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Artículos de revistas 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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1

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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3

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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4

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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6

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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7

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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9

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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10

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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11

Angelaccio, Sebastiana. "Extremophilic SHMTs: From Structure to Biotechnology." BioMed Research International 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/851428.

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Recent advances in molecular and structural biology have improved the availability of virtually any biocatalyst in large quantity and have also provided an insight into the detailed structure-function relationships of many of them. These results allowed the rational exploitation of biocatalysts for use in organic synthesis. In this context, extremophilic enzymes are extensively studied for their potential interest for many biotechnological and industrial applications, as they offer increased rates of reactions, higher substrate solubility, and/or longer enzyme half-lives at the conditions of i

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12

NARKEWICZ, Michael R., S. David SAULS, Susan S. TJOA, Cecilia TENG, and Paul V. FENNESSEY. "Evidence for intracellular partitioning of serine and glycine metabolism in Chinese hamster ovary cells." Biochemical Journal 313, no. 3 (1996): 991–96. http://dx.doi.org/10.1042/bj3130991.

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Serine hydroxymethyltransferase (SHMT) is the primary enzyme in the interconversion of serine and glycine. The roles of mitochondrial and cytosolic SHMT in the interconversion of serine and glycine were determined in two Chinese hamster ovary (CHO) cell lines that both contain cytosolic SHMT but either have (CHOm+) or lack (CHOm-) mitochondrial SHMT. Mitochondrial SHMT activity was significantly reduced in CHOm- (0.24±0.11 nmol/min per mg of mitochondrial protein) compared with CHOm+ (3.21±0.66 nmol/min per mg of mitochondrial protein; P = 0.02) cells, whereas cytosolic SHMT activity was simil

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13

Talwar, R., J. R. Jagath, A. Datta, V. Prakash, H. S. Savithri, and N. A. Rao. "The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase." Acta Biochimica Polonica 44, no. 4 (1997): 679–88. http://dx.doi.org/10.18388/abp.1997_4370.

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The active site lysine residue, K256, involved in Schiff's base linkage with pyridoxal-5'-phosphate (PLP) in sheep liver recombinant serine hydroxymethyltransferase (rSHMT) was changed to glutamine or arginine by site-directed mutagenesis. The purified K256Q and K256R SHMTs had less than 0.1% of catalytic activity with serine and H4folate as substrates compared to rSHMT. The mutant enzymes also failed to exhibit the characteristic visible absorbance spectrum (lambda(max) 425 nm) and did not produce the quinonoid intermediate (lambda(max) 495 nm) upon the addition of glycine and H4folate. The m

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14

Korasick, David A., Pramod K. Kandoth, John J. Tanner, Melissa G. Mitchum, and Lesa J. Beamer. "Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode." Journal of Biological Chemistry 295, no. 11 (2020): 3708–18. http://dx.doi.org/10.1074/jbc.ra119.012256.

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Management of the agricultural pathogen soybean cyst nematode (SCN) relies on the use of SCN-resistant soybean cultivars, a strategy that has been failing in recent years. An underutilized source of resistance in the soybean genotype Peking is linked to two polymorphisms in serine hydroxy-methyltransferase 8 (SHMT8). SHMT is a pyridoxal 5′-phosphate–dependent enzyme that converts l-serine and (6S)-tetrahydrofolate to glycine and 5,10-methylenetetrahydrofolate. Here, we determined five crystal structures of the 1884-residue SHMT8 tetramers from the SCN-susceptible cultivar (cv.) Essex and the S

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15

Simic, Petra, Juliane Willuhn, Hermann Sahm, and Lothar Eggeling. "Identification of glyA (Encoding Serine Hydroxymethyltransferase) and Its Use Together with the Exporter ThrE To Increase l-Threonine Accumulation by Corynebacterium glutamicum." Applied and Environmental Microbiology 68, no. 7 (2002): 3321–27. http://dx.doi.org/10.1128/aem.68.7.3321-3327.2002.

