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

Schürmann, Marc; Deters, Anika; Wübbeler, Jan Hendrik; Steinbüchel, Alexander

doi:10.1128/jb.02105-12

Cited by 19 publications

(41 citation statements)

References 66 publications

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“…2), and a gene showing homology to acyl-CoA dehydrogenases (acd) is found in the downstream region. Only recently it was shown that acd DPN7 encodes a 3SP-CoA desulfinase (51). Acd TBEA6 shows high homology to Acd DPN7 (79% identical and 88% similar amino acid residues) and to Acd LB400 (64% identical and 76% similar residues).…”

Section: Resultsmentioning

confidence: 99%

“…In A. mimigardefordensis DPN7 T , 3SP is activated by SucCD DPN7 , a succinate-CoA ligase, to 3SP-CoA (step III b) (37). Subsequent abstraction of the sulfur moiety is catalyzed by a desulfinase, Acd, yielding sulfite and propionyl-CoA (step IV) (51). The latter enters the central metabolism via the methylcitric acid cycle.…”

Section: Methodsmentioning

confidence: 99%

“…The complementation vector pBBR1MCS-5::acd DPN7 was constructed and described in a previous study (51,52). In this study, the vector was first transferred to CaCl 2 -competent cells of E. coli S17-1.…”

Section: Methodsmentioning

confidence: 99%

“…3SP-CoA formation by Act TBEA6 was measured by applying A. mimigardefordensis strain DPN7 T 3SP-CoA desulfinase (Acd DPN7 ) as a coupling enzyme in an aerobic continuous spectrophotometric assay (51). Kinetic parameters were determined in cuvettes with a total volume of 1 ml containing 50 mM TrisHCl (pH 7.6), 150 mM NaCl, 0.2 mM 5,5=-dithiobis(2-nitrobenzoic acid) (DTNB), and purified Acd DPN7 as an auxiliary enzyme.…”

Section: Enzyme Assays (I) Initial Identification Of An Appropriate mentioning

confidence: 99%

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Succinyl-CoA:3-Sulfinopropionate CoA-Transferase from Variovorax paradoxus Strain TBEA6, a Novel Member of the Class III Coenzyme A (CoA)-Transferase Family

et al. 2013

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Enzyme Assays (I) Initial Identification Of An Appropriate mentioning

confidence: 99%

See 2 more Smart Citations

Succinyl-CoA:3-Sulfinopropionate CoA-Transferase from Variovorax paradoxus Strain TBEA6, a Novel Member of the Class III Coenzyme A (CoA)-Transferase Family

et al. 2013

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“…7) stands in contrast to the enzymatically catalyzed desulfonation of the analogue in taurine degradation, sulfoacetaldehyde, and to the enzymatically catalyzed desulfinations known so far, of three other organosulfinates: (i) the sulfinate analogue of aspartate, cysteine sulfinate, is desulfinated by aspartate beta-decarboxylase (EC 4.1. 1.12) of Alcaligenes faecalis (54) (57), and (iii) 3-sulfinopropionyl-CoA is desulfinated by a new desulfinase, an acyl-CoA dehydrogenase-superfamily enzyme (EC 1.3.8.x) involved in dissimilation of 3,3=-dithiodipropionate in Advenella mimigardefordensis (58).…”

Section: Discussionmentioning

confidence: 99%

Paracoccus denitrificans PD1222 Utilizes Hypotaurine via Transamination Followed by Spontaneous Desulfination To Yield Acetaldehyde and, Finally, Acetate for Growth

et al. 2013

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Hypotaurine (HT; 2-aminoethane-sulfinate) is known to be utilized by bacteria as a sole source of carbon, nitrogen, and energy for growth, as is taurine (2-aminoethane-sulfonate); however, the corresponding HT degradation pathway has remained undefined. Genome-sequenced Paracoccus denitrificans PD1222 utilized HT (and taurine) quantitatively for heterotrophic growth and released the HT sulfur as sulfite (and sulfate) and HT nitrogen as ammonium. Enzyme assays with cell extracts suggested that an HT-inducible HT:pyruvate aminotransferase (Hpa) catalyzes the deamination of HT in an initial reaction step. Partial purification of the Hpa activity and peptide fingerprinting-mass spectrometry (PF-MS) identified the Hpa candidate gene; it encoded an archetypal taurine:pyruvate aminotransferase (Tpa). The same gene product was identified via differential PAGE and PF-MS, as was the gene of a strongly HT-inducible aldehyde dehydrogenase (Adh). Both genes were overexpressed in Escherichia coli. The overexpressed, purified Hpa/Tpa showed HT:pyruvate-aminotransferase activity. Alanine, acetaldehyde, and sulfite were identified as the reaction products but not sulfinoacetaldehyde; the reaction of Hpa/Tpa with taurine yielded sulfoacetaldehyde, which is stable. The overexpressed, purified Adh oxidized the acetaldehyde generated during the Hpa reaction to acetate in an NAD ؉ -dependent reaction. Based on these results, the following degradation pathway for HT in strain PD1222 can be depicted. The identified aminotransferase converts HT to sulfinoacetaldehyde, which desulfinates spontaneously to acetaldehyde and sulfite; the inducible aldehyde dehydrogenase oxidizes acetaldehyde to yield acetate, which is metabolized, and sulfite, which is excreted.

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Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

Nalivaiko,

Vasseur,

Seebeck

2024

Angewandte Chemie

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Ergothioneine is a sulfur‐containing metabolite that is produced by bacteria and fungi, and is absorbed by plants and animals as a micronutrient. Ergothioneine reacts with harmful oxidants including singlet oxygen or hydrogen peroxide, and may therefore protect cells against oxidative stress. In this report we describe two enzymes from actinobacteria that cooperate in the specific oxidative degradation of ergothioneine. The first enzyme is an iron‐dependent thiol dioxygenase that produces ergothioneine sulfinic acid. A crystal structure of ergothioneine dioxygenase from Thermocatellispora tengchongensis reveals many similarities with cysteine dioxygenases, suggesting that the two enzymes share a common mechanism. The second enzyme is a metal‐dependent ergothioneine sulfinic acid desulfinase that produces Na‐trimethylhistidine and SO2. The discovery that certain actinobacteria contain the enzymatic machinery for O2‐dependent biosynthesis and O2‐dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content

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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

Cited by 19 publications

References 66 publications

Succinyl-CoA:3-Sulfinopropionate CoA-Transferase from Variovorax paradoxus Strain TBEA6, a Novel Member of the Class III Coenzyme A (CoA)-Transferase Family

Succinyl-CoA:3-Sulfinopropionate CoA-Transferase from Variovorax paradoxus Strain TBEA6, a Novel Member of the Class III Coenzyme A (CoA)-Transferase Family

Paracoccus denitrificans PD1222 Utilizes Hypotaurine via Transamination Followed by Spontaneous Desulfination To Yield Acetaldehyde and, Finally, Acetate for Growth

Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

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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

Cited by 19 publications

References 66 publications

Succinyl-CoA:3-Sulfinopropionate CoA-Transferase from Variovorax paradoxus Strain TBEA6, a Novel Member of the Class III Coenzyme A (CoA)-Transferase Family

Succinyl-CoA:3-Sulfinopropionate CoA-Transferase from Variovorax paradoxus Strain TBEA6, a Novel Member of the Class III Coenzyme A (CoA)-Transferase Family

Paracoccus denitrificans PD1222 Utilizes Hypotaurine via Transamination Followed by Spontaneous Desulfination To Yield Acetaldehyde and, Finally, Acetate for Growth

Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

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Product

Resources

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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