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 | 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 | Comment | Organism | Structure |
---|---|---|---|
additional information | substrate inhibition at concentrations above 0.1 mM | Homo sapiens |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
56800 | - |
4 * 56800 | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphonooxypyruvate + NADH + H+ | Homo sapiens | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O43175 | gene PHGDH | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | skin-derived | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphonooxypyruvate + NADH + H+ | - |
Homo sapiens | ? | - |
? |
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 | Comment | Organism |
---|---|---|
3-PGDH | - |
Homo sapiens |
3-phosphoglycerate dehydrogenase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.1 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Homo sapiens |
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 |