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ABSTRACT l-Threonine can be made by the amino acid-producing bacterium Corynebacterium glutamicum. However, in the course of this process, some of the l-threonine is degraded to glycine. We detected an aldole cleavage activity of l-threonine in crude extracts with an activity of 2.2 nmol min−1 (mg of protein)−1. In order to discover the molecular reason for this activity, we cloned glyA, encoding serine hydroxymethyltransferase (SHMT). By using affinity-tagged glyA, SHMT was isolated and its substrate specificity was determined. The aldole cleavage activity of purified SHMT with l-threonine as

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16

Thompson, Henry R., Gayle M. Jones, and Michael R. Narkewicz. "Ontogeny of hepatic enzymes involved in serine- and folate-dependent one-carbon metabolism in rabbits." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 5 (2001): G873—G878. http://dx.doi.org/10.1152/ajpgi.2001.280.5.g873.

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Serine occupies a central position in folate-dependent, one-carbon metabolism through 5,10-methylenetetrahydrofolate (MTHF) and 5-formyltetrahydrofolate (FTHF). We characterized the ontogeny of the specific activity of key enzymes involved in serine, 5,10-MTHF, and 5-FTHF metabolism: methenyltetrahydrofolate synthetase (MTHFS), MTHF reductase (MTHFR), the glycine cleavage system (GCS), methionine synthase (MS), and serine hydroxymethyltransferase (SHMT) in rabbit liver, placenta, brain, and kidney. In liver, MTHFS activity is low in the fetus (0.36 ± 0.07 nmol · min−1 · mg protein−1), peaks at

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17

Stolz, Michael, Petra Peters-Wendisch, Helga Etterich, et al. "Reduced Folate Supply as a Key to Enhanced l-Serine Production by Corynebacterium glutamicum." Applied and Environmental Microbiology 73, no. 3 (2006): 750–55. http://dx.doi.org/10.1128/aem.02208-06.

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ABSTRACT The amino acid l-serine is required for pharmaceutical purposes, and the availability of a sugar-based microbial process for its production is desirable. However, a number of intracellular utilization routes prevent overproduction of l-serine, with the essential serine hydroxymethyltransferase (SHMT) (glyA) probably occupying a key position. We found that constructs of Corynebacterium glutamicum strains where chromosomal glyA expression is dependent on P tac and lacI Q are unstable, acquiring mutations in lacI Q, for instance. To overcome the inconvenient glyA expression control, we i

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18

Liu, Hao, Na Li, Yuan Zhao, Guo-Zhang Kang, Yan-Hong Zhao, and Hua-Wei Xu. "Serine Hydroxymethyltransferase (SHMT) Gene Family in Wheat (Triticum aestivum L.): Identification, Evolution, and Expression Analysis." Agronomy 12, no. 6 (2022): 1346. http://dx.doi.org/10.3390/agronomy12061346.

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Serine hydroxymethyltransferase (SHMT) plays a vital role in one-carbon metabolic, photorespiration, and various stress responses. However, the genome-wide analysis has not been performed in wheat. In this study, a total of 12 TaSHMT genes were identified in wheat and classified into groups Ⅰa, Ⅰb, and Ⅱb. TaSHMT genes in each group shared similar conserved domain distributions. Chromosomal location, synteny, and cis-elements analysis of TaSHMTs were also analyzed. Real-time PCR results indicated that most TaSHMT genes were mainly expressed in leaves and stems during the wheat seedling stage.

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19

McClung, C. R., C. R. Davis, K. M. Page, and S. A. Denome. "Characterization of the formate (for) locus, which encodes the cytosolic serine hydroxymethyltransferase of Neurospora crassa." Molecular and Cellular Biology 12, no. 4 (1992): 1412–21. http://dx.doi.org/10.1128/mcb.12.4.1412-1421.1992.

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Serine hydroxymethyltransferase (SHMT) occupies a central position in one-carbon (C1) metabolism, catalyzing the reaction of serine and tetrahydrofolate to yield glycine and 5,10-methylenetetrahydrofolate. Methylenetetrahydrofolate serves as a donor of C1 units for the synthesis of numerous compounds, including purines, thymidylate, lipids, and methionine. We provide evidence that the formate (for) locus of Neurospora crassa encodes cytosolic SHMT. The for+ gene was localized to a 2.8-kb BglII fragment by complementation (restoration to formate-independent growth) of a strain carrying a recess

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McClung, C. R., C. R. Davis, K. M. Page, and S. A. Denome. "Characterization of the formate (for) locus, which encodes the cytosolic serine hydroxymethyltransferase of Neurospora crassa." Molecular and Cellular Biology 12, no. 4 (1992): 1412–21. http://dx.doi.org/10.1128/mcb.12.4.1412.

