Identifying the missing steps of the autotrophic 3-hydroxypropionate CO
            <sub>2</sub>
            fixation cycle in
            <i>Chloroflexus aurantiacus</i>

Zarzycki, Jan; Brecht, Volker; Müller, Michael; Fuchs, Georg

doi:10.1073/pnas.0908356106

Cited by 210 publications

(194 citation statements)

References 47 publications

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“…A mixture of mesaconyl-C1-CoA and mesaconyl-C4-CoA was synthesized chemically from the free acid by the mixed anhydride method of Stadtman (1957). From this mixture, mesaconyl-C1-CoA was purified using highperformance liquid chromatography (Zarzycki et al, 2009). The dry powders of the CoA-esters were stored at − 20°C.…”

Section: Synthesesmentioning

confidence: 99%

“…β-Methylmalyl-CoA was synthesized enzymatically with recombinant (S)-malyl-CoA/β-methylmalyl-CoA/(S)-citramalyl-CoA lyase from Chloroflexus aurantiacus (Zarzycki et al, 2009), as described previously (Sasikaran et al, 2014). A mixture of mesaconyl-C1-CoA and mesaconyl-C4-CoA was synthesized chemically from the free acid by the mixed anhydride method of Stadtman (1957).…”

Section: Synthesesmentioning

confidence: 99%

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The methylaspartate cycle in haloarchaea and its possible role in carbon metabolism

et al. 2015

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Haloarchaea (class Halobacteria) live in extremely halophilic conditions and evolved many unique metabolic features, which help them to adapt to their environment. The methylaspartate cycle, an anaplerotic acetate assimilation pathway recently proposed for Haloarcula marismortui, is one of these special adaptations. In this cycle, acetyl-CoA is oxidized to glyoxylate via methylaspartate as a characteristic intermediate. The following glyoxylate condensation with another molecule of acetylCoA yields malate, a starting substrate for anabolism. The proposal of the functioning of the cycle was based mainly on in vitro data, leaving several open questions concerning the enzymology involved and the occurrence of the cycle in halophilic archaea. Using gene deletion mutants of H. hispanica, enzyme assays and metabolite analysis, we now close these gaps by unambiguous identification of the genes encoding all characteristic enzymes of the cycle. Based on these results, we were able to perform a solid study of the distribution of the methylaspartate cycle and the alternative acetate assimilation strategy, the glyoxylate cycle, among haloarchaea. We found that both of these cycles are evenly distributed in haloarchaea. Interestingly, 83% of the species using the methylaspartate cycle possess also the genes for polyhydroxyalkanoate biosynthesis, whereas only 34% of the species with the glyoxylate cycle are capable to synthesize this storage compound. This finding suggests that the methylaspartate cycle is shaped for polyhydroxyalkanoate utilization during carbon starvation, whereas the glyoxylate cycle is probably adapted for growth on substrates metabolized via acetyl-CoA.

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Section: Synthesesmentioning

confidence: 99%

Section: Synthesesmentioning

confidence: 99%

The methylaspartate cycle in haloarchaea and its possible role in carbon metabolism

et al. 2015

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“…Nevertheless, this pilot work shaped the path for ACCase metabolic engineering in bacteria and thus proved that this multisubunit enzyme might be reconstituted in bacteria and is able to efficiently produce fatty acids. Some of the reoccurring problems were solved by equipping the E. coli strain overexpressing ACCase ge- (Zarzycki et al 2009). Acetyl-coenzyme A and propionyl-coenzyme A carboxylases facilitate an inorganic carbon dioxide fixation forming glyoxylate nes with additional modifications, targeted to directly increase fatty acids production efficiency (Lu et al, 2008).…”

Section: Accase In Bacteria and Algae-based Biotech Projectsmentioning

confidence: 99%

“…Whereas a global demand for renewable fuel makes fatty acids production in bacteria the most obvious goal of biotechnology, the other bacterial routes of malonyl-CoA processing may also find practical applications. One of such promising pathways is the 3-hydroxypropionate cycle in autotrophic carbon fixation present in some bacteria and archaeons, which allows them to fix inorganic carbon dioxide (or bicarbonate), as shown schematically in Figure 4 (Zarzycki et al, 2009;Tabita, 2009). The ability to synthesize all building blocks of life from the most oxidized form of carbon is of particularly great biotechnological value as a method for production of an unlimited variety of compounds or carbon dioxide sequestration.…”

