Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node

Hubrich, Florian; Müller, Michael; Andexer, Jennifer N.

doi:10.1039/d0cc08078k

Cited by 20 publications

(16 citation statements)

References 146 publications

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“…Notably, strain BOVIS40 harbors the siderophore gene u. Siderophore catecholate found in the bacterial genome has been recognized to play an important role in bacterial adherence to the receptor surfaces, iron chelation and transport (Pedraza et al 2010). Conversely, other related genes such as entABCDEFGHS and fepABCDG are involved in siderophore production and transport that function in the conversion process of chorismate into enterobactin that was not detected in this study have been documented (Tortora et al 2011;Hubrich et al 2021).…”

Section: Discussionmentioning

confidence: 54%

Genomic assessment of Stenotrophomonas indicatrix for improved sunflower plant

Adeleke

Babalola

2021

Curr Genet

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Plant growth-promotion screening and genome analysis of Stenotrophomonas indicatrix BOVIS40 were presented in this study. The genomic information reveals various genes underlining plant growth promotion and resistance to environmental stressors. The genome of S. indicatrix BOVIS40 harbors genes involved in the degradation and biotransformation of organic molecules. Also, other genes involved in bio lm production, chemotaxis, and agellation that facilitate bacterial colonization in the root endosphere and phytohormone genes that modulate root development and stress response in plants were detected in strain BOVIS40. IAA activity of the bacterial strain may be a factor responsible for root formation. Nevertheless, the results highlighted here provide insights into the genomic functions of S. indicatrix and which can be explored in agricultural management. Hence, a measurable approach to the S. indicatrix lifestyle can strategically provide several opportunities in their use as bioinoculants in developing environmentally friendly agriculture sustainably.

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Section: Discussionmentioning

confidence: 54%

Genomic assessment of Stenotrophomonas indicatrix for improved sunflower plant

Adeleke

Babalola

2021

Curr Genet

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“…A radical proposition would be that this water, polarized by the charged residues in its environment, is in fact the entity that initiates a nucleophilic attack on the methyl group of SAM. Two main arguments against this idea are, first, that the other transfer step would still be needed to ligate the methyl group to the recipient (this would make the reaction mechanism, strictly speaking, something other than SN2), and, second, that water as a nucleophile has been implicated in hydrolase and lyase/isomerase reactions but is relatively uncommon in transferases ([ 68 , 69 ], but see [ 70 ]). Perhaps a more realistic possibility is that this water is needed to protonate the leaving group, i.e., S -adenosylhomocysteine.…”

Section: Resultsmentioning

confidence: 99%

Methyltransferases of Riboviria

Mushegian

2022

Biomolecules

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Many viruses from the realm Riboviria infecting eukaryotic hosts encode protein domains with sequence similarity to S-adenosylmethionine-dependent methyltransferases. These protein domains are thought to be involved in methylation of the 5′-terminal cap structures in virus mRNAs. Some methyltransferase-like domains of Riboviria are homologous to the widespread cellular FtsJ/RrmJ-like methyltransferases involved in modification of cellular RNAs; other methyltransferases, found in a subset of positive-strand RNA viruses, have been assigned to a separate “Sindbis-like” family; and coronavirus-specific Nsp13/14-like methyltransferases appeared to be different from both those classes. The representative structures of proteins from all three groups belong to a specific variety of the Rossmann fold with a seven-stranded β-sheet, but it was unclear whether this structural similarity extends to the level of conserved sequence signatures. Here I survey methyltransferases in Riboviria and derive a joint sequence alignment model that covers all groups of virus methyltransferases and subsumes the previously defined conserved sequence motifs. Analysis of the spatial structures indicates that two highly conserved residues, a lysine and an aspartate, frequently contact a water molecule, which is located in the enzyme active center next to the methyl group of S-adenosylmethionine cofactor and could play a key role in the catalytic mechanism of the enzyme. Phylogenetic evidence indicates a likely origin of all methyltransferases of Riboviria from cellular RrmJ-like enzymes and their rapid divergence with infrequent horizontal transfer between distantly related viruses.

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“…The metabolite chorismate, which results from the shikimate biosynthetic pathway, represents a central branching point and, as such, is the precursor of numerous aromatic natural products as well as some nonaromatic secondary metabolites in microorganisms and plants. [1] Thus, in anaerobic and Gram-positive bacteria, the biosynthesis of the electron carrier menaquinone begins with the conversion of chorismate into isochorismate (1). Subsequently, the thiamine diphosphate (ThDP)-dependent enzyme (1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxycyclohex-3-ene-1-carboxylate (SEPHCHC)-synthase MenD catalyzes the Stetter reaction (1,4-addition) of α-ketoglutarate (2) and isochorismate (1) into SEPHCHC (3) (Scheme 1).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biosynthesis of Menaquinone in E. coli: Identification of an Elusive Isomer of SEPHCHC

et al. 2022

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In the biosynthesis of menaquinone in bacteria, the thiamine diphosphate‐dependent enzyme MenD catalyzes the decarboxylative carboligation of α‐ketoglutarate and isochorismate to (1R,2S,5S,6S)‐2‐succinyl‐5‐enolpyruvyl‐6‐hydroxycyclohex‐3‐ene‐1‐carboxylate (SEPHCHC). The regioisomer of SEPHCHC, namely (1R,5S,6S)‐2‐succinyl‐5‐enolpyruvyl‐6‐hydroxycyclohex‐2‐ene‐1‐carboxylate (iso‐SEPHCHC), has been considered as a possible product, however, its existence has been doubtful due to a spontaneous elimination of pyruvate from SEPHCHC to 2‐succinyl‐6‐hydroxy‐2,4‐cyclohexadiene‐1‐carboxylate (SHCHC). In this work, the regioisomer iso‐SEPHCHC was distinguished from SEPHCHC by liquid chromatography‐tandem mass spectrometry. Iso‐SEPHCHC was purified and identified by NMR spectroscopy. Just as SEPHCHC remained hidden as a MenD product for more than two decades, its regioisomer iso‐SEPHCHC has remained until now.

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Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node

Abstract: The interplay between (iso)chorismate, chorismate-converting enzymes, and further influencing factors is a prime example for the dynamics of enzyme catalysis.

Cited by 20 publications

References 146 publications

Genomic assessment of Stenotrophomonas indicatrix for improved sunflower plant

Genomic assessment of Stenotrophomonas indicatrix for improved sunflower plant

Methyltransferases of Riboviria

Biosynthesis of Menaquinone in E. coli: Identification of an Elusive Isomer of SEPHCHC

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