Relevant bibliographies by topics / Sulfur insertase

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  2. Dissertations / Theses

Academic literature on the topic 'Sulfur insertase'

Author: Grafiati
Published: 25 May 2024
Last updated: 31 July 2025

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Journal articles on the topic "Sulfur insertase"

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Fellner, Matthias, Benoît Desguin, Robert P. Hausinger, and Jian Hu. "Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE." Proceedings of the National Academy of Sciences 114, no. 34 (2017): 9074–79. http://dx.doi.org/10.1073/pnas.1704967114.

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The lar operon in Lactobacillus plantarum encodes five Lar proteins (LarA/B/C/D/E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. Previous studies have established that two molecules of LarE catalyze successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. However, the catalytic mechanism of this very unusual sulfur-sacrificing reaction remains elusive. In this work, we present the crystal structures of LarE in ligand-free and several ligand-bound form
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Fellner, Matthias, Joel A. Rankin, Benoît Desguin, Jian Hu, and Robert P. Hausinger. "Analysis of the Active Site Cysteine Residue of the Sacrificial Sulfur Insertase LarE from Lactobacillus plantarum." Biochemistry 57, no. 38 (2018): 5513–23. http://dx.doi.org/10.1021/acs.biochem.8b00601.

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Leimkühler, Silke, and Werner Klipp. "Role of XDHC in Molybdenum Cofactor Insertion into Xanthine Dehydrogenase of Rhodobacter capsulatus." Journal of Bacteriology 181, no. 9 (1999): 2745–51. http://dx.doi.org/10.1128/jb.181.9.2745-2751.1999.

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ABSTRACT Rhodobacter capsulatus xanthine dehydrogenase (XDH) is composed of two subunits, XDHA and XDHB. Immediately downstream ofxdhB, a third gene was identified, designatedxdhC, which is cotranscribed with xdhAB. Interposon mutagenesis revealed that the xdhC gene product is required for XDH activity. However, XDHC is not a subunit of active XDH, which forms an α2β2 heterotetramer inR. capsulatus. It was shown that XDHC neither is a transcriptional regulator for xdh gene expression nor influences XDH stability. To analyze the function of XDHC for XDH inR. capsulatus, inactive XDH was purifie
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Wunsch, Patrick, Margitta Herb, Hagen Wieland, Ulrike M. Schiek, and Walter G. Zumft. "Requirements for CuA and Cu-S Center Assembly of Nitrous Oxide Reductase Deduced from Complete Periplasmic Enzyme Maturation in the Nondenitrifier Pseudomonas putida." Journal of Bacteriology 185, no. 3 (2003): 887–96. http://dx.doi.org/10.1128/jb.185.3.887-896.2003.

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ABSTRACT Bacterial nitrous oxide (N2O) reductase is the terminal oxidoreductase of a respiratory process that generates dinitrogen from N2O. To attain its functional state, the enzyme is subjected to a maturation process which involves the protein-driven synthesis of a unique copper-sulfur cluster and metallation of the binuclear CuA site in the periplasm. There are seven putative maturation factors, encoded by nosA, nosD, nosF, nosY, nosL, nosX, and sco. We wanted to determine the indispensable proteins by expressing nos genes from Pseudomonas stutzeri in the nondenitrifying organism Pseudomo
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Rudenko, Tatyana S., Sergey V. Tarlachkov, Nikolay D. Shatskiy, and Margarita Yu Grabovich. "Comparative Genomics of Beggiatoa leptomitoformis Strains D-401 and D-402T with Contrasting Physiology But Extremely High Level of Genomic Identity." Microorganisms 8, no. 6 (2020): 928. http://dx.doi.org/10.3390/microorganisms8060928.

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Representatives of filamentous colorless sulfur-oxidizing bacteria often dominate in sulfide biotopes, preventing the diffusion of toxic sulfide into the water column. One of the most intriguing groups is a recently described Beggiatoa leptomitoformis including strains D-401 and D-402T. Both strains have identical genes encoding enzymes which are involved in the oxidation of hydrogen sulfide and thiosulfate. Surprisingly, the B. leptomitoformis strain D-401 is not capable to grow lithotrophically in the presence of reduced sulfur compounds and to accumulate elemental sulfur inside the cells, i
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Ye, Ke-Yin, Markus Bursch, Zheng-Wang Qu, et al. "Reversible formylborane/SO2coupling at a frustrated Lewis pair framework." Chemical Communications 53, no. 3 (2017): 633–35. http://dx.doi.org/10.1039/c6cc07071j.

