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PHGDH encodes the enzyme which is involved in the early steps of L-serine synthesis in animal cells. Additionally we are shipping PHGDH Antibodies (119) and PHGDH Kits (16) and many more products for this protein.
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Human PHGDH Protein expressed in Escherichia coli (E. coli) - ABIN2005507
Pind, Slominski, Mauthe, Pearlman, Swoboda, Wilkins, Sauder, Natowicz: V490M, a common mutation in 3-phosphoglycerate dehydrogenase deficiency, causes enzyme deficiency by decreasing the yield of mature enzyme. in The Journal of biological chemistry 2002
PGDH1 (show HPGD Proteins) is essential for Arabidopsis development.
Genetic and molecular evidence were provided for the essential role of EDA9 for embryo and pollen development.
Data indicate that 3-phosphoglycerate dehydrogenases PGDH (show HPGD Proteins) (At1g17745) and EDA9 (At4g34200) were expressed preferentially in roots while 3-PGDH (At3g19480) was expressed mainly in the aerial parts and was not expressed or very poorly in roots.
These results indicate that the PHGDH gene expression, dictated by IL-2R signaling, is a crucial event for DNA synthesis during S phase of activated T cells.
Using transgenic mice expressing enhanced GFP under the Srr (show SRR Proteins) promoter and mice with targeted deletion of Srr (show SRR Proteins) or 3-Phosphoglycerate dehydrogenase, we demonstrate predominantly neuronal sources of d-serine dependent on astrocytic supply of l-serine.
Elevated levels of 4E-BP1 (show EIF4EBP1 Proteins) may be involved in a mechanism to arrest brain development in Phgdh knock out embryos.
Phgdh deletion reveals a pivotal role for L-serine biosynthesis in controlling the level of brain D-serine, an N-methyl-D-aspartate receptor (show GRIN1 Proteins) co-agonist
Data suggest expression of Phgdh in endometrium is regulated by Hoxa10.
the Phgdh-dependent phosphorylated pathway is essential for normal embryonic development, especially for brain morphogenesis
the presence of cis (show CISH Proteins)-acting elements confer the cell type specificity of Phgdh transcription in the distal promoter region.
The mouse Phgdh gene spans approximately 27 kilobases in length and comprises 12 exons with 11 intervening introns and is mapped to chromosome 3, region F2-F3 by FISH.
either Phgdh or ASCT1 (show SLC1A4 Proteins) is provided to each segment of renal tubules, suggesting that metabolic interplay mediated by L-serine biosynthesis and supply may exist in the kidney
Inactivation of Phgdh gene with changes in gene expression and associated regulatory networks resulting from serine deficiency are reported.
Overexpression of Phgdh may be generally associated with CK5 (show KRT5 Proteins) cells, and oncogenic function may be determined by isoform expression.
High expression of PHGDH is associated with Colon Cancer.
p53 (show TP53 Proteins)-mediated repression of PHGDH enhances the apoptotic response upon serine starvation in melanoma cells.
Phosphoglycerate Dehydrogenase deficiency is associated with Neu-Laxova syndrome.
We report on the identification of homozygous mutations in PHGDH and serine deficiency in individuals with Neu (show ERBB2 Proteins)-Laxova syndrome. This disorder thus seems to be an extremely severe expression of PHGDH deficiency.
PHGDH overexpression is found in cervical cancer, in particular, in bigger tumors and with advanced stages. Its expression is positively correlated with squamous cell carcinoma antigen level
The potential mechanisms by which PHGDH promotes cancer are discussed.
in some cancer cells a relatively large amount of glycolytic carbon is diverted into serine and glycine metabolism through phosphoglycerate dehydrogenase.
results reveal that certain breast cancers are dependent upon increased serine pathway flux caused by PHGDH overexpression and demonstrate the utility of in vivo negative-selection RNAi screens for finding potential anticancer targets
The crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase has been solved with bound effector, 1-serine, and substrate, hydroxypyruvic acid phosphate. The human enzyme was also examined.
This gene encodes the enzyme which is involved in the early steps of L-serine synthesis in animal cells. L-serine is required for D-serine and other amino acid synthesis. The enzyme requires NAD/NADH as a cofactor and forms homotetramers for activity. Mutations in this gene have been found in a family with congenital microcephaly, psychomotor retardation and other symptoms. Multiple alternatively spliced transcript variants have been found, however the full-length nature of most are not known.
, 3-phosphoglycerate dehyrogenase
, 3-phosphoglycerate dehydrogenase