A new family of CoA‐transferases

Heider, Johann

doi:10.1016/s0014-5793(01)03178-7

Cited by 123 publications

(165 citation statements)

References 36 publications

Supporting

Mentioning

155

Contrasting

Unclassified

Order By: Relevance

“…A2-183 that belongs to the family I CoA-transferases (Heider, 2001), based on its ping-pong reaction mechanism as well as its sequence relationship with other CoA-transferases. The deduced protein sequence showed the highest similarity to a presumptive acetyl-CoA hydrolase sequence from D. hafniense.…”

Section: Discussionmentioning

confidence: 99%

A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria

Charrier¹,

Duncan²,

Reid³

et al. 2006

Microbiology

View full text Add to dashboard Cite

Bacterial butyryl-CoA CoA-transferase activity plays a key role in butyrate formation in the human colon, but the enzyme and corresponding gene responsible for this activity have not previously been identified. A novel CoA-transferase gene is described from the colonic bacterium Roseburia sp. A2-183, with similarity to acetyl-CoA hydrolase as well as 4-hydroxybutyrate CoA-transferase sequences. The gene product, overexpressed in an Escherichia coli lysate, showed activity with butyryl-CoA and to a lesser degree propionyl-CoA in the presence of acetate. Butyrate, propionate, isobutyrate and valerate competed with acetate as the co-substrate. Despite the sequence similarity to 4-hydroxybutyrate CoA-transferases, 4-hydroxybutyrate did not compete with acetate as the co-substrate. Thus the CoA-transferase preferentially uses butyryl-CoA as substrate. Similar genes were identified in other butyrate-producing human gut bacteria from clostridial clusters IV and XIVa, while other candidate CoA-transferases for butyrate formation could not be detected in Roseburia sp. A2-183. This suggests strongly that the newly identified group of CoA-transferases described here plays a key role in butyrate formation in the human colon.

show abstract

Section: Discussionmentioning

confidence: 99%

A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria

Charrier¹,

Duncan²,

Reid³

et al. 2006

Microbiology

View full text Add to dashboard Cite

show abstract

“…A variety of genes encoding putative enzymes with CoA-transferase activities were identified, indicating that various organic substrates could be activated for beta-oxidation (Supplementary Table 2). Most CoA-transferases were related to 'family III' type enzymes, which are typically highly substrate specific (Heider 2001). Genes encoding enzymes of the methylmalonyl-CoA pathway were detected and included at least eight copies of methylmalonyl-CoA mutases in the primary data set and a propionyl-CoA carboxylase in the fragment data set (Supplementary Table 2).…”

Section: Electron Donating and Processing Reactionsmentioning

confidence: 99%

Genome sequencing of a single cell of the widely distributed marine subsurface Dehalococcoidia, phylum Chloroflexi

et al. 2013

View full text Add to dashboard Cite

Bacteria of the class Dehalococcoidia (DEH), phylum Chloroflexi, are widely distributed in the marine subsurface, yet metabolic properties of the many uncultivated lineages are completely unknown. This study therefore analysed genomic content from a single DEH cell designated 'DEH-J10' obtained from the sediments of Aarhus Bay, Denmark. Real-time PCR showed the DEH-J10 phylotype was abundant in upper sediments but was absent below 160 cm below sea floor. A 1.44 Mbp assembly was obtained and was estimated to represent up to 60.8% of the full genome. The predicted genome is much larger than genomes of cultivated DEH and appears to confer metabolic versatility. Numerous genes encoding enzymes of core and auxiliary beta-oxidation pathways were identified, suggesting that this organism is capable of oxidising various fatty acids and/or structurally related substrates. Additional substrate versatility was indicated by genes, which may enable the bacterium to oxidise aromatic compounds. Genes encoding enzymes of the reductive acetyl-CoA pathway were identified, which may also enable the fixation of CO 2 or oxidation of organics completely to CO 2 . Genes encoding a putative dimethylsulphoxide reductase were the only evidence for a respiratory terminal reductase. No evidence for reductive dehalogenase genes was found. Genetic evidence also suggests that the organism could synthesise ATP by converting acetyl-CoA to acetate by substrate-level phosphorylation. Other encoded enzymes putatively conferring marine adaptations such as salt tolerance and organo-sulphate sulfohydrolysis were identified. Together, these analyses provide the first insights into the potential metabolic traits that may enable members of the DEH to occupy an ecological niche in marine sediments.

