Biochemical characterization of a Rhizobium etli monovalent cation-stimulated acyl-coenzyme A carboxylase with a high substrate specificity constant for propionyl-coenzyme A

Dunn, Michael F.; Araíza, Gisela; Mora, Jaime

doi:10.1099/mic.0.26779-0

Cited by 4 publications

(3 citation statements)

References 38 publications

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“…A Rhizobium etli acyl-CoA carboxylase has ~15-fold higher activity toward propionyl-CoA than acetyl-CoA, and it is activated substantially by mono-valent cations, K + , NH 4 + and Cs + [238]. …”

Section: Other Acyl-coa Carboxylasesmentioning

confidence: 99%

Structure and function of biotin-dependent carboxylases

Tong

2012

Cell. Mol. Life Sci.

373

338

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Biotin-dependent carboxylases include acetyl-CoA carboxylase (ACC), propionyl-CoA carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase (GCC), pyruvate carboxylase (PC), and urea carboxylase (UC). They contain biotin carboxylase (BC), carboxyltransferase (CT) and biotin-carboxyl carrier protein (BCCP) components. These enzymes are widely distributed in nature and have important functions in fatty acid metabolism, amino acid metabolism, carbohydrate metabolism, polyketide biosynthesis, urea utilization, and other cellular processes. ACCs are also attractive targets for drug discovery against type 2 diabetes, obesity, cancer, microbial infections, and other diseases, and the plastid ACC of grasses is the target of action of three classes of commercial herbicides. Deficiencies in the activities of PCC, MCC or PC are linked to serious diseases in humans. Our understanding of these enzymes has been greatly enhanced over the past few years by the crystal structures of the holoenzymes of PCC, MCC, PC, and UC. The structures reveal unanticipated features in the architectures of the holoenzymes, including the presence of previously unrecognized domains, and provide a molecular basis for understanding their catalytic mechanism as well as the large collection of disease-causing mutations in PCC, MCC and PC. This review will summarize the recent advances in our knowledge on the structure and function of these important metabolic enzymes.

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Section: Other Acyl-coa Carboxylasesmentioning

confidence: 99%

Structure and function of biotin-dependent carboxylases

Tong

2012

Cell. Mol. Life Sci.

373

338

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“…PYC is required for growth on sugars or pyruvate and, although its inactivation has no effect on nodulation and nitrogen fixation in S. meliloti , R. etli or R. tropici [13,19], it would be interesting to determine whether it plays a role in rhizosphere competition, since sugars are excreted to the rhizosphere by legume roots [20]. The symbiotic phenotype of a rhizobial PCC mutant has not been determined but inactivation of the S. meliloti methylmalonyl‐CoA mutase, which catalyzes the step following that of PCC during propionyl‐CoA degradation, does not affect symbiotic performance [21,22]. ACC has not been characterized but would be expected to be essential for fatty acid synthesis [18] and thus viability.…”

Section: Biotin‐dependent Carboxylases and Biotin–protein Ligase In mentioning

confidence: 99%

Biotin biosynthesis, transport and utilization in rhizobia

Guillén-Navarro

Encarnación

Dunn

2005

FEMS Microbiology Letters

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Biotin, a B-group vitamin, performs an essential metabolic function in all organisms. Rhizobia are alpha-proteobacteria with the remarkable ability to form a nitrogen-fixing symbiosis in combination with a compatible legume host, a process in which the importance of biotin biosynthesis and/or transport has been demonstrated for some rhizobia-legume combinations. Rhizobia have also been used to delimit the biosynthesis, metabolic effects and, more recently, transport of biotin. Molecular genetic analysis shows that an orthodox biotin biosynthesis pathway occurs in some rhizobia while others appear to synthesize the vitamin using alternative pathways. In addition to its well established function as a prosthetic group for biotin-dependent carboxylases, we are beginning to delineate a role for biotin as a metabolic regulator in rhizobia.

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“…Carbon assimilation was diminished under these conditions, mainly due to the lack of the vitamin biotin, which is the prosthetic group of several carboxylases such as acetyl-CoA carboxylase, propionyl-CoA carboxylase, 3-methyl crotonyl-CoA carboxylase, geranyl-CoA carboxylase, urea carboxylase and PYC. The last enzyme is crucial for anaplerotic carbon assimilation through oxaloacetate formation [3,4]. These enzymes consist of biotin carboxylase, carboxyltransferase and biotin carboxyl carrier protein components.…”

Section: Introductionmentioning

confidence: 99%

A Tar aspartate receptor and Rubisco-like protein substitute biotin in the growth of rhizobial strains

et al. 2022

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Biotin is a key cofactor of metabolic carboxylases, although many rhizobial strains are biotin auxotrophs. When some of these strains were serially subcultured in minimal medium, they showed diminished growth and increased excretion of metabolites. The addition of biotin, or genetic complementation with biotin synthesis genes resulted in full growth of Rhizobium etli CFN42 and Rhizobium phaseoli CIAT652 strains. Half of rhizobial genomes did not show genes for biotin biosynthesis, but three-quarters had genes for biotin transport. Some strains had genes for an avidin homologue (rhizavidin), a protein with high affinity for biotin but an unknown role in bacteria. A CFN42-derived rhizavidin mutant showed a sharper growth decrease in subcultures, revealing a role in biotin storage. In the search of biotin-independent growth of subcultures, CFN42 and CIAT652 strains with excess aeration showed optimal growth, as they also did, unexpectedly, with the addition of aspartic acid analogues α- and N-methyl aspartate. Aspartate analogues can be sensed by the chemotaxis aspartate receptor Tar. A tar homologue was identified and its mutants showed no growth recovery with aspartate analogues, indicating requirement of the Tar receptor in such a phenotype. Additionally, tar mutants did not recover full growth with excess aeration. A Rubisco-like protein was found to be necessary for growth as the corresponding mutants showed no recovery either with high aeration or aspartate analogues; also, diminished carboxylation was observed. Taken together, our results indicate a route of biotin-independent growth in rhizobial strains that included oxygen, a Tar receptor and a previously uncharacterized Rubisco-like protein.

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Biochemical characterization of a Rhizobium etli monovalent cation-stimulated acyl-coenzyme A carboxylase with a high substrate specificity constant for propionyl-coenzyme A

Cited by 4 publications

References 38 publications

Structure and function of biotin-dependent carboxylases

Structure and function of biotin-dependent carboxylases

Biotin biosynthesis, transport and utilization in rhizobia

A Tar aspartate receptor and Rubisco-like protein substitute biotin in the growth of rhizobial strains

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