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Serine hydroxymethyltransferase (SHMT) occupies a central position in one-carbon (C1) metabolism, catalyzing the reaction of serine and tetrahydrofolate to yield glycine and 5,10-methylenetetrahydrofolate. Methylenetetrahydrofolate serves as a donor of C1 units for the synthesis of numerous compounds, including purines, thymidylate, lipids, and methionine. We provide evidence that the formate (for) locus of Neurospora crassa encodes cytosolic SHMT. The for+ gene was localized to a 2.8-kb BglII fragment by complementation (restoration to formate-independent growth) of a strain carrying a recess

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21

Pai, Vinitha R., V. Rajaram, Shveta Bisht, et al. "Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of Asn341, Tyr60 and Phe351 in tetrahydrofolate binding." Biochemical Journal 418, no. 3 (2009): 635–42. http://dx.doi.org/10.1042/bj20081739.

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SHMT (serine hydoxymethyltransferase), a type I pyridoxal 5′-phosphate-dependent enzyme, catalyses the conversion of L-serine and THF (tetrahydrofolate) into glycine and 5,10-methylene THF. SHMT also catalyses several THF-independent side reactions such as cleavage of β-hydroxy amino acids, transamination, racemization and decarboxylation. In the present study, the residues Asn341, Tyr60 and Phe351, which are likely to influence THF binding, were mutated to alanine, alanine and glycine respectively, to elucidate the role of these residues in THF-dependent and -independent reactions catalysed b

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22

Chaves, A. C. S. D., M. Fernandez, A. L. S. Lerayer, I. Mierau, M. Kleerebezem, and J. Hugenholtz. "Metabolic Engineering of Acetaldehyde Production by Streptococcus thermophilus." Applied and Environmental Microbiology 68, no. 11 (2002): 5656–62. http://dx.doi.org/10.1128/aem.68.11.5656-5662.2002.

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ABSTRACT The process of acetaldehyde formation by the yogurt bacterium Streptococcus thermophilus is described in this paper. Attention was focused on one specific reaction for acetaldehyde formation catalyzed by serine hydroxymethyltransferase (SHMT), encoded by the glyA gene. In S. thermophilus, SHMT also possesses threonine aldolase (TA) activity, the interconversion of threonine into glycine and acetaldehyde. In this work, several wild-type S. thermophilus strains were screened for acetaldehyde production in the presence and absence of l-threonine. Supplementation of the growth medium with

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23

KRISHNA RAO, J. V., Junutula R. JAGATH, Balasubramanya SHARMA, N. APPAJI RAO, and H. S. SAVITHRI. "Asp-89: a critical residue in maintaining the oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase." Biochemical Journal 343, no. 1 (1999): 257–63. http://dx.doi.org/10.1042/bj3430257.

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Aspartate residues function as proton acceptors in catalysis and are involved in ionic interactions stabilizing subunit assembly. In an attempt to unravel the role of a conserved aspartate (D89) in sheep-liver tetrameric serine hydroxymethyltransferase (SHMT), it was converted into aspargine by site-directed mutagenesis. The purified D89N mutant enzyme had a lower specific activity compared with the wild-type enzyme. It was a mixture of dimers and tetramers with the proportion of tetramers increasing with an increase in the pyridoxal-5′-phosphate (PLP) concentration used during purification. T

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24

JALA, Venkatakrishna Rao, Naropantul APPAJI RAO, and Handanahal Subbarao SAVITHRI. "Identification of amino acid residues, essential for maintaining the tetrameric structure of sheep liver cytosolic serine hydroxymethyltransferase, by targeted mutagenesis." Biochemical Journal 369, no. 3 (2003): 469–76. http://dx.doi.org/10.1042/bj20021160.

