinase from Advenella mimigardefordensis Strain DPN7 ^T Acting as a Key Enzyme during Catabolism of 3,3′-Dithiodipropionic Acid Is a Member of the Acyl-CoA Dehydrogenase Superfamily