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Literature summary for 4.2.3.12 extracted from

  • Burgisser, D.M.; Thöny, B.; Redweik, U.; Hess, D.; Heizmann, C.W.; Huber, R.; Nar, H.
    6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif. Site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modeling of substrate binding (1995), J. Mol. Biol., 253, 358-369.
    View publication on PubMed
Search for more literature for 4.2.3.12

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C42A no catalytic activity, complete loss of metal binding site and activity, it is the only Cys in the active site Rattus norvegicus
E133Q 1.3% of wild-type activity but similar affinity for the substrate Rattus norvegicus
H23L complete loss of metal binding site and activity Rattus norvegicus
H48L complete loss of metal binding site and activity Rattus norvegicus
H50L complete loss of metal binding site and activity Rattus norvegicus
H89N 4.3% of wild-type activity but similar affinity for the substrate Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0005
-
 7,8-dihydroneopterin triphosphate mutant E133Q pH 7.4, 37ºC Rattus norvegicus
0.00177
-
 7,8-dihydroneopterin triphosphate mutant H89N pH 7.4, 37ºC Rattus norvegicus
0.008
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin wild-type enzyme Rattus norvegicus
0.008
-
 7,8-dihydroneopterin triphosphate pH 7.4, 37ºC Rattus norvegicus
5
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin mutant enzyme E133Q Rattus norvegicus
17.7
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin mutant enzyme H89N Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ less than 15% of activity with Mg2+ with 5 mM Rattus norvegicus
Co2+ free metal enzyme activity reaches 60% of activity of wild type with 0.50 mM and concentrations higher than 0.15 mM completely inactivates the enzyme. Less than 15% of activity with Mg2+ with 5 mM Rattus norvegicus
Mg2+ free metal enzyme activity is 15% of the wild type with 8 mM, it is not bound to the enzyme Rattus norvegicus
Mn2+ less than 15% of activity with Mg2+ with 5 mM Rattus norvegicus
additional information Cu2+, Fe2+, less than 15% of activity with Mg2+ with 5 mM of each ion Rattus norvegicus
Ni2+ 71% of the activity with Mg2+ with NiCl2, 5 mM Rattus norvegicus
Zn2+ the zinc/enzyme-subunit ratio of the wild-type enzyme is 0.8 Rattus norvegicus
Zn2+ free metal enzyme activity reaches 85% of activity of wild type with 0.05 mM and 8 mM Mg2+ Rattus norvegicus
Zn2+ bound to the enzyme Rattus norvegicus
Zn2+ concentrations higher than 0.15 mM completely inactivates the enzyme Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15855
-
 x * 15855, calculation from nucleotide sequence 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 is involved in tetrahydrobiopterin biosynthesis 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
7,8-dihydroneopterin triphosphate Rattus norvegicus assay at 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 cloned in Escherichia coli
-

Purification (Commentary)

Purification (Comment) Organism
affinity chromatography, gel filtration, SDS-PAGE Rattus norvegicus

Storage Stability

Storage Stability Organism
4ºC, Tris-HCl, 4 weeks, no degradation Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 is involved in tetrahydrobiopterin biosynthesis Rattus norvegicus 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
7,8-dihydroneopterin triphosphate
-
 Rattus norvegicus 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
7,8-dihydroneopterin triphosphate assay at Rattus norvegicus 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 15855, calculation from nucleotide sequence Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Rattus norvegicus