Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.12 cloned in Escherichia coli Rattus norvegicus

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.12 0.0005
-
 7,8-dihydroneopterin triphosphate mutant E133Q pH 7.4, 37ºC Rattus norvegicus
4.2.3.12 0.00177
-
 7,8-dihydroneopterin triphosphate mutant H89N pH 7.4, 37ºC Rattus norvegicus
4.2.3.12 0.008
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin wild-type enzyme Rattus norvegicus
4.2.3.12 0.008
-
 7,8-dihydroneopterin triphosphate pH 7.4, 37ºC Rattus norvegicus
4.2.3.12 5
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin mutant enzyme E133Q Rattus norvegicus
4.2.3.12 17.7
-
 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin mutant enzyme H89N Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.12 Ca2+ less than 15% of activity with Mg2+ with 5 mM Rattus norvegicus
4.2.3.12 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
4.2.3.12 Mg2+ free metal enzyme activity is 15% of the wild type with 8 mM, it is not bound to the enzyme Rattus norvegicus
4.2.3.12 Mn2+ less than 15% of activity with Mg2+ with 5 mM Rattus norvegicus
4.2.3.12 additional information Cu2+, Fe2+, less than 15% of activity with Mg2+ with 5 mM of each ion Rattus norvegicus
4.2.3.12 Ni2+ 71% of the activity with Mg2+ with NiCl2, 5 mM Rattus norvegicus
4.2.3.12 Zn2+ the zinc/enzyme-subunit ratio of the wild-type enzyme is 0.8 Rattus norvegicus
4.2.3.12 Zn2+ free metal enzyme activity reaches 85% of activity of wild type with 0.05 mM and 8 mM Mg2+ Rattus norvegicus
4.2.3.12 Zn2+ bound to the enzyme Rattus norvegicus
4.2.3.12 Zn2+ concentrations higher than 0.15 mM completely inactivates the enzyme Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.3.12 15855
-
 x * 15855, calculation from nucleotide sequence Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.12 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
-
 ?
4.2.3.12 7,8-dihydroneopterin triphosphate Rattus norvegicus assay at 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.12 Rattus norvegicus
-
 cloned in Escherichia coli
-

Purification (Commentary)

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

Storage Stability

EC Number Storage Stability Organism
4.2.3.12 4ºC, Tris-HCl, 4 weeks, no degradation Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.12 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
-
 Rattus norvegicus 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
4.2.3.12 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
-
 ?
4.2.3.12 7,8-dihydroneopterin triphosphate
-
 Rattus norvegicus 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
 ?
4.2.3.12 7,8-dihydroneopterin triphosphate assay at Rattus norvegicus 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
 ?

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.3.12 37
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.12 7.4
-
 assay at Rattus norvegicus