Enzymes Involved in a Novel Anaerobic Cyclohexane Carboxylic Acid Degradation Pathway

Kung, Johannes W.; Meier, Anne-Katrin; Mergelsberg, Mario; Boll, Matthias

doi:10.1128/jb.02071-14

Cited by 26 publications

(32 citation statements)

References 36 publications

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“…1972;Mohn et al, 1999). The Z. resiniphila genomes harbor multiple monooxygenase, dioxygenase and dehydrogenase genes for aerobic degradation of aromatic compounds including toluene, benzoate, 2-nitrobenzoate, long-chain alkylphenol (lap), cinnamic acid, pcymene, indole-3-acetic acid, cyclohexanecaboxylate, extradiol, and xanthine (Muraki et al, 2003;Leveau and Lindow, 2005;Kung et al, 2014). The catechol derivatives could be oxidized by central meta-cleavage pathway to 2-hydroxymuconic semialdehyde by catechol 2,3-dioxygenase in the Zoogloea strains (Arai et al, 2000).…”

Section: Carbon Source Utilizationmentioning

confidence: 99%

Comparative genomics analyses on EPS biosynthesis genes required for floc formation of Zoogloea resiniphila and other activated sludge bacteria

et al. 2016

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Section: Carbon Source Utilizationmentioning

confidence: 99%

Comparative genomics analyses on EPS biosynthesis genes required for floc formation of Zoogloea resiniphila and other activated sludge bacteria

et al. 2016

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“…The ChCoA dehydrogenase of R. palustris involved in this pathway shows only 29% amino acid sequence identity with the ChCoA dehydrogenase from S. aciditrophicus . This finding suggests that this pathway evolved independently of the cyclohexane carboxylate degradation pathway of Deltaproteobacteria [Kung et al, 2014]. It is evident that all bacteria that degrade cyclohexane carboxylate can also grow with aromatic compounds but not vice versa [Aklujkar et al, 2010;Peters et al, 2004;Prakash et al, 2010;Wischgoll et al, 2005].…”

Section: Cyclohexane Carboxylate Fermentation Versus Degradationmentioning

confidence: 75%

“…In G. metallireducens the enzyme plays a role in the complete degradation of cyclohexane carboxylate to CO 2 coupled to respiratory Fe(III) or nitrate reduction [Kung et al, 2014]. Accordingly, the ring moiety of the reduced Ch1CoA was bound into the expected active site position sandwiched between the isoalloxazine ring of FAD and Thr363, Asn241, Ile87 and Asp91 (online suppl.…”

Section: Ch1coa Dehydrogenasementioning

confidence: 99%

“…In respiring organisms these genes are used for complete cyclohexane carboxylate degradation, as demonstrated for G. metallireducens. In this organism a succinylCoA:cyclohexane carboxylate CoA transferase activates the substrate [Kung et al, 2014]. In S. aciditrophicus the ChCoA and Ch1CoA dehydrogenases are expected to play a crucial role in both axenic cyclohexane carboxylate formation and syntrophic cyclohexane carboxylate oxidation [Kung et al, 2013].…”

Section: Cyclohexane Carboxylate Fermentation Versus Degradationmentioning

confidence: 99%

“…2 , 3 ). The enzymatic steps that convert this intermediate to cyclohexane carboxylate have only recently been studied, and a 1,2-adding as well as an unusual 1,4-adding acyl-CoA dehydrogenase were characterized [Kung et al, 2013[Kung et al, , 2014 ( fig. 4 ).…”

Section: Characteristic Enzymes Involved In Cyclohexane Carboxylate Fmentioning

confidence: 99%

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Fermentative Cyclohexane Carboxylate Formation in <b><i>Syntrophus aciditrophicus</i></b>

et al. 2016

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Short-chain fatty acids such as acetic, propionic, butyric or lactic acids are typical primary fermentation products in the anaerobic feeding chain. Fifteen years ago, a novel fermentation type was discovered in the obligately anaerobic Deltaproteobacterium Syntrophus aciditrophicus. During fermentative growth with crotonate and/or benzoate, acetate is formed in the oxidative branch and cyclohexane carboxylate in the reductive branch. In both cases cyclohexa-1,5-diene-1-carboxyl-CoA (Ch1,5CoA) is a central intermediate that is either formed by a class II benzoyl-CoA reductase (fermentation of benzoate) or by reverse reactions of the benzoyl-CoA degradation pathway (fermentation of crotonate). Here, we summarize the current knowledge of the enzymology involved in fermentations yielding cyclohexane carboxylate as an excreted product. The characteristic enzymes involved are two acyl-CoA dehydrogenases specifically acting on Ch1,5CoA and cyclohex-1-ene-1-carboxyl-CoA. Both enzymes are also employed during the syntrophic growth of S. aciditrophicus with cyclohexane carboxylate as the carbon source in coculture with a methanogen. An investigation of anabolic pathways in S. aciditrophicus revealed a rather unusual pathway for glutamate synthesis involving a Re-citrate synthase. Future work has to address the unresolved question concerning which components are involved in reoxidation of the NADH formed in the oxidative branch of the unique cyclohexane carboxylate fermentation pathway in S. aciditrophicus.

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Structural Basis of Cyclic 1,3‐Diene Forming Acyl‐Coenzyme A Dehydrogenases

et al. 2021

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The biologically important, FAD-containing acyl-coenzyme A (CoA) dehydrogenases (ACAD) usually catalyze the anti-1,2elimination of a proton and a hydride of aliphatic CoA thioesters. Here, we report on the structure and function of an ACAD from anaerobic bacteria catalyzing the unprecedented 1,4-elimination at C3 and C6 of cyclohex-1-ene-1-carboxyl-CoA (Ch1CoA) to cyclohex-1,5-diene-1-carboxyl-CoA (Ch1,5CoA) and at C3 and C4 of the latter to benzoyl-CoA. Based on highresolution Ch1CoA dehydrogenase crystal structures, the unorthodox reactivity is explained by the presence of a catalytic aspartate base (D91) at C3, and by eliminating the catalytic glutamate base at C1. Moreover, C6 of Ch1CoA and C4 of Ch1,5CoA are positioned towards FAD-N5 to favor the biologically relevant C3,C6-over the C3,C4-dehydrogenation activity. The C1,C2-dehydrogenation activity was regained by structure-inspired amino acid exchanges. The results provide the structural rationale for the extended catalytic repertoire of ACADs and offer previously unknown biocatalytic options for the synthesis of cyclic 1,3-diene building blocks.

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Enzymes Involved in a Novel Anaerobic Cyclohexane Carboxylic Acid Degradation Pathway

Cited by 26 publications

References 36 publications

Comparative genomics analyses on EPS biosynthesis genes required for floc formation of Zoogloea resiniphila and other activated sludge bacteria

Comparative genomics analyses on EPS biosynthesis genes required for floc formation of Zoogloea resiniphila and other activated sludge bacteria

Fermentative Cyclohexane Carboxylate Formation in <b><i>Syntrophus aciditrophicus</i></b>

Structural Basis of Cyclic 1,3‐Diene Forming Acyl‐Coenzyme A Dehydrogenases

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