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Literature summary extracted from

  • Unterlass, J.E.; Wood, R.J.; Basle, A.; Tucker, J.; Cano, C.; Noble, M.M.E.; Curtin, N.J.
    Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH) (2017), Oncotarget, 8, 104478-104491 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.95 sitting drop vapour diffusion method, cocrystal structure of catalytic subunit of the enzyme (PHGDHs) with NAD+ and L-tartrate reveals a domain movement upon substrate binding Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.95 adenosine 5'-diphosphoribose 0.12 mM, 50% inhibition. NAD+ competitive inhibitor Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.95 0.0053
-
 NAD+ pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.0118
-
 Thionicotinamide pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.0393
-
 acetylpyridine pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.1477
-
 pyridinealdehyde adenine dinucleotide pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.187
-
 3-phospho-D-glycerate pH 7.5, temperature not specified in the publication Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.95 3-phospho-D-glycerate + NAD+ Homo sapiens
-
 3-phosphooxypyruvate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.95 Homo sapiens O43175
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 3-phospho-D-glycerate + NAD+
-
 Homo sapiens 3-phosphooxypyruvate + NADH + H+
-
 r
1.1.1.95 3-phospho-D-glycerate + NAD+ the enzyme has a 400fold higher affinity for NADH than NAD+ Homo sapiens 3-phosphooxypyruvate + NADH + H+
-
 r
1.1.1.95 3-phosphooxypyruvate + acetylpyridine
-
 Homo sapiens 3-phospho-D-glycerate + ?
-
 r
1.1.1.95 3-phosphooxypyruvate + NADH + H+ the enzyme has a 400fold higher affinity for NADH than NAD+ Homo sapiens 3-phospho-D-glycerate + NAD+
-
 r
1.1.1.95 3-phosphooxypyruvate + pyridinealdehyde adenine dinucleotide
-
 Homo sapiens 3-phospho-D-glycerate + ?
-
 r
1.1.1.95 3-phosphooxypyruvate + thionicotinamide
-
 Homo sapiens 3-phospho-D-glycerate + ?
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.95 dimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.1.1.95 3-phosphoglycerate dehydrogenase
-
 Homo sapiens
1.1.1.95 Phgdh
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.95 0.0035
-
 pyridinealdehyde adenine dinucleotide pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.005
-
 NAD+ pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.0075
-
 Thionicotinamide pH 7.5, temperature not specified in the publication Homo sapiens
1.1.1.95 0.017
-
 acetylpyridine pH 7.5, temperature not specified in the publication Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.95 NAD+
-
 Homo sapiens
1.1.1.95 NADH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.1.1.95 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 Homo sapiens