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Serine hydroxymethyltransferase (SHMT), a pyridoxal 5′-phosphate (PLP)-dependent enzyme, catalyses the transfer of the hydroxymethyl group from serine to tetrahydrofolate to yield glycine and N5,N10-methylenetetrahydrofolate. An analysis of the known SHMT sequences indicated that several amino acid residues were conserved. In this paper, we report the identification of the amino acid residues essential for maintaining the oligomeric structure of sheep liver cytosolic recombinant SHMT (scSHMT) through intra- and inter-subunit interactions and by stabilizing the binding of PLP at the active site

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Wilke, Anne C., Carmen Doebele, Alena Zindel, et al. "SHMT2 inhibition disrupts the TCF3 transcriptional survival program in Burkitt lymphoma." Blood 139, no. 4 (2022): 538–53. http://dx.doi.org/10.1182/blood.2021012081.

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Abstract Burkitt lymphoma (BL) is an aggressive lymphoma type that is currently treated by intensive chemoimmunotherapy. Despite the favorable clinical outcome for most patients with BL, chemotherapy-related toxicity and disease relapse remain major clinical challenges, emphasizing the need for innovative therapies. Using genome-scale CRISPR-Cas9 screens, we identified B-cell receptor (BCR) signaling, specific transcriptional regulators, and one-carbon metabolism as vulnerabilities in BL. We focused on serine hydroxymethyltransferase 2 (SHMT2), a key enzyme in one-carbon metabolism. Inhibition

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Lakhssassi, Naoufal, Dounya Knizia, Abdelhalim El Baze, Aicha Lakhssassi, Jonas Meksem, and Khalid Meksem. "Proteomic, Transcriptomic, Mutational, and Functional Assays Reveal the Involvement of Both THF and PLP Sites at the GmSHMT08 in Resistance to Soybean Cyst Nematode." International Journal of Molecular Sciences 23, no. 19 (2022): 11278. http://dx.doi.org/10.3390/ijms231911278.

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The serine hydroxymethyltransferase (SHMT; E.C. 2.1.2.1) is involved in the interconversion of serine/glycine and tetrahydrofolate (THF)/5,10-methylene THF, playing a key role in one-carbon metabolism, the de novo purine pathway, cellular methylation reactions, redox homeostasis maintenance, and methionine and thymidylate synthesis. GmSHMT08 is the soybean gene underlying soybean cyst nematode (SCN) resistance at the Rhg4 locus. GmSHMT08 protein contains four tetrahydrofolate (THF) cofactor binding sites (L129, L135, F284, N374) and six pyridoxal phosphate (PLP) cofactor binding/catalysis site

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Ernst, Dustin C., and Diana M. Downs. "2-Aminoacrylate Stress Induces a Context-Dependent Glycine Requirement inridAStrains of Salmonella enterica." Journal of Bacteriology 198, no. 3 (2015): 536–43. http://dx.doi.org/10.1128/jb.00804-15.

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ABSTRACTThe reactive enamine 2-aminoacrylate (2AA) is a metabolic stressor capable of damaging cellular components. Members of the broadly conserved Rid (RidA/YER057c/UK114) protein family mitigate 2AA stressin vivoby facilitating enamine and/or imine hydrolysis. Previous work showed that 2AA accumulation inridAstrains ofSalmonella entericaled to the inactivation of multiple target enzymes, including serine hydroxymethyltransferase (GlyA). However, the specific cause of aridAstrain's inability to grow during periods of 2AA stress had yet to be determined. Work presented here shows that glycine

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Heil, Sandra G., Nathalie M. J. Van der Put, Erwin T. Waas, Martin den Heijer, Frans J. M. Trijbels, and Henk J. Blom. "Is Mutated Serine Hydroxymethyltransferase (SHMT) Involved in the Etiology of Neural Tube Defects?" Molecular Genetics and Metabolism 73, no. 2 (2001): 164–72. http://dx.doi.org/10.1006/mgme.2001.3175.

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Devor, Eric J., Rebecca M. Dill-Devor, Harry J. Magee, and Rafiq Waziri. "Serine hydroxymethyltransferase pseudogene, SHMT-ps1: A unique genetic marker of the order primates." Journal of Experimental Zoology 282, no. 1-2 (1998): 150–56. http://dx.doi.org/10.1002/(sici)1097-010x(199809/10)282:1/2<150::aid-jez16>3.0.co;2-y.