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confidence: 99%

OPINIONS Acetyl-coenzyme A carboxylase – an attractive enzyme for biotechnology

Podkowiński¹,

Tworak²

2011

bta

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Acetyl-CoA carboxylase catalyzes the carboxylation of acetyl-CoA to malonyl-CoA. This reaction constitutes the first committed step of fatty acid synthesis in most organisms, while its product also serves as a universal precursor for various other high-value compounds. The important regulatory and rate-limiting role of acetyl-CoA carboxylase makes this enzyme a powerful tool in a variety of biotechnological and medical projects. This review presents the current knowledge on structural and functional features of the enzyme and focuses on its divergent applications. Different metabolic engineering attempts that lead to the production of various compounds, such as fatty acids, polyketides or flavonoids, are presented and their advantages and limitations discussed. The importance of studies on acetyl-CoA carboxylase activity for design and development of new herbicides and antibiotics as well as for medical intervention is also highlighted. Acetyl-coenzyme A carboxylase -enzyme architecture, biochemistry and its role in cell physiologyA variety of biotechnological projects targeted to modulate acetyl-coenzyme A carboxylase activity in bacteria, plants and humans have been proposed and experimentally tested. Here, we would like to present a comprehensive review of these strategies together with a survey of the potential of acetyl-CoA carboxylase for biotechnology.Acetyl-coenzyme A carboxylase (ACC, E.C.6.4.1.2), recognized as an essential enzyme for all Eukaryotes and the majority of Bacteria, is responsible for carboxylation of acetyl-CoA that results in malonyl-coenzyme A formation (Fig. 1). Malonyl-CoA is a major building block for compounds such as fatty acids, polyketides and flavonoids -important components for cell growth, as well as for food, pharmaceuticals and energy production.The malonyl-CoA synthesis consists of two half-reactions (Nikolau et al., 2003). The first one, adenosine triphosphate-dependent carboxylation of biotin prosthetic group covalently bound to a module named biotin carboxyl carrier protein (BCCP), is catalyzed by ACCase segment of biotin carboxylase activity (BC) (Fig. 2). This reaction is immediately followed by the second half-re action: the transfer of a carboxyl group from carboxylated biotin to acetyl-CoA, resulting in malonyl-CoA formation. Carboxyl transferase (CT) is a module that catalyzes the second reaction and provides the required specificity in recognition of the carboxyl acceptor (acetyl-CoA). The ACCase model usually presents BCCP, a module with covalently attached biotin, as a beam responsible for biotin dislocation between two active centers -one with BT and the other with CT activity. The three (Fig. 3). The prokaryotic and eukaryotic types of ACCases are evolutionary related and the phylogeny of the modules provides some hints about their cenancestor, a split between Archaea and Bacteria, and arising of Eukaryota (Lombard and Moreira, 2011).Phylogeny is out of scope of this manuscript, but acetyl-coenzyme A carboxylases from various organisms representing v...

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“…Besides this, they are able to grow in aerobic chemo-organotrophic conditions (Hanada & Pierson, 2006). Autotrophic CO 2 assimilation by the representatives of family Chloroflexaceae (Chloroflexus aurantiacus) is performed through the 3-hydroxypropionate cycle (Herter et al, 2002;Zarzycki et al, 2009). The representatives of the family Oscillochloridaceae are able to grow as photo-organotrophs and photolithotrophs, and they are strict anaerobes (Keppen et al, 1994(Keppen et al, , 2000.…”

Section: Introductionmentioning

confidence: 99%

Reconstruction of bacteriochlorophyll biosynthesis pathways in the filamentous anoxygenic phototrophic bacterium Oscillochloris trichoides DG-6 and evolution of anoxygenic phototrophs of the order Chloroflexales

et al. 2015

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It is commonly accepted that green filamentous anoxygenic phototrophic (FAP) bacteria are the most ancient representatives of phototrophic micro-organisms. Modern FAPs belonging to the order Chloroflexales are divided into two suborders: Chloroflexineae and Roseiflexineae. Representatives of Roseiflexineae lack chlorosomes and synthesize bacteriochlorophyll a, whereas those of Chloroflexineae synthesize bacteriochlorophylls a and c and utilize chlorosomes for light harvesting. Though they constitute a small number of species, FAPs are quite diverse in their physiology. This bacterial group includes autotrophs and heterotrophs, thermophiles and mesophiles, aerobes and anaerobes, occupying both freshwater and halophilic environments. The anaerobic mesophilic autotroph Oscillochloris trichoides DG-6 is still not well studied in its physiology, and its evolutionary origin remains unclear. The goals of this study included identification of the reaction centre type of O. trichoides DG-6, reconstruction of its bacteriochlorophyll biosynthesis pathways, and determination of its evolutionary relationships with other FAPs. By enzymic and genomic analysis, the presence of RCII in O. trichoides DG-6 was demonstrated and the complete gene set involved in biosynthesis of bacteriochlorophylls a and c was established. We found that the bacteriochlorophyll gene sets differed between aerobic and anaerobic FAPs. The aerobic FAP genomes code oxygen-dependent AcsF cyclases, but lack the bchQ/bchR genes, which have been associated with adaptation to low light conditions in the anaerobic FAPs. A scenario of evolution of FAPs belonging to the order Chloroflexales is proposed.

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Identifying the missing steps of the autotrophic 3-hydroxypropionate CO ₂ fixation cycle in Chloroflexus aurantiacus

Cited by 210 publications

References 47 publications

The methylaspartate cycle in haloarchaea and its possible role in carbon metabolism

The methylaspartate cycle in haloarchaea and its possible role in carbon metabolism

OPINIONS Acetyl-coenzyme A carboxylase – an attractive enzyme for biotechnology

Reconstruction of bacteriochlorophyll biosynthesis pathways in the filamentous anoxygenic phototrophic bacterium Oscillochloris trichoides DG-6 and evolution of anoxygenic phototrophs of the order Chloroflexales

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Identifying the missing steps of the autotrophic 3-hydroxypropionate CO 2 fixation cycle in Chloroflexus aurantiacus

Cited by 210 publications

References 47 publications

The methylaspartate cycle in haloarchaea and its possible role in carbon metabolism

The methylaspartate cycle in haloarchaea and its possible role in carbon metabolism

OPINIONS Acetyl-coenzyme A carboxylase – an attractive enzyme for biotechnology

Reconstruction of bacteriochlorophyll biosynthesis pathways in the filamentous anoxygenic phototrophic bacterium Oscillochloris trichoides DG-6 and evolution of anoxygenic phototrophs of the order Chloroflexales

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Identifying the missing steps of the autotrophic 3-hydroxypropionate CO ₂ fixation cycle in Chloroflexus aurantiacus