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Paietta, J. V., R. A. Akins, A. M. Lambowitz, and G. A. Marzluf. "Molecular cloning and characterization of the cys-3 regulatory gene of Neurospora crassa." Molecular and Cellular Biology 7, no. 7 (1987): 2506–11. http://dx.doi.org/10.1128/mcb.7.7.2506.

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The regulatory gene cys-3+ controls the synthesis of a number of enzymes involved in sulfur metabolism. cys-3 mutants show a multiple loss of enzymes in different pathways of sulfur metabolism. The cys-3+ gene was isolated by transformation of an aro-9 qa-2 cys-3 inl strain with a clone bank followed by screening with the "sib selection" method. The library used (pRAL1) contained inserts of Sau3a partial digest fragments of about 9 kilobases as well as the Neurospora qa-2+ gene. Double selection for qa-2+ and cys-3+ function was carried out. The transformants obtained with the isolated cys-3+
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8

Timina, Olga, Oleg Timin, and Anna Stepanova. "Some biochemical characteristics of the hairy roots of Pisum sativum L. mutants." Ecological genetics 21, no. 3S (2023): 40. http://dx.doi.org/10.17816/ecogen568310.

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Two high-protein root cultures of vegetable pea mutants were received [1]. In continuation a PCR analysis of the obtained root cultures genes was carried out according [2] and the amino acid composition of the cultures protein was clarified in a dry product on the AAA 339TM device [3]. Obtained results confirmed the absence of rhizobia contamination of the cultures, which grow steadily on a hormone-free media for 5 years. PCR analysis revealed that fourrolgenesA,B,C,Dwere inserted into the genome of the root culture with genotypeafaftltl, and two —rol Candrol D— in the genome of the root cultu
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Pinto, Rachel, Joseph S. Harrison, Tsungda Hsu, William R. Jacobs, and Thomas S. Leyh. "Sulfite Reduction in Mycobacteria." Journal of Bacteriology 189, no. 18 (2007): 6714–22. http://dx.doi.org/10.1128/jb.00487-07.

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ABSTRACT Mycobacterium tuberculosis places an enormous burden on the welfare of humanity. Its ability to grow and its pathogenicity are linked to sulfur metabolism, which is considered a fertile area for the development of antibiotics, particularly because many of the sulfur acquisition steps in the bacterium are not found in the host. Sulfite reduction is one such mycobacterium-specific step and is the central focus of this paper. Sulfite reduction in Mycobacterium smegmatis was investigated using a combination of deletion mutagenesis, metabolite screening, complementation, and enzymology. Th
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Douglas, Paul, Marco Kriek, Penny Bryant, and Peter L. Roach. "Lipoyl Synthase Inserts Sulfur Atoms into an Octanoyl Substrate in a Stepwise Manner." Angewandte Chemie 118, no. 31 (2006): 5321–23. http://dx.doi.org/10.1002/ange.200601910.

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Dissertations / Theses on the topic "Sulfur insertase"

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Zecchin, Paolo. "Mobilisation et incorporation enzymatique du soufre lors de réactions non-redox impliquant un centre [4Fe-4S] : étude biochimique et structurale d’une cystéine désulfidase et d’une sulfurtransférase." Electronic Thesis or Diss., Sorbonne université, 2023. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2023SORUS667.pdf.

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Les composés soufrés, tels que la cystéine et certains cofacteurs, jouent un rôle essentiel dans les processus cellulaires. Cette thèse se concentre sur deux enzymes dépendantes d’un centre [4Fe-4S], impliquées dans le métabolisme du soufre chez l'archée anaérobie Methanococcus maripaludis : MmCyuA, une L-cystéine désulfidase, et MmLarE, une sulfurtransférase dépendante de l'ATP. La première partie porte sur MmCyuA, qui catalyse la conversion de la L-cystéine en sulfure d’hydrogène et 2-aminoacrylate, ultérieurement transformé en pyruvate et ammoniac. Les structures cristallographiques de MmCy
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