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Kronenberger, Thales, Jasmin Lindner, Kamila A. Meissner, et al. "Vitamin B6-Dependent Enzymes in the Human Malaria ParasitePlasmodium falciparum: A Druggable Target?" BioMed Research International 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/108516.

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Malaria is a deadly infectious disease which affects millions of people each year in tropical regions. There is no effective vaccine available and the treatment is based on drugs which are currently facing an emergence of drug resistance and in this sense the search for new drug targets is indispensable. It is well established that vitamin biosynthetic pathways, such as the vitamin B6de novosynthesis present inPlasmodium, are excellent drug targets. The active form of vitamin B6, pyridoxal 5-phosphate, is, besides its antioxidative properties, a cofactor for a variety of essential enzymes pres

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Nikiforov, Mikhail A., Sanjay Chandriani, Brenda O'Connell, et al. "A Functional Screen for Myc-Responsive Genes Reveals Serine Hydroxymethyltransferase, a Major Source of the One-Carbon Unit for Cell Metabolism." Molecular and Cellular Biology 22, no. 16 (2002): 5793–800. http://dx.doi.org/10.1128/mcb.22.16.5793-5800.2002.

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ABSTRACT A cDNA library enriched with Myc-responsive cDNAs but depleted of myc cDNAs was used in a functional screen for growth enhancement in c-myc-null cells. A cDNA clone for mitochondrial serine hydroxymethyltransferase (mSHMT) that was capable of partial complementation of the growth defects of c-myc-null cells was identified. Expression analysis and chromatin immunoprecipitation demonstrated that mSHMT is a direct Myc target gene. Furthermore, a separate gene encoding the cytoplasmic isoform of the same enzyme is also a direct target of Myc regulation. SHMT enzymes are the major source o

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Zhang, Zhi-Bi, Yuan-Ling Xia, Guang-Heng Dong, Yun-Xin Fu, and Shu-Qun Liu. "Exploring the Cold-Adaptation Mechanism of Serine Hydroxymethyltransferase by Comparative Molecular Dynamics Simulations." International Journal of Molecular Sciences 22, no. 4 (2021): 1781. http://dx.doi.org/10.3390/ijms22041781.

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Cold-adapted enzymes feature a lower thermostability and higher catalytic activity compared to their warm-active homologues, which are considered as a consequence of increased flexibility of their molecular structures. The complexity of the (thermo)stability-flexibility-activity relationship makes it difficult to define the strategies and formulate a general theory for enzyme cold adaptation. Here, the psychrophilic serine hydroxymethyltransferase (pSHMT) from Psychromonas ingrahamii and its mesophilic counterpart, mSHMT from Escherichia coli, were subjected to μs-scale multiple-replica molecu

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Scaletti, Emma, Ann‐Sofie Jemth, Thomas Helleday, and Pål Stenmark. "Structural basis of inhibition of the human serine hydroxymethyltransferase SHMT 2 by antifolate drugs." FEBS Letters 593, no. 14 (2019): 1863–73. http://dx.doi.org/10.1002/1873-3468.13455.

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34

Niclot, Sidonie, Quentin Pruvot, Caroline Besson, et al. "Implication of the folate-methionine metabolism pathways in susceptibility to follicular lymphomas." Blood 108, no. 1 (2006): 278–85. http://dx.doi.org/10.1182/blood-2005-04-1567.

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The incidence of follicular lymphoma (FL) in industrialized countries has been increasing since the 1950s. Polymorphisms in genes encoding key enzymes controlling folate-methionine metabolism, including methylenetetrahydrofolate reductase (MTHFR), methionine synthase (MS or MTR), serine hydroxymethyltransferase (SHMT), and thymidylate synthase (TS or TYMS), modify the risk of various cancers and possibly FL. This study specifically looks for an association between MTHFR, MTR, TYMS, and SHMT polymorphisms and the risk of FL. We carried out a case-control study with 172 patients diagnosed with F

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35

LEE, C. S., E. SALCEDO, Q. WANG, P. WANG, P. F. G. SIMS, and J. E. HYDE. "Characterization of three genes encoding enzymes of the folate biosynthetic pathway in Plasmodium falciparum." Parasitology 122, no. 1 (2001): 1–13. http://dx.doi.org/10.1017/s0031182000006946.

