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evolution
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serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
evolution
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serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
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the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
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the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
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the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes
evolution
the enzyme belongs to the fold type-I superfamily of PLP-dependent enzymes
evolution
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SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
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evolution
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SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
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evolution
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the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes
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evolution
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SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
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evolution
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SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
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evolution
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SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
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evolution
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SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
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malfunction
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Shmt1 null mice are fertile and do not demonstrate maternal lethality
malfunction
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a shm1 null mutant requires CO2-enriched air to inhibit photorespiration, while a shm2 null mutant does not show any visible impairment, a double-null mutant cannot survive in CO2-enriched air. Residual SHM activity is undetectably low in purified leaf mesophyll mitochondria of the shm1 mutant. In roots, the knockout of SHM1 does not reduce total SHM activity, whereas the knockout of SHM2 significantly lowers total SHM activity
malfunction
overexpression of mitochondrial serine hydroxymethyltransferase assures an adequate supply of glycine to rapidly proliferating cancer cells, silencing of mitochondrial serine hydroxymethyltransferase halts cancer cell proliferation and supplementation with sarcosine (a glycine-related metabolite) or formate (a source of one carbon units) fails to rescue cell proliferation
malfunction
suppression of SHMT2 decreases both net serine consumption and glycine production in LN229 cells and completely prevents glycine cleavage activity in isolated mitochondria. The preemptive knockdown of SHMT2 protects BT145, LN229, and U251 cells against the detrimental effects of GLDC knockdown
malfunction
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a shm1mutant has chlorotic lesions and a considerably smaller, lethal phenotype under natural ambient CO2 concentrations, but can be restored to wild type with normal growth under elevated CO2 levels (0.5% CO2), showing a typical photorespiratory phenotype
malfunction
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digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal
malfunction
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digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal
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metabolism
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SHMT1 is a rate-limiting enzyme in de novo thymidylate biosynthesis
metabolism
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the enzyme regulates the partitioning of 5,10-methylenetetrahydrofolate between the thymidylate and homocysteine remethylation pathways, mitochondrial SHMT-derived one-carbon units are essential for folate-mediated one-carbon metabolism in the cytoplasm
metabolism
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the de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation, SHMT1 scaffold function can determine de novo thymidylate synthesis capacity, SHMT1 interaction with TYMS and DHFR is DNA-dependent, but the formation of thymidylate biosynthesis complex is nucleotide-independent. Folate-mediated one-carbon metabolism in the cytoplasm and nucleus, overview
metabolism
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the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes
metabolism
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the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes
metabolism
the enzyme plays an essential role in one-carbon unit metabolism
metabolism
key role for serine and glycine metabolism in the survival of brain cancer cells within the ischemic zones of gliomas. Glycine decarboxylase inhibition impairs cells with high SHMT2 levels as the excess glycine not metabolized by glycine decarboxylase can be converted to the toxic molecules aminoacetone and methylglyoxal. SHMT2 activity limits that of pyruvate kinase (PKM2) and reduces oxygen consumption, eliciting a metabolic state that confers a profound survival advantage to cells in poorly vascularized tumor regions
metabolism
the enzyme is involved in folate recycling and dTMP synthesis
metabolism
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the mitochondrial isoform SHMT2 is a crucial factor in the serine/glycine metabolism in several cancer cell types. Correlation of expression level of SHMT2 and other clinicopathological parameters in clinical breast cancer, overview
metabolism
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Shm2 is a key enzyme at the crossing point between purine, methionine and folate metabolism
metabolism
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Shm2 is a key enzyme at the crossing point between purine, methionine and folate metabolism
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metabolism
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the enzyme plays an essential role in one-carbon unit metabolism
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physiological function
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cytoplasmic serine hydroxymethyltransferase regulates the metabolic partitioning of methylenetetrahydrofolate but is not essential in mice
physiological function
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the mitochondrial SHMT is required for photorespiration
physiological function
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the UV-induced increase in SHMT1 translation is accompanied by an increase in the small ubiquitin-like modifier-dependent nuclear localization of the de novo thymidylate biosynthesis pathway and a decrease in DNA strand breaks, suggesting that SHMT1 plays a role in DNA repair
physiological function
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functional redundancy of SHMT2alpha and SHMT1 in nuclear de novo thymidylate synthesis. The de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation. SHMT expression is rate-limiting for de novo thymidylate synthesis
