Bibliografías temáticas / Serine Hydroxymethyltransferase (SHMT)

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Literatura académica sobre el tema "Serine Hydroxymethyltransferase (SHMT)"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 7 de septiembre de 2023

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Artículos de revistas sobre el tema "Serine Hydroxymethyltransferase (SHMT)"

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McNeil, J. Bryan, Andrew L. Bognar, and Ronald E. Pearlman. "In Vivo Analysis of Folate Coenzymes and Their Compartmentation in Saccharomyces cerevisiae." Genetics 142, no. 2 (1996): 371–81. http://dx.doi.org/10.1093/genetics/142.2.371.

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Abstract In eukaryotes, enzymes responsible for the interconversion of one-carbon units exist in parallel in both mitochondria and the cytoplasm. Strains of Saccharomyces cerevisiae were constructed that possess combinations of gene disruptions at the SHM1 [mitochondrial serine hydroxymethyltransferase (SHMTm)], SHM2 [cytoplasmic SHMT (SHMTc)], MIS1 [mitochondrial C1-tetrahydrofolate synthase (C1-THFSm)], ADE3 [cytoplasmic C1-THF synthase (C1-THFSc)], GCV1 [glycine cleavage system (GCV) protein T], and the GLY1 (involved in glycine synthesis) loci. Analysis of the in vivo growth characteristic
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2

Zhang, Yi, Kehan Sun, Francisco J. Sandoval, Katherine Santiago, and Sanja Roje. "One-carbon metabolism in plants: characterization of a plastid serine hydroxymethyltransferase." Biochemical Journal 430, no. 1 (2010): 97–105. http://dx.doi.org/10.1042/bj20100566.

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SHMT (serine hydroxymethyltransferase; EC 2.1.2.1) catalyses reversible hydroxymethyl group transfer from serine to H4PteGlun (tetrahydrofolate), yielding glycine and 5,10-methylenetetrahydrofolate. In plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units. Genes encoding putative plastid SHMTs were found in the genomes of various plant species. SHMT activity was detected in chloroplasts in pea (Pisum sativum) and barley (Hordeum vulgare), suggesting that plastid SHMTs exist in all flowering plants.
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Batool, Nayab, Kwan Soo Ko, Akhilesh Kumar Chaurasia, and Kyeong Kyu Kim. "Functional Identification of Serine Hydroxymethyltransferase as a Key Gene Involved in Lysostaphin Resistance and Virulence Potential of Staphylococcus aureus Strains." International Journal of Molecular Sciences 21, no. 23 (2020): 9135. http://dx.doi.org/10.3390/ijms21239135.

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Gaining an insight into the mechanism underlying antimicrobial-resistance development in Staphylococcus aureus is crucial for identifying effective antimicrobials. We isolated S. aureus sequence type 72 from a patient in whom the S. aureus infection was highly resistant to various antibiotics and lysostaphin, but no known resistance mechanisms could explain the mechanism of lysostaphin resistance. Genome-sequencing followed by subtractive and functional genomics revealed that serine hydroxymethyltransferase (glyA or shmT gene) plays a key role in lysostaphin resistance. Serine hydroxymethyltra
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Lin, Zhaosheng, and Richard Sparling. "Investigation of serine hydroxymethyltransferase in methanogens." Canadian Journal of Microbiology 44, no. 7 (1998): 652–56. http://dx.doi.org/10.1139/w98-050.

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The cofactor specificity of serine hydroxymethyltransferase (SHMT) activities was tested in extracts of several methanogens using tetrahydromethanopterin (H4MPt) from Methanobacterium thermoautotrophicum Marburg, tetrahydrosarcinapterin (H4SPt) from Methanosarcina barkeri, and tetrahydrofolate (H4folate) as the potential C1 carrier. In Methanosphaera stadtmanae and Methanococcus thermolithotrophicus, the activities were H4MPt dependent. In Methanospirillum hungatei GP1, Methanosaeta concilii, Methanolobus tindarius, and Methanosarcina barkeri Fusaro, the activities were strictly H4folate depen
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5

Lucas, Stephanie, Guohua Chen, Siddhesh Aras, and Jian Wang. "Serine catabolism is essential to maintain mitochondrial respiration in mammalian cells." Life Science Alliance 1, no. 2 (2018): e201800036. http://dx.doi.org/10.26508/lsa.201800036.