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Although the folate metabolic pathway in malaria parasites is a major chemotherapeutic target, resistance to currently available antifolate drugs is an increasing problem. This pathway, however, includes a number of enzymes that, to date, have not been characterized despite their potential for clinical exploitation. As a step towards evaluation of additional targets in this pathway, we report the isolation and characterization of 3 new genes that encode homologues of GTP cyclohydrolase I (GTP-CH), dihydrofolate synthase/folylpolyglutamate synthase (DHFS/FPGS) and serine hydroxymethyltransferas

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36

Bourguignon, J., M. Neuburger, and R. Douce. "Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase." Biochemical Journal 255, no. 1 (1988): 169–78. http://dx.doi.org/10.1042/bj2550169.

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High-molecular-mass proteins from pea (Pisum sativum) mitochondrial matrix retained on an XM-300 Diaflo membrane (‘matrix extract’) exhibited high rates of glycine oxidation in the presence of NAD+ and tetrahydropteroyl-L-glutamic acid (H4 folate) as long as the medium exhibited a low ionic strength. Serine hydroxymethyltransferase (SHMT) (4 x 53 kDa) and the four proteins of the glycine-cleavage system, including a pyridoxal phosphate-containing enzyme (‘P-protein’ 2 x 97 kDa), a carrier protein containing covalently bound lipoic acid (‘H-protein’ 15.5 kDa), a protein exhibiting lipoamide deh

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37

Witschel, Matthias C., Matthias Rottmann, Anatol Schwab, et al. "Inhibitors of Plasmodial Serine Hydroxymethyltransferase (SHMT): Cocrystal Structures of Pyrazolopyrans with Potent Blood- and Liver-Stage Activities." Journal of Medicinal Chemistry 58, no. 7 (2015): 3117–30. http://dx.doi.org/10.1021/jm501987h.

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Palmer, Ashley M., Elena Kamynina, Martha S. Field, and Patrick J. Stover. "Folate rescues vitamin B12 depletion-induced inhibition of nuclear thymidylate biosynthesis and genome instability." Proceedings of the National Academy of Sciences 114, no. 20 (2017): E4095—E4102. http://dx.doi.org/10.1073/pnas.1619582114.

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Clinical vitamin B12 deficiency can result in megaloblastic anemia, which results from the inhibition of DNA synthesis by trapping folate cofactors in the form of 5-methyltetrahydrofolate (5-methylTHF) and subsequent inhibition of de novo thymidylate (dTMP) biosynthesis. In the cytosol, vitamin B12 functions in the remethylation of homocysteine to methionine, which regenerates THF from 5-methylTHF. In the nucleus, THF is required for de novo dTMP biosynthesis, but it is not understood how 5-methylTHF accumulation in the cytosol impairs nuclear dTMP biosynthesis. The impact of vitamin B12 deple

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39

Schwertz, Geoffrey, Michelle S. Frei, Matthias C. Witschel, et al. "Conformational Aspects in the Design of Inhibitors for Serine Hydroxymethyltransferase (SHMT): Biphenyl, Aryl Sulfonamide, and Aryl Sulfone Motifs." Chemistry - A European Journal 23, no. 57 (2017): 14345–57. http://dx.doi.org/10.1002/chem.201703244.

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40

Wińska, Patrycja, Anna Sobiepanek, Katarzyna Pawlak, Monika Staniszewska та Joanna Cieśla. "Phosphorylation of Thymidylate Synthase and Dihydrofolate Reductase in Cancer Cells and the Effect of CK2α Silencing". International Journal of Molecular Sciences 24, № 3 (2023): 3023. http://dx.doi.org/10.3390/ijms24033023.

