Methylcrotonyl-CoA and geranyl-CoA carboxylases are involved in leucine/isovalerate utilization (Liu) and acyclic terpene utilization (Atu), and are encoded by liuB/liuD and atuC/atuF, in Pseudomonas aeruginosa

Höschle, Birgit; Gnau, Volker; Jendrossek, Dieter

doi:10.1099/mic.0.28260-0

Cited by 52 publications

(55 citation statements)

References 20 publications

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“…However, in contrast to other acyl-CoA esters, which are usually carboxylated at the ␣ position, the CO 2 group is in this case introduced at the ␥ position (50,52,59). Recently, the genes encoding geranoyl-CoA carboxylase, a homolog of 3-methylcrotonyl-CoA carboxylase, were identified and functionally assigned (4,63). Geranoyl-CoA carboxylase is involved in the degradation of branched iosoprenoids (acylic terpenes) and also employs ␥-carboxylation to overcome incomplete ␤-oxidation (50,51).…”

Section: Carboxylases In Assimilatory Pathwaysmentioning

confidence: 99%

Carboxylases in Natural and Synthetic Microbial Pathways

Erb

2011

Appl Environ Microbiol

183

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Carboxylases are among the most important enzymes in the biosphere, because they catalyze a key reaction in the global carbon cycle: the fixation of inorganic carbon (CO 2 ). This minireview discusses the physiological roles of carboxylases in different microbial pathways that range from autotrophy, carbon assimilation, and anaplerosis to biosynthetic and redox-balancing functions. In addition, the current and possible future uses of carboxylation reactions in synthetic biology are discussed. Such uses include the possible transformation of the greenhouse gas carbon dioxide into value-added compounds and the production of novel antibiotics.

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Section: Carboxylases In Assimilatory Pathwaysmentioning

confidence: 99%

Carboxylases in Natural and Synthetic Microbial Pathways

Erb

2011

Appl Environ Microbiol

183

165

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“…A combination of functional and genome context analysis, as depicted in the SEED Viewer subsystems "leucine degradation," "isoleucine degradation," and "valine degradation" (at http://seed-viewer.theseed.org/), provided convincing evidence for the presence of the ILV catabolic pathways in a number of diverse bacteria (30). According to this analysis, the ILV catabolic pathways are present in many lineages of gammaproteobacteria (e.g., in Pseudomonas aeruginosa and Shewanella oneidensis), with a notable exception of Escherichia coli and other enterobacteria.The liu gene cluster involved in leucine and isovalerate utilization was recently identified and characterized for P. aeruginosa (1,11,15). Functional roles of the liuABCDE genes are shown in Fig.…”

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confidence: 99%

“…The liu gene cluster involved in leucine and isovalerate utilization was recently identified and characterized for P. aeruginosa (1,11,15). Functional roles of the liuABCDE genes are shown in Fig.…”

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Comparative Genomics of Regulation of Fatty Acid and Branched-Chain Amino Acid Utilization in Proteobacteria

et al. 2009

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Bacteria can use branched-chain amino acids (ILV, i.e., isoleucine, leucine, valine) and fatty acids (FAs) as sole carbon and energy sources converting ILV into acetyl-coenzyme A (CoA), propanoyl-CoA, and propionylCoA, respectively. In this work, we used the comparative genomic approach to identify candidate transcriptional factors and DNA motifs that control ILV and FA utilization pathways in proteobacteria. The metabolic regulons were characterized based on the identification and comparison of candidate transcription factor binding sites in groups of phylogenetically related genomes. The reconstructed ILV/FA regulatory network demonstrates considerable variability and involves six transcriptional factors from the MerR, TetR, and GntR families binding to 11 distinct DNA motifs. The ILV degradation genes in gamma-and betaproteobacteria are regulated mainly by a novel regulator from the MerR family (e.g., LiuR in Pseudomonas aeruginosa) (40 species); in addition, the TetR-type regulator LiuQ was identified in some betaproteobacteria (eight species). Besides the core set of ILV utilization genes, the LiuR regulon in some lineages is expanded to include genes from other metabolic pathways, such as the glyoxylate shunt and glutamate synthase in Shewanella species. The FA degradation genes are controlled by four regulators including FadR in gammaproteobacteria (34 species), PsrA in gamma-and betaproteobacteria (45 species), FadP in betaproteobacteria (14 species), and LiuR orthologs in alphaproteobacteria (22 species). The remarkable variability of the regulatory systems associated with the FA degradation pathway is discussed from functional and evolutionary points of view.Proteobacteria comprise one of the largest divisions within prokaryotes and incorporate species possessing a very complex collection of phenotypic and physiological attributes including many phototrophs, heterotrophs, and chemolithotrophs. The proteobacterial group is of great biological significance, as it includes a large number of pathogens and symbionts of animals and plants. Thus, proteobacteria display an amazing versatility in their abilities to use various carbon sources such as carbohydrates, nucleotides, amino acids, and lipids. The degradation of branched-chain amino acids valine, leucine, and isoleucine (ILV) and fatty acids (FAs) is used for ATP and energy production by many proteobacteria.The ILV degradation pathways are outlined in Fig. 1A. The first reaction is transamination to the corresponding ␣-keto acids using either branched-chain amino acid aminotransferase or leucine dehydrogenase. The second step is oxidative decarboxylation to the corresponding acyl-coenzyme A (CoA) derivative coupled to dehydrogenation, which is carried out by a common branched-chain ␣-keto acid dehydrogenase (BCDH) (EC 1.2.4.4) complex. The further conversion of branchedchain acyl-CoA derivatives of ILV amino acids, namely, isovaleryl-CoA for leucine, 2-methylbutanoyl-CoA for isoleucine, and isobutyryl-CoA for valine, into acetyl-CoA and propionyl-CoA is...

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“…1). These enzymes are composed of two subunits, i.e., LiuB and AtuC (␤ subunits) and LiuD and AtuF (␣ subunits), of their respective MCCase and GCCase enzymes (1,10,16). MCCase and GCCase enzymes show two main domains, the acyl-CoA-binding and the carboxybiotin-binding domains, which are implicated in the transfer of a carboxyl group to the acyl-CoA substrate (17).…”

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confidence: 99%