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Literature summary for 1.1.1.95 extracted from

  • Tabatabaie, L.; de Koning, T.J.; Geboers, A.J.; van den Berg, I.E.; Berger, R.; Klomp, L.W.
    Novel mutations in 3-phosphoglycerate dehydrogenase (PHGDH) are distributed throughout the protein and result in altered enzyme kinetics (2009), Hum. Mutat., 30, 749-756.
    View publication on PubMed
Search for more literature for 1.1.1.95

Cloned(Commentary)

Cloned (Comment) Organism
gene PHGDH consists of 12 exons and maps to chromosome 1p12, enzyme expression analysis in fibroblasts, transient overexpression of FLAG-tagged wild-type and mutant enzymes in HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
A373T naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive Homo sapiens
G377S naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive Homo sapiens
additional information p.G238fsX is a naturally occuring frameshift mutation, the mutant is almost catalytically inactive with a 4fold increased Km for 3-phosphohydroxypyruvate Homo sapiens
R135W naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive Homo sapiens
V261M naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive Homo sapiens
V425M naturally occuring mutation in the carboxy-terminal regulatory domain, leads to 3-PGDH deficiency, the mutant is almost catalytically inactive Homo sapiens
V490M naturally occuring mutation in the carboxy-terminal regulatory domain, leads to 3-PGDH deficiency, the mutant is almost catalytically inactive Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information substrate inhibition at concentrations above 0.1 mM Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics, overview Homo sapiens
0.015 0.02 3-phosphohydroxypyruvate pH 7.1, 25°C, wild-type enzyme from fibroblasts Homo sapiens
0.0216
-
 3-phosphohydroxypyruvate pH 7.1, 25°C, recombinant FLAG-tagged wild-type enzyme from HEK-293 cells Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56800
-
 4 * 56800 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphonooxypyruvate + NADH + H+ Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens O43175 gene PHGDH
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast skin-derived Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphonooxypyruvate + NADH + H+
-
 Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 56800 Homo sapiens
More each subunit consists of three distinct domains: a cofactor or nucleotide binding domain, a substrate binding domain, and a regulatory domain. Structural molecular modeling of mutant enzymes, overview Homo sapiens

Synonyms

Synonyms Comment Organism
3-PGDH
-
 Homo sapiens
3-phosphoglycerate dehydrogenase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
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 Homo sapiens