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Literature summary for 3.6.1.9 extracted from

  • Joye, I.J.; Belien, T.; Brijs, K.; Soetaert, W.; Delcour, J.A.
    Mutational analysis of wheat (Triticum aestivum L.) nucleotide pyrophosphatase/phosphodiesterase shows the role of six amino acids in the catalytic mechanism (2011), Appl. Microbiol. Biotechnol., 90, 173-180.
    View publication on PubMed
Search for more literature for 3.6.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Pichia pastoris, the enzymes are secreted Triticum aestivum

Protein Variants

Protein Variants Comment Organism
E199A site-directed mutagenesis, the mutant shows increased activity with substrate 4-nitrophenyl phosphate compared to the wild-type Triticum aestivum
E199D site-directed mutagenesis, the mutation doubles the enzyme activity against NAD(H) Triticum aestivum
F194S site-directed mutagenesis, the mutation increases the relative enzyme activity against adenosine 5'-monophosphate-containing substrates, although the overall enzyme activity of the mutant enzyme decreases compared to the wild-type Triticum aestivum
H255A site-directed mutagenesis, mutation of the highly conserved residue into an apolar increases enzyme activity against most phosphodiester substrates Triticum aestivum
additional information construction and 3D structure model of the truncated form of wheat nucleotide pyrophosphatase/phosphodiesterase, overview Triticum aestivum
N153A site-directed mutagenesis, the mutant shows increased activity with substrate 4-nitrophenyl phosphate compared to the wild-type Triticum aestivum
N165A site-directed mutagenesis, the mutant shows increased activity with substrate 4-nitrophenyl phosphate compared to the wild-type Triticum aestivum
T132A site-directed mutagenesis, substitution of the highly conserved catalytic residue results in an inactive mutant Triticum aestivum
T132S site-directed mutagenesis, substitution of the highly conserved catalytic residue results in an inactive mutant Triticum aestivum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane transmembrane enzyme Triticum aestivum 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metal binding enzyme Triticum aestivum

Organism

Organism UniProt Comment Textmining
Triticum aestivum D9YT79 cf. EC 3.1.4.1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Pichia pastoris culture medium by concanavalin A affinity chromatography, elution with methyl-alpha-D-glucopyranoside, anion exchange chromatography, dialysis, and another step of anion exchange chromatography followed by gel filtration Triticum aestivum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Triticum aestivum 4-nitrophenol + phosphate
-
 ?
ATP + H2O
-
 Triticum aestivum ADP + phosphate
-
 ?
CTP + H2O
-
 Triticum aestivum CDP + phosphate
-
 ?
GTP + H2O
-
 Triticum aestivum GDP + phosphate
-
 ?
additional information the structural requirements and the conservation of the amino acids of the catalytic site of TaNPPr and, by extension, probably of all NPPs, are very stringent Triticum aestivum ?
-
 ?
NAD+ + H2O
-
 Triticum aestivum NMN + AMP
-
 ?
NADH + H2O
-
 Triticum aestivum NMNH + AMP
-
 ?
NADPH + H2O
-
 Triticum aestivum NMNH + adