Identification of residues essential for a two-step reaction by malonyl-CoA synthetase from Rhizobium trifolii

An, Jee Hyun; Lee, Gha Young; Jung, Jin; Lee, Weontae; Kim, Yu Sam

doi:10.1042/bj3440159

Cited by 18 publications

(4 citation statements)

References 28 publications

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“…trifolii, which is symbiotic with clover [5]. The matA, matB, and matC genes encode malonyl-CoA decarboxylase, malonyl-CoA synthetase, and a putative malonate transporter, respectively [6,7]. These results suggested that these enzymes are involved in the uptake and conversion of malonate to acetyl-CoA in bacteroids.…”

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confidence: 99%

Identification and characterization of a novel transcriptional regulator, MatR, for malonate metabolism in Rhizobium leguminosarum bv. trifolii

Lee

Kim

2000

European Journal of Biochemistry

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A novel gene, matR, located upstream of matABC, transcribed in the opposite direction, and encoding a putative regulatory protein by sequence analysis was discovered from Rhizobium leguminosarum bv. trifolii. The matA, matB, and matC genes encode malonyl-CoA decarboxylase, malonyl-CoA synthetase, and a presumed malonate transporter, respectively. Together, these enzymes catalyze the uptake and conversion of malonate to acetyl-CoA. The deduced amino-acid sequence of matR showed sequence similarity with GntR from Bacillus subtilis in the N-terminal region encoding a helix-turn-helix domain. Electrophoretic mobility shift assay indicated that MatR bound to a fragment of DNA corresponding to the mat promoter region. The addition of malonate or methylmalonate increased the association of MatR and DNA fragment. DNase I footprinting assays identified a MatR binding site encompassing 66 nucleotides near the mat promoter. The mat operator region included an inverted repeat (TCTTGTA/TACACGA) centered -46.5 relative to the transcription start site. Transcriptional assays, using the luciferase gene, revealed that MatR represses transcription from the mat promoter and malonate alleviates MatR-mediated repression effect on the expression of Pmat-luc+ reporter fusion.

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confidence: 99%

Identification and characterization of a novel transcriptional regulator, MatR, for malonate metabolism in Rhizobium leguminosarum bv. trifolii

Lee

Kim

2000

European Journal of Biochemistry

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“…The combination of DLS and MALS can greatly improve the overall characterization of the samples. The Rg/Rh ratio and the slope of the conformation plot (log(Rg)/log(Mw)) provide an indication of the shape and density of the analytes, which can improve the knowledge of the protein structure-function relationship [65][66][67].…”

Section: Applications 21 Protein Analysismentioning

confidence: 99%

Field-Flow Fractionation in Molecular Biology and Biotechnology

Giordani,

Marassi,

Placci

et al. 2023

Molecules

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Field-flow fractionation (FFF) is a family of single-phase separative techniques exploited to gently separate and characterize nano- and microsystems in suspension. These techniques cover an extremely wide dynamic range and are able to separate analytes in an interval between a few nm to 100 µm size-wise (over 15 orders of magnitude mass-wise). They are flexible in terms of mobile phase and can separate the analytes in native conditions, preserving their original structures/properties as much as possible. Molecular biology is the branch of biology that studies the molecular basis of biological activity, while biotechnology deals with the technological applications of biology. The areas where biotechnologies are required include industrial, agri-food, environmental, and pharmaceutical. Many species of biological interest belong to the operational range of FFF techniques, and their application to the analysis of such samples has steadily grown in the last 30 years. This work aims to summarize the main features, milestones, and results provided by the application of FFF in the field of molecular biology and biotechnology, with a focus on the years from 2000 to 2022. After a theoretical background overview of FFF and its methodologies, the results are reported based on the nature of the samples analyzed.

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“…In the second step, free electrons of the sulfur group of the acyl acceptor coenzyme A causes a nucleophilic attack on the carbon atom of the carboxyl group, thereby AMP is released and a thioester is formed. There are several AAEs that allow the activation of various substrates like acetate and fatty acids of different length (Watkins 1997), benzoic acid derivatives (Chang et al 1997), cinnamic acid derivatives (Ehlting et al 1999) or citrate, malate and malonate (An et al 1999). In most cases, the acyl moiety is transferred to coenzyme A, but other acceptors are also described, for example, amino acids or molecular oxygen (Conti et al 1996;Staswick and Tiryaki 2004).…”

Section: Electronic Supplementary Materialsmentioning

confidence: 99%

Phenolic metabolism in the hornwort Anthoceros agrestis: 4-coumarate CoA ligase and 4-hydroxybenzoate CoA ligase

Wohl

Petersen

2020

Plant Cell Rep

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Key message 4-Coumarate coenzyme A ligase and 4-hydroxybenzoate coenzyme A ligase from the hornwort Anthoceros agrestis expressed in E. coli were characterized on biochemical and molecular levels and showed interesting substrate specificities. Abstract Acyl-activating enzymes are associated with the biosynthesis or degradation of various metabolic products such as lipids, amino acids, sugars, and natural compounds. In this work, cDNA sequences encoding 4-coumarate coenzyme A ligase (4CL) and 4-hydroxybenzoate coenzyme A ligase (4HBCL) were amplified from the hornwort Anthoceros agrestis. The coding sequences were expressed in E. coli and purified by Ni-chelate chromatography. The CoA ligases exhibited different substrate specificities. 4CL catalyzed the activation of 4-coumaric acid, 3-coumaric acid, 2-coumaric acid, caffeic acid, isoferulic acid, ferulic acid, and cinnamic acid but lacked activities towards sinapic acid and benzoic acids. In contrast, 4HBCL preferred 4-hydroxybenzoic acid and benzoic acid, but also accepted other benzoic acid derivatives except salicylic acid and 3-aminosalicylic acid. Furthermore, 4HBCL also activated isoferulic acid, cinnamic acid, 2-coumaric acid, 3-coumaric acid, 4-coumaric acid and caffeic acid, but lacked affinity for ferulic acid and sinapic acid. These substrate specificities could be related to the phenolic compounds identified in Anthoceros agrestis.

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Identification of residues essential for a two-step reaction by malonyl-CoA synthetase from Rhizobium trifolii

Cited by 18 publications

References 28 publications

Identification and characterization of a novel transcriptional regulator, MatR, for malonate metabolism in Rhizobium leguminosarum bv. trifolii

Identification and characterization of a novel transcriptional regulator, MatR, for malonate metabolism in Rhizobium leguminosarum bv. trifolii

Field-Flow Fractionation in Molecular Biology and Biotechnology

Phenolic metabolism in the hornwort Anthoceros agrestis: 4-coumarate CoA ligase and 4-hydroxybenzoate CoA ligase

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