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Our previous research suggests an important regulatory role of CK2-mediated phosphorylation of enzymes involved in the thymidylate biosynthesis cycle, i.e., thymidylate synthase (TS), dihydrofolate reductase (DHFR), and serine hydroxymethyltransferase (SHMT). The aim of this study was to show whether silencing of the CK2α gene affects TS and DHFR expression in A-549 cells. Additionally, we attempted to identify the endogenous kinases that phosphorylate TS and DHFR in CCRF-CEM and A-549 cells. We used immunodetection, immunofluorescence/confocal analyses, reverse transcription–quantitative poly

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41

Read, Martin, Ingrid B. Müller, Sarah L. Mitchell, Paul FG Sims, and John E. Hyde. "Dynamic subcellular localization of isoforms of the folate pathway enzyme serine hydroxymethyltransferase (SHMT) through the erythrocytic cycle of Plasmodium falciparum." Malaria Journal 9, no. 1 (2010): 351. http://dx.doi.org/10.1186/1475-2875-9-351.

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42

Schwertz, Geoffrey, Matthias C. Witschel, Matthias Rottmann, et al. "Antimalarial Inhibitors Targeting Serine Hydroxymethyltransferase (SHMT) with in Vivo Efficacy and Analysis of their Binding Mode Based on X-ray Cocrystal Structures." Journal of Medicinal Chemistry 60, no. 12 (2017): 4840–60. http://dx.doi.org/10.1021/acs.jmedchem.7b00008.

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43

SCHLÜPEN, Christina, Maria A. SANTOS, Ulrike WEBER, Albert de GRAAF, José L. REVUELTA, and K. Peter STAHMANN. "Disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine in Ashbya gossypii." Biochemical Journal 369, no. 2 (2003): 263–73. http://dx.doi.org/10.1042/bj20021224.

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Riboflavin overproduction in the ascomycete Ashbya gossypii is limited by glycine, a precursor of purine biosynthesis, and therefore an indicator of glycine metabolism. Disruption of the SHM2 gene, encoding a serine hydroxymethyltransferase, resulted in a significant increase in riboflavin productivity. Determination of the enzyme's specific activity revealed a reduction from 3m-units/mg of protein to 0.5m-unit/mg protein. The remaining activity was due to an isoenzyme encoded by SHM1, which is probably mitochondrial. A hypothesis proposed to account for the enhanced riboflavin overproduction

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44

Yuan, Yang, Danyun Xu, Denghao Xiang, Li Jiang, and Honghong Hu. "Serine Hydroxymethyltransferase 1 Is Essential for Primary-Root Growth at Low-Sucrose Conditions." International Journal of Molecular Sciences 23, no. 9 (2022): 4540. http://dx.doi.org/10.3390/ijms23094540.

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Plant roots are essential organs for absorbing nutrients from the soil or medium. Sucrose functions as a vital carbon source in root development, and sucrose starvation interferes with the redox state of plant cells. However, the mechanism of root growth at sucrose starvation remains unclear. Here, we report that SHMT1 (serine hydroxymethyltransferase 1) plays a crucial role in primary-root growth. SHMT1 mutation caused decreased sugar levels, excessive H2O2 accumulation, and severe root-growth arrest at sucrose-free conditions, whereas plants with SHMT1 overexpression had increased sugar and

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45

Beckmann, Katja, Christine Dzuibany, Klaus Biehler, et al. "Photosynthesis and fluorescence quenching, and the mRNA levels of plastidic glutamine synthetase or of mitochondrial serine hydroxymethyltransferase (SHMT) in the leaves of the wild-type and of the SHMT-deficient stm mutant of Arabidopsis thaliana in relation to the rate of photorespiration." Planta 202, no. 3 (1997): 379–86. http://dx.doi.org/10.1007/s004250050140.

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46

Papadopoulou, Anastasia, Panayotis Kaloyannidis, Maria Alvanou, Joanne Kalogeropoulou, Achilles Anagnostopoulos, and Evangelia Yannaki. "An Optimized, Large Scale Generation and Validation of Aspergillus-Specific T Lymphocytes for the Management of Invasive Aspergillosis in Immunocompromised Patients." Blood 126, no. 23 (2015): 4293. http://dx.doi.org/10.1182/blood.v126.23.4293.4293.