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Breakdown of serine by the enzyme serine hydroxymethyltransferase (SHMT) produces glycine and one-carbon (1C) units. These serine catabolites provide important metabolic intermediates for the synthesis of nucleotides, as well as methyl groups for biosynthetic and regulatory methylation reactions. Recently, it has been shown that serine catabolism is required for efficient cellular respiration. Using CRISPR-Cas9 gene editing, we demonstrate that the mitochondrial SHMT enzyme, SHMT2, is essential to maintain cellular respiration, the main process through which mammalian cells acquire energy. We
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Schneider, Mathew Joseph, Carrie O'connor, Xun Bao, et al. "Abstract 4903: Levels of folate transporters impact the compartmentalization of one-carbon metabolism in the mitochondria vs cytosol providing a unique vulnerability to SHMT inhibition." Cancer Research 83, no. 7_Supplement (2023): 4903. http://dx.doi.org/10.1158/1538-7445.am2023-4903.

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Abstract These studies characterize the critical role of the Reduced Folate Carrier (RFC) and the Proton Coupled Folate Transporter (PCFT) as determinants of cancer cell reliance on mitochondrial vs cytosolic one carbon (C1) metabolism, to identify a unique susceptibility towards SHMT1 and SHMT2 inhibition in cancer cells. C1 metabolism is frequently reprogrammed in cancer cells to provide nucleotides, amino acids, and glutathione, and to maintain redox homeostasis for proliferation. The mitochondrial C1 converting enzymes serine hydroxymethyltransferase (SHMT) 2 and methylene tetrahydrofolate
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Tramonti, Angela, Elisabet Cuyàs, José Antonio Encinar, et al. "Metformin Is a Pyridoxal-5′-Phosphate (PLP)-Competitive Inhibitor of SHMT2." Cancers 13, no. 16 (2021): 4009. http://dx.doi.org/10.3390/cancers13164009.

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The anticancer actions of the biguanide metformin involve the functioning of the serine/glycine one-carbon metabolic network. We report that metformin directly and specifically targets the enzymatic activity of mitochondrial serine hydroxymethyltransferase (SHMT2). In vitro competitive binding assays with human recombinant SHMT1 and SHMT2 isoforms revealed that metformin preferentially inhibits SHMT2 activity by a non-catalytic mechanism. Computational docking coupled with molecular dynamics simulation predicted that metformin could occupy the cofactor pyridoxal-5′-phosphate (PLP) cavity and d
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8

Liu, Zesheng, Xuejuan Pan, Chunlei Wang, et al. "Genome-wide identification and expression analysis of serine hydroxymethyltransferase (SHMT) gene family in tomato (Solanum lycopersicum)." PeerJ 10 (February 10, 2022): e12943. http://dx.doi.org/10.7717/peerj.12943.

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Serine hydroxymethyltransferase (SHMT) is one of the most important enzyme families in one-carbon metabolic pathway and photorespiration within plant cells. Recently studies reported the active roles of plant SHMTs in defending abiotic stresses. However, genome-scale analysis of SHMT in tomato is currently unknown. In this study, seven SHMT genes were identified in the tomato genome using a genome-wide search approach. In addition, their physicochemical properties, protein secondary structure, subcellular localization, gene structure, conserved motifs, phylogenetic and collinear relationships
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Chitnumsub, Penchit, Aritsara Jaruwat, Pinpunya Riangrungroj, et al. "Structures ofPlasmodium vivaxserine hydroxymethyltransferase: implications for ligand-binding specificity and functional control." Acta Crystallographica Section D Biological Crystallography 70, no. 12 (2014): 3177–86. http://dx.doi.org/10.1107/s1399004714023128.

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Plasmodiumparasites, the causative agent of malaria, rely heavily onde novofolate biosynthesis, and the enzymes in this pathway have therefore been explored extensively for antimalarial development. Serine hydroxymethyltransferase (SHMT) fromPlasmodiumspp., an enzyme involved in folate recycling and dTMP synthesis, has been shown to catalyze the conversion of L- and D-serine to glycine (Gly) in a THF-dependent reaction, the mechanism of which is not yet fully understood. Here, the crystal structures ofP. vivaxSHMT (PvSHMT) in a binary complex with L-serine and in a ternary complex with D-serin
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Rebeille, F., M. Neuburger, and R. Douce. "Interaction between glycine decarboxylase, serine hydroxymethyltransferase and tetrahydrofolate polyglutamates in pea leaf mitochondria." Biochemical Journal 302, no. 1 (1994): 223–28. http://dx.doi.org/10.1042/bj3020223.