physiological function
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in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
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in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
salt-induced ApSHMT increases the level of glycine betaine via L-serine and choline and confers tolerance to salinity stress
physiological function
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serine hydroxymethyltransferases are important enzymes of cellular one-carbon metabolism and are essential for the photorespiratory glycine-into-serine conversion in leaf mesophyll mitochondria. SHM1 is the photorespiratory isozyme. Due to exclusion of SHM2 from the photorespiratory environment of mesophyll mitochondria, SHM2 cannot substitute for SHM1 in photorespiratory metabolism. SHM1 and SHM2 operate in a redundant manner in one-carbon metabolism of nonphotorespiring cells with a high demand of one-carbon units, e.g. during lignification of vascular cells, detailed overview
physiological function
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the enzyme is essential for the acquisition of one-carbon units for subsequent transfer reactions
physiological function
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the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes, e.g. as a primary source of the one carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate, which serves as a storage form of reduced folates and one-carbon groups in cells in a dormant stage
physiological function
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the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes, e.g. as a primary source of the one carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate,which serves as a storage formof reduced folates and onecarbon groups in cells in a dormant stage
physiological function
mitochondrial serine hydroxymethyltransferase seems to be fundamental to sustain cancer metabolism since production of glycine fuels heme biosynthesis and therefore oxidative phosphorylation. Respiration of cancer cells may then ultimately rely on endogenous glycine synthesis by mitochondrial serine hydroxymethyltransferase. The link between mitochondrial serine hydroxymethyltransferase activity and heme biosynthesis represents an important aspect of cancer cell metabolism. Glycine itself, rather than one-carbon units deriving from the SHMT2 reaction, is specifically critical in cancer cells
physiological function
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SHMT plays an important role in the assimilation of C1 compounds, yielding the main L-serine intermediate
physiological function
SHMT2 is required for cancer cells to adapt to the tumor environment, but also renders these cells sensitive to glycine cleavage system inhibition. The enzyme has a key role in cells in environments with limited oxygen or nutrient levels
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the 5,10-methylenetetrahydropteroylglutamate-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
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the enzyme is crucial for deoxythymidylate biosynthesis and a target for antimalarial drug development, the Plasmodium vivax enzyme catalyzes the reaction via a ternary complex mechanism
physiological function
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the enzyme is essential for parasite viability
physiological function
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the enzyme is essential for parasite viability
physiological function
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Synechococcus elongatus PCC7942 cells expressing the enzyme from Aphanothece halophytica reveal an increase in growth under salt stress condition
physiological function
the enzyme dynamically changes the fluxes of one-carbon metabolism by reversibly converting L-serine and tetrahydrofolate into 5,10-methylene-tetrahydrofolate and glycine. The cytosolic isoforms can also translocate to the nucleus to sustain de novo thymidylate synthesis and support cell proliferation
physiological function
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the enzyme has additional functions aside from its main enzymatic role in soybean cyst nematode resistance
physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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physiological function
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in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
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physiological function
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in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
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physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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physiological function
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SHMT plays an important role in the assimilation of C1 compounds, yielding the main L-serine intermediate
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physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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additional information
amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction
additional information
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amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction
additional information
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both PfSHMTc and PfSHMTm show dynamic, stage-dependent localization among the different compartments of the parasite and sequence analysis suggests they may also reversibly associate with each other, a factor that may be critical to folate cofactor function, given the apparent lack of enzymic activity of PfSHMTm
additional information
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kinetic properties of SHM2 might render this enzyme unsuitable for the high-folate conditions of photorespiring mesophyll mitochondria
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1DFO, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1KKJ, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 2DKJ, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3GBX, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4N0W, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview
additional information
the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
additional information
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the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview
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additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview
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additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
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additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview
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additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview
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additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview
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