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Abstract Invansive aspergillosis (IA) represents a leading cause of morbidity and mortality in patients with hematological malignancies and hematopoietic stem cell (HSC)/solid organ transplant recipients. The limitations of the contemporary antifungal treatment include the lack of efficacy in several cases, the drug-associated toxicity, the emergence of uncommon or drug-resistant molds and the added financial burden in transplant care. Adoptive immunotherapy with Aspergillus-specific T cells (Asp-STs) constitutes an alternative and promising therapeutic approach against IA, however, the comple

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47

Wu, Hao, He Bai, Shigang Duan, and Fangchao Yuan. "Downregulating Serine Hydroxymethyltransferase 2 Deteriorates Hepatic Ischemia-Reperfusion Injury through ROS/JNK/P53 Signaling in Mice." BioMed Research International 2019 (November 18, 2019): 1–9. http://dx.doi.org/10.1155/2019/2712185.

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Background. Serine hydroxymethyltransferase 2 (SHMT2) activity ensures that cells have a survival advantage in ischemic conditions and regulates redox homeostasis. In this study, we aimed to investigate the role of SHMT2 after hepatic ischemia-reperfusion (IR), which involves hypoxia, ischemic conditions, and cell apoptosis. Methods. A 70% IR model was established in C57BL/6J mice with or without SHMT2 knockdown. H&E staining, liver weight/body weight, serum alanine aminotransferase (ALT), and aspartate aminotransferase (AST) levels and cell apoptosis were tested to analyze liver damage an

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48

Mao, Yu, та Tiyong Zhang. "Knockdown of SHMT2 enhances the sensitivity of gastric cancer cells to radiotherapy through the Wnt/β-catenin pathway". Open Life Sciences 17, № 1 (2022): 1249–55. http://dx.doi.org/10.1515/biol-2022-0480.

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Abstract Gastric cancer (GC) is one of the most common malignant tumors. The mechanism of GC radioresistance and new radiosensitizers must be revealed and developed to treat GC. Serine hydroxymethyltransferase 2 (SHMT2) is responsible for encoding the mitochondrial form of the pyridoxal phosphate-dependent enzyme. SHMT2 plays a critical role in several types of cancers, while its possible effect on the radiological resistance in GC is still unclear. In this study, we investigated the role of SHMT2 in the radiological resistance of GC. Our data confirmed that SHMT2 was highly expressed in radia

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Ning, Shanglei, Siquan Ma, Abdul Qahar Saleh, Lingyu Guo, Zixiao Zhao, and Yuxin Chen. "SHMT2 Overexpression Predicts Poor Prognosis in Intrahepatic Cholangiocarcinoma." Gastroenterology Research and Practice 2018 (August 28, 2018): 1–6. http://dx.doi.org/10.1155/2018/4369253.

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Background and Objective. Serine hydroxymethyltransferase 2 (SHMT2) functions as a key enzyme in serine/glycine biosynthesis and one-carbon metabolism. Recent studies have shown that SHMT2 participated in tumor growth and progression in a variety of cancer types. The objective of the present study is to explore the expression of SHMT2 and evaluate its prognostic value in patients with intrahepatic cholangiocarcinoma (iCCA). Patients and Methods. We retrospectively investigated the expression of SHMT2 in 100 primary iCCA samples through immunohistochemical (IHC) staining on a tissue array. Resu

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Cui, Ximao, Yanfen Cui, Tao Du, et al. "SHMT2 Drives the Progression of Colorectal Cancer by Regulating UHRF1 Expression." Canadian Journal of Gastroenterology and Hepatology 2022 (February 15, 2022): 1–14. http://dx.doi.org/10.1155/2022/3758697.

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Introduction. Serine hydroxymethyltransferase 2 (SHMT2) has a critical role in serine-glycine metabolism to drive cancer cell proliferation. Yet, the function of SHMT2 in tumorigenesis, especially in human colorectal cancer (CRC) progression, remains largely unclear. Materials and Methods. CRC and paired normal samples were collected in the Department of Colorectal Surgery, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine, and assessed by real-time polymerase chain reaction (qPCR) analysis, western blot (WB), and immunohistochemistry (IHC). Moreover, SHMT2 expression in human

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