show abstract

“…Oxidation of the 3α-hydroxy group is followed by the formation of 3-oxo-Δ 4 -cholenoic acid-CoA intermediates by unidentified NAD(P)(H)-dependent 3-oxo-Δ 4 -cholenoic acid oxidoreductase(s). At some point in the pathway, the CoA-ester is hydrolyzed or more likely the CoA moiety is transferred to incoming primary bile acids (2,(29)(30)(31). The baiF gene product has been shown to have bile acid CoA hydrolase activity (32); however, recent evidence indicates that the baiF belongs to a family of enzymes that have CoA transferase activity (2,30).…”

Section: Introductionmentioning

confidence: 99%

“…At some point in the pathway, the CoA-ester is hydrolyzed or more likely the CoA moiety is transferred to incoming primary bile acids (2,(29)(30)(31). The baiF gene product has been shown to have bile acid CoA hydrolase activity (32); however, recent evidence indicates that the baiF belongs to a family of enzymes that have CoA transferase activity (2,30). The gene encoding the bile acid 7α-dehydratase has been shown to be the baiE gene product; however, the 7β-dehydratase has not been identified, although is predicted to be encoded by the baiI, a homologue of the baiE located on the same bai operon (33).…”

Section: Introductionmentioning

confidence: 99%

Clostridium scindens baiCD and baiH genes encode stereo-specific 7α/7β-hydroxy-3-oxo-Δ4-cholenoic acid oxidoreductases☆

Kang

Ridlon

Moore

et al. 2008

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

View full text Add to dashboard Cite

Secondary bile acids, formed by intestinal bacteria, are suggested to play a significant role in cancers of the gastrointestinal tract in humans. Bile acid 7α/β-dehydroxylation is carried out by a few species of intestinal clostridia which harbor a multi-gene bile acid inducible (bai) operon. Several genes encoding enzymes in this pathway have been cloned and characterized. However, no gene product (s) has yet been assigned to the production of 3-oxo-Δ 4 -cholenoic acid intermediates of cholic acid (CA), chenodeoxycholic acid (CDCA) or ursodeoxycholic acid (UDCA). We previously reported the baiH gene encodes an NADH:flavin oxidoreductase (NADH:FOR); however, the role of this protein in bile acid 7-dehydroxylation is unclear. Homology searches and secondary structural alignments suggest this protein to be similar to flavoproteins which reduce α/β-unsaturated carbonyl compounds. The baiH gene product was expressed in E. coli, purified and discovered to be a stereospecific NAD(H)-dependent 7β-hydroxy-3-oxo-Δ 4 -cholenoic acid oxidoreductase. Additionally, high sequence similarity between the baiH and baiCD gene products suggests the baiCD gene may encode a 3-oxo-Δ 4 -cholenoic acid oxidoreductase specific for CDCA and CA. We tested this hypothesis using cell extracts prepared from E. coli overexpressing the baiCD gene and discovered that it encodes a stereo-specific NAD(H)-dependent 7α-hydroxy-3-oxo-Δ 4 -cholenoic acid oxidoreductase.

show abstract

A new family of CoA‐transferases

Cited by 123 publications

References 36 publications

A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria

A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria

Genome sequencing of a single cell of the widely distributed marine subsurface Dehalococcoidia, phylum Chloroflexi

Clostridium scindens baiCD and baiH genes encode stereo-specific 7α/7β-hydroxy-3-oxo-Δ4-cholenoic acid oxidoreductases☆

Contact Info

Product

Resources

About