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The aim of the present work was to further determine how the T-protein of the glycine-cleavage system and serine hydroxy-methyltransferase (SHMT), two folate-dependent enzymes from pea leaf mitochondria, interact through a common pool of tetrahydrofolate polyglutamates (H4PteGlun). It was observed that the binding affinity of tetrahydrofolate polyglutamates for these proteins continuously increased with increasing number of glutamates up to six residues. It was also established that, once bound to the proteins, tetrahydrofolate, a very O2-sensitive molecule, was protected from oxidative degrad
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Tesis sobre el tema "Serine Hydroxymethyltransferase (SHMT)"

1

Bhaskar, B. "Interactions At The Active Site Of Serine Hydroxymethyltransferases." Thesis, 1995. https://etd.iisc.ac.in/handle/2005/1858.

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Bhaskar, B. "Interactions At The Active Site Of Serine Hydroxymethyltransferases." Thesis, 1995. http://etd.iisc.ernet.in/handle/2005/1858.

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FIASCARELLI, ALESSIO. "Serine, Glycine, One-carbon (SGOC) Metabolism and Cancer: Characterization and Inhibition of Serine Hydroxymethyltransferase." Doctoral thesis, 2015. http://hdl.handle.net/11573/857186.

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GUIDUCCI, GIULIA. "Beyond intermediary metabolism: characterization of the moonlighting nucleic acid binding function of human serine hydroxymethyltransferase." Doctoral thesis, 2019. http://hdl.handle.net/11573/1342046.

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The present thesis aims to dissect the moonlighting nucleic acid binding activity of human cytosolic serine hydroxymethyltransferase (SHMT1), a double-faced metabolic enzyme. Indeed, the work characterizes the interaction between SHMT1 and RNA molecules in vitro as well as in cell models, thus unraveling an unexpected complex mechanism in which the synergy among SHMT1, RNA and metabolites fine tunes the compartmentalization of serine metabolism in lung cancer cells. On the other hand, the study of the SHMT1-DNA complexes, presented herein, set the basis to hypothesize a nuclear function of the
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5

Rajaram, V. "Structural Studies On Three Pyridoxal-5'-Phosphate Dependent Enzymes : N-Acetylornithine Aminotransferase, Serine Hydroxymethyltransferase And Diaminopropionate Ammonia Lyase." Thesis, 2007. https://etd.iisc.ac.in/handle/2005/606.

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Pyridoxal 5’-phosphate (PLP), the active form of vitamin B6, is a cofactor for many enzymes involved in the metabolism of amino acids, amino acid derived metabolites and some amino sugars. PLP is one of the most versatile cofactors and the PLP-dependent enzymes catalyze a variety of reactions including transamination, decarboxylation, inter-conversion of L-and D-amino acids and removal or replacement of chemical groups bound at β or γ carbon of amino acids. The thesis describes the structural studies carried out on three PLP-dependent enzymes; N-acetylornithine aminotransferase (AcOAT), ser
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Rajaram, V. "Structural Studies On Three Pyridoxal-5'-Phosphate Dependent Enzymes : N-Acetylornithine Aminotransferase, Serine Hydroxymethyltransferase And Diaminopropionate Ammonia Lyase." Thesis, 2007. http://hdl.handle.net/2005/606.

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Pyridoxal 5’-phosphate (PLP), the active form of vitamin B6, is a cofactor for many enzymes involved in the metabolism of amino acids, amino acid derived metabolites and some amino sugars. PLP is one of the most versatile cofactors and the PLP-dependent enzymes catalyze a variety of reactions including transamination, decarboxylation, inter-conversion of L-and D-amino acids and removal or replacement of chemical groups bound at β or γ carbon of amino acids. The thesis describes the structural studies carried out on three PLP-dependent enzymes; N-acetylornithine aminotransferase (AcOAT), seri
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Actas de conferencias sobre el tema "Serine Hydroxymethyltransferase (SHMT)"

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Woo, Chern Chiuh, Way Cherng Chen, and Teck Hock Philip Lee. "Abstract 1060: Targeting serine hydroxymethyltransferase 2 (SHMT2) suppresses hepatocarcinoma." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1060.

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Nayeen, Md Junayed, Khushbu Shah, Aleem Gangjee, Aamod Dekhne, Zhanjun Hou, and Larry H. Matherly. "Abstract 1656: First-in-class, fluorinated folate receptor specific agents that target tumor cells via inhibition of serine hydroxymethyltransferase 2 (SHMT2) and 5-aminoimidazole-4-carboxamide formyltransferase (AICARFTase)." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1656.

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