Diversions of the Shikimate Pathway — The Biosynthesis of Cyclohexanecarboxylic Acid

Floss, Heinz G.; Cho, H.; Casati, R.; Reynolds, Kevin A.; Kennedy, Eileen; Moore, Bradley S.; Beale, John M.; Mocek, Ursula; Poralla, Karl

doi:10.1007/978-1-4615-3012-1_6

Cited by 4 publications

(2 citation statements)

References 20 publications

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“…An energy-conserving synthetase or a transferase is likely to catalyze the final cyclohexane carboxylate-releasing step. This pathway represents an alternative route to the known cyclohexane carboxylate formation pathway from shikimate, which has been described for Streptomyces species and Alicyclobacillus species (17,18).…”

Section: Discussionmentioning

confidence: 93%

Cyclohexanecarboxyl-Coenzyme A (CoA) and Cyclohex-1-ene-1-Carboxyl-CoA Dehydrogenases, Two Enzymes Involved in the Fermentation of Benzoate and Crotonate in Syntrophus aciditrophicus

Kung¹,

Seifert²,

Bergen³

et al. 2013

Journal of Bacteriology

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The strictly anaerobic Syntrophus aciditrophicus is a fermenting deltaproteobacterium that is able to degrade benzoate or crotonate in the presence and in the absence of a hydrogen-consuming partner. During growth in pure culture, both substrates are dismutated to acetate and cyclohexane carboxylate. In this work, the unknown enzymes involved in the late steps of cyclohexane carboxylate formation were studied. Using enzyme assays monitoring the oxidative direction, a cyclohex-1-ene-1-carboxyl-CoA (Ch1CoA)-forming cyclohexanecarboxyl-CoA (ChCoA) dehydrogenase was purified and characterized from S. aciditrophicus and after heterologous expression of its gene in Escherichia coli. In addition, a cyclohexa-1,5-diene-1-carboxyl-CoA (Ch1,5CoA)-forming Ch1CoA dehydrogenase was characterized after purification of the heterologously expressed gene. Both enzymes had a native molecular mass of 150 kDa and were composed of a single, 40-to 45-kDa subunit; both contained flavin adenine dinucleotide (FAD) as a cofactor. While the ChCoA dehydrogenase was competitively inhibited by Ch1CoA in the oxidative direction, Ch1CoA dehydrogenase further converted the product Ch1,5CoA to benzoyl-CoA. The results obtained suggest that Ch1,5CoA is a common intermediate in benzoate and crotonate fermentation that serves as an electron-accepting substrate for the two consecutively operating acyl-CoA dehydrogenases characterized in this work. In the case of benzoate fermentation, Ch1,5CoA is formed by a class II benzoyl-CoA reductase; in the case of crotonate fermentation, Ch1,5CoA is formed by reversing the reactions of the benzoyl-CoA degradation pathway that are also employed during the oxidative (degradative) branch of benzoate fermentation.

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Section: Discussionmentioning

confidence: 93%

Cyclohexanecarboxyl-Coenzyme A (CoA) and Cyclohex-1-ene-1-Carboxyl-CoA Dehydrogenases, Two Enzymes Involved in the Fermentation of Benzoate and Crotonate in Syntrophus aciditrophicus

Kung¹,

Seifert²,

Bergen³

et al. 2013

Journal of Bacteriology

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“…The alicyclic compound cyclohexane carboxylate (CHC) is present in the environment where it is synthesized as a functional moiety of plant secondary products (Floss et al, 1992 ), as part of polyketide antibiotics produced by some microorganisms, e.g. Streptomyces species (Cropp et al, 2000 ), or as a metabolite produced during fermentation of benzoate or crotonate (Boll et al, 2016 ; Kung et al, 2013 ; Mouttaki et al, 2007 ).…”

Section: Introductionmentioning

confidence: 99%

Genetic characterization of the cyclohexane carboxylate degradation pathway in the denitrifying bacterium Aromatoleum sp. CIB

Sanz

Dı́az

2022

Environmental Microbiology

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The alicyclic compound cyclohexane carboxylate (CHC) is anaerobically degraded through a peripheral pathway that converges with the central benzoyl‐CoA degradation pathway of aromatic compounds in Rhodopseudomonas palustris (bad pathway) and some strictly anaerobic bacteria. Here we show that in denitrifying bacteria, e.g. Aromatoleum sp. CIB strain, CHC is degraded through a bad‐ali pathway similar to that reported in R. palustris but that does not share common intermediates with the benzoyl‐CoA degradation pathway (bzd pathway) of this bacterium. The bad‐ali genes are also involved in the aerobic degradation of CHC in strain CIB, and orthologous bad‐ali clusters have been identified in the genomes of a wide variety of bacteria. Expression of bad‐ali genes in strain CIB is under control of the BadR transcriptional repressor, which was shown to recognize CHC‐CoA, the first intermediate of the pathway, as effector, and whose operator region (CAAN4TTG) was conserved in bad‐ali clusters from Gram‐negative bacteria. The bad‐ali and bzd pathways generate pimelyl‐CoA and 3‐hydroxypimelyl‐CoA, respectively, that are metabolized through a common aab pathway whose genetic determinants form a supraoperonic clustering with the bad‐ali genes. A synthetic bad‐ali‐aab catabolic module was engineered and it was shown to confer CHC degradation abilities to different bacterial hosts.

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The cyclohexane moiety of rapamycin is derived from shikimic acid inStreptomyces hygroscopicus

Paiva¹,

Roberts²,

Demain³

1993

Journal of Industrial Microbiology

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Diversions of the Shikimate Pathway — The Biosynthesis of Cyclohexanecarboxylic Acid

Cited by 4 publications

References 20 publications

Cyclohexanecarboxyl-Coenzyme A (CoA) and Cyclohex-1-ene-1-Carboxyl-CoA Dehydrogenases, Two Enzymes Involved in the Fermentation of Benzoate and Crotonate in Syntrophus aciditrophicus

Cyclohexanecarboxyl-Coenzyme A (CoA) and Cyclohex-1-ene-1-Carboxyl-CoA Dehydrogenases, Two Enzymes Involved in the Fermentation of Benzoate and Crotonate in Syntrophus aciditrophicus

Genetic characterization of the cyclohexane carboxylate degradation pathway in the denitrifying bacterium Aromatoleum sp. CIB

The cyclohexane moiety of rapamycin is derived from shikimic acid inStreptomyces hygroscopicus

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