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drug target
high expression of the enzyme (PHGDH) is dramatically related to tumor resistance to chemotherapies, and treatment with PHGDH inhibitor works synergistically with chemotherapy drugs and may be an effective approach to improve overall patient survival
drug target
potential cancer therapy target
drug target
since the enzyme controls flux through the sreine biosynthetic pathway it represents a putative target in oncology
drug target
the enzyme is an attractive drug target in tumors that overexpress PHGDH or amplify the PHGDH gene
malfunction
3-PGDH deficiency is a rare recessive inborn error in the biosynthesis of the amino acid L-serine characterized clinically by congenital microcephaly, psychomotor retardation, and intractable seizures. The biochemical abnormalities associated with this disorder are low concentrations of L-serine, D-serine, and glycine in cerebrospinal fluid
malfunction
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mutations in the human PHGDH cause serine deficiency disorders characterized by severe neurological symptoms including congenital microcephaly and psychomotor retardation, growth retardation phenotypes seen in human patients suffering from SDD caused by PHGDH mutations, overview
malfunction
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Phgdh null mice have markedly decreased free serine content in their tissues, which is associated with overall growth retardation, striking brain malformation, and embryonic lethality
malfunction
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targeted disruption of Phgdh in mice causes overall growth retardation with severe brain microcephaly and leads to embryonic lethality
malfunction
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enzyme-depleted astrocytes accumulate 20fold less L-serine compared with controls
malfunction
lacking of isoform EDA9 expression causes drastic developmental defects
malfunction
PGDH1-silenced lines are inhibited in growth
malfunction
PGDH deficiency results in metabolic defects of the nervous system whose systems range from microcephaly at birth, seizures, and psychomotor retardation
malfunction
tryptophan-derived metabolites such as indole acetic acid and indole glucosinolates are present at lower concentrations in AtPGDH1-silenced plants, demonstrating that serine used as a precursor for tryptophan biosynthesis is synthesized in the phosphorylated pathway, and that the involvement of AtPGDH1 is greatest among the three isoforms
metabolism
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3-phosphoglycerate dehydrogenase catalyzes the first step of the phosphorylated pathway in the de novo synthesis of L-serine. Availability of L-serine within neural stem/progenitor cells may be a critical factor for neurogenesis in developing and adult brain
metabolism
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the enzyme is involved in L-serine biosynthesis
metabolism
the enzyme is required for the de novo biosynthesis of L-serine
metabolism
the enzyme is required for the de novo biosynthesis of L-serine
metabolism
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the enzyme catalyzes the first committed step of L-serine biosynthesis
metabolism
enzyme in the L-serine biosynthetic pathway
metabolism
enzyme in the L-serine biosynthetic pathway
metabolism
enzyme in the L-serine biosynthetic pathway
metabolism
first committed enzyme of the phosphorylated pathway of L-serine biosynthesis, regulated by negative feedback from L-serine in bacteria and plants
metabolism
first committed enzyme of the phosphorylated pathway of L-serine biosynthesis. Regulated by negative feedback from L-serine in bacteria
metabolism
first step of L-serine biosynthesis
metabolism
first step of L-serine biosynthesis
metabolism
key enzyme in L-serine biosynthesis. The coupling between D-3-phosphoglycerate dehydrogenase (SerA) and D-2-hydroxyglutarate dehydrogenase (D2HGDH) sits in the hub of L-serine biosynthesis and establishes a linkage among intermediates in glycolysis, TCA cycle, and amino acid biosynthesis. The reactions catalyzed by cytoplasmic SerA and mitochondrial D2HGDH may be coupled through the shuttle of 2-ketoglutarate and D-2-hydroxyglutarate between the cytosol and mitochondrial matrix
metabolism
key enzyme in L-serine biosynthesis. The coupling between D-3-phosphoglycerate dehydrogenase (SerA) and D-2-hydroxyglutarate dehydrogenase (D2HGDH) sits in the hub of L-serine biosynthesis and establishes a linkage among intermediates in glycolysis, TCA cycle, and amino acid biosynthesis. The reactions catalyzed by cytoplasmic SerA and mitochondrial D2HGDH may be coupled through the shuttle of 2-ketoglutarate and D-2-hydroxyglutarate between the cytosol and mitochondrial matrix
metabolism
the enzyme catalyzes the first committed step of Ser biosynthetic pathway in plastids. Activity of PGDH2 is not enhanced upon reduction by thioredoxin
metabolism
the enzyme catalyzes the first committed step of Ser biosynthetic pathway in plastids. Activity of PGDH3 is not enhanced upon reduction by thioredoxin
metabolism
the enzyme catalyzes the first committed step of Ser biosynthetic pathway in plastids. Isoform PGDH1 forms the intramolecular disulfide bond between Cys86 and Cys102, lowering PGDH enzyme activity. It is activated by cleavage of intramolecular disulfide bond. Some thioredoxin subtypes in plastids support PGDH1 reductive activation. PGDH1 is a redox-sensitive protein whose activity is enhanced upon reduction
metabolism
the enzyme catalyzes the first step in the de novo synthesis pathway of serine, a critical amino acid for protein and nucleic acid biosynthesis
metabolism
the enzyme catalyzes the first, rate-limiting step in the synthesis of serine from glucose
metabolism
the enzyme catalyzes the rate limiting step in serine biosynthesis pathway
metabolism
the first and only rate-limiting enzyme in the de novo serine biosynthetic pathway
metabolism
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key enzyme in L-serine biosynthesis. The coupling between D-3-phosphoglycerate dehydrogenase (SerA) and D-2-hydroxyglutarate dehydrogenase (D2HGDH) sits in the hub of L-serine biosynthesis and establishes a linkage among intermediates in glycolysis, TCA cycle, and amino acid biosynthesis. The reactions catalyzed by cytoplasmic SerA and mitochondrial D2HGDH may be coupled through the shuttle of 2-ketoglutarate and D-2-hydroxyglutarate between the cytosol and mitochondrial matrix
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metabolism
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first step of L-serine biosynthesis
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metabolism
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enzyme in the L-serine biosynthetic pathway
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metabolism
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first step of L-serine biosynthesis
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physiological function
3-PGDH deficiency is a rare recessive inborn error in the biosynthesis of the amino acid L-serine characterized clinically by congenital microcephaly, psychomotor retardation, and intractable seizures. The biochemical abnormalities associated with this disorder are low concentrations of L-serine, D-serine, and glycine in cerebrospinal fluid
physiological function
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mutations in the human PHGDH cause serine deficiency disorders characterized by severe neurological symptoms including congenital microcephaly and psychomotor retardation
physiological function
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Phgdh knockout mouse embryos demonstrate that free serine and glycine concentrations are decreased markedly in head samples
physiological function
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Phgdh null mice have markedly decreased free serine content in their tissues, which is associated with overall growth retardation, striking brain malformation, and embryonic lethality
physiological function
phosphoglycerate dehydrogenase isoform EDA9 is the essential gene for embryo and male gametophyte development in Arabidopsis thaliana
physiological function
the gene EDA9 plays a crucial role in embryo and pollen development
physiological function
key enzyme involved in the synthesis of L-serine. Might play a crucial role in the provision of L-serine in the larva of Bombyx mori
physiological function
the enzyme plays an important role during salt stress in sugar beet
physiological function
the enzyme promotes some tumors growth via non-metabolic way by upregulating target cancer-promoting genes