Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon <i>Sulfolobus solfataricus</i>

Payne, K.A.P.; Hough, David W.; Danson, Michael J.

doi:10.1016/j.febslet.2010.02.037

Cited by 12 publications

(8 citation statements)

References 20 publications

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“…These data also suggest that P. furiosus is unable to take up acetoin, since the concentration of acetoin continues to rise throughout the growth phase for the COM1c and AHDA strains. Only one archaeon, Sulfolobus solfataricus, has been reported to utilize acetoin as an energy source and, although it contains an als homolog similar to P. furiosus als, it is not known to produce acetoin (22).…”

Section: Als Is Responsible For Acetoin Formation In P Furiosusmentioning

confidence: 99%

Temperature-dependent acetoin production by Pyrococcus furiosus is catalyzed by a biosynthetic acetolactate synthase and its deletion improves ethanol production

Nguyen

Lipscomb

Schut

et al. 2016

Metabolic Engineering

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The hyperthermophilic archaeon, Pyrococcus furiosus, grows optimally near 100°C by fermenting sugars to acetate, carbon dioxide and molecular hydrogen as the major end products. The organism has recently been exploited to produce biofuels using a temperature-dependent metabolic switch using genes from microorganisms that grow near 70°C. However, little is known about its metabolism at the lower temperatures. We show here that P. furiosus produces acetoin (3-hydroxybutanone) as a major product at temperatures below 80°C. A novel type of acetolactate synthase (ALS), which is involved in branched-chain amino acid biosynthesis, is responsible and deletion of the als gene abolishes acetoin production. Accordingly, deletion of als in a strain of P. furiosus containing a novel pathway for ethanol production significantly improved the yield of ethanol. These results also demonstrate that P. furiosus is a potential platform for the biological production of acetoin at temperatures in the 70-80°C range.

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Section: Als Is Responsible For Acetoin Formation In P Furiosusmentioning

confidence: 99%

Temperature-dependent acetoin production by Pyrococcus furiosus is catalyzed by a biosynthetic acetolactate synthase and its deletion improves ethanol production

Nguyen

Lipscomb

Schut

et al. 2016

Metabolic Engineering

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“…The initial step of acetoin breakdown was catalysed by AoDH ES E1 in the catabolic pathway of acetoin in bacteria [4]. Only AoDH ESs from mesophilic bacteria were characterized before Payne et al [39] reported the AoDH ES from a hyperthermophilic archaeon Sulfolobus solfataricus with an optimum temperature of 80°C. This study thus provided an example of a moderately thermophilic AoDH ES.…”

Section: Discussionmentioning

confidence: 99%

Thermophilic fermentation of acetoin and 2,3-butanediol by a novel Geobacillus strain

Xiao

Wang

Zhao

et al. 2012

Biotechnol Biofuels

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BackgroundAcetoin and 2,3-butanediol are two important biorefinery platform chemicals. They are currently fermented below 40°C using mesophilic strains, but the processes often suffer from bacterial contamination.ResultsThis work reports the isolation and identification of a novel aerobic Geobacillus strain XT15 capable of producing both of these chemicals under elevated temperatures, thus reducing the risk of bacterial contamination. The optimum growth temperature was found to be between 45 and 55°C and the medium initial pH to be 8.0. In addition to glucose, galactose, mannitol, arabionose, and xylose were all acceptable substrates, enabling the potential use of cellulosic biomass as the feedstock. XT15 preferred organic nitrogen sources including corn steep liquor powder, a cheap by-product from corn wet-milling. At 55°C, 7.7 g/L of acetoin and 14.5 g/L of 2,3-butanediol could be obtained using corn steep liquor powder as a nitrogen source. Thirteen volatile products from the cultivation broth of XT15 were identified by gas chromatography–mass spectrometry. Acetoin, 2,3-butanediol, and their derivatives including a novel metabolite 2,3-dihydroxy-3-methylheptan-4-one, accounted for a total of about 96% of all the volatile products. In contrast, organic acids and other products were minor by-products. α-Acetolactate decarboxylase and acetoin:2,6-dichlorophenolindophenol oxidoreductase in XT15, the two key enzymes in acetoin metabolic pathway, were found to be both moderately thermophilic with the identical optimum temperature of 45°C.ConclusionsGeobacillus sp. XT15 is the first naturally occurring thermophile excreting acetoin and/or 2,3-butanediol. This work has demonstrated the attractive prospect of developing it as an industrial strain in the thermophilic fermentation of acetoin and 2,3-butanediol with improved anti-contamination performance. The novel metabolites and enzymes identified in XT15 also indicated its strong promise as a precious biological resource. Thermophilic fermentation also offers great prospect for improving its yields and efficiencies. This remains a core aim for future work.

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“…A second lipoylated complex with activity related to PDH is the acetoin dehydrogenase complex (AoDH); like PDH, AoDH also produces acetyl-CoA. AoDH is only found in bacteria, and is responsible for the catabolism of the acetoin energy storage molecule into acetyl-CoA and acetylaldehyde [23,24].…”

Section: Metabolic Roles Of Lipoylated Complexesmentioning

confidence: 99%

Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease

Rowland

Snowden

Cristea

2018

Current Opinion in Chemical Biology

138

109

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Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape. The dysregulation of these mitochondrial proteins is linked to a range of human metabolic disorders. Perhaps most striking is that lipoylation itself, the proteins that add or remove the modification, as well as the proteins it decorates are all evolutionarily conserved from bacteria to humans, highlighting the importance of this essential cofactor. Here, we discuss the biological significance of protein lipoylation, the importance of understanding its regulation in health and disease states, and the advances in mass spectrometry-based proteomic technologies that can aid these studies.

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Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus

Cited by 12 publications

References 20 publications

Temperature-dependent acetoin production by Pyrococcus furiosus is catalyzed by a biosynthetic acetolactate synthase and its deletion improves ethanol production

Temperature-dependent acetoin production by Pyrococcus furiosus is catalyzed by a biosynthetic acetolactate synthase and its deletion improves ethanol production

Thermophilic fermentation of acetoin and 2,3-butanediol by a novel Geobacillus strain

Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease

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