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Literature summary for 4.2.3.12 extracted from

  • Ploom, T.; Thony, B.; Yim, J.; Lee, S.; Nar, H.; Leimbacher, W.; Richardson, J.; Huber, R.; Auerbach, G.
    Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase (1999), J. Mol. Biol., 286, 851-860.
    View publication on PubMed
Search for more literature for 4.2.3.12

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystallography, sitting drop vapor diffusion Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin pH 7.4, 37ºC Rattus norvegicus
1.8
-
 6-(L-erythro-1,2-dihydroxypropyl 3-monophosphate)-7,8-dihydropterin pH 7.4, 37ºC Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin Rattus norvegicus the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin Rattus norvegicus the enzyme has six active sites located at the interface of three subunits. The enzyme contains an intersubunit catalytic triad motif composed of the amino acid residues Cys A42, His B89 and Asp B88 which is involved in the abstraction of protons from the substrate side-chain carbons. The gamma and beta phosphates of the substrate are essential for substrate binding and enhance the catalytic efficiency 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-(L-erythro-1,2-dihydroxypropyl 3-monophosphate)-7,8-dihydropterin the binding constant is 225fold increased with respect to the natural substrate Rattus norvegicus 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + monophosphate
-
 ?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
-
 Rattus norvegicus 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway Rattus norvegicus 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin the enzyme has six active sites located at the interface of three subunits. The enzyme contains an intersubunit catalytic triad motif composed of the amino acid residues Cys A42, His B89 and Asp B88 which is involved in the abstraction of protons from the substrate side-chain carbons. The gamma and beta phosphates of the substrate are essential for substrate binding and enhance the catalytic efficiency Rattus norvegicus 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Rattus norvegicus
hexamer
-
 Rattus norvegicus
More each subunit consists of 144 residues with 2497 non-hydrogen atoms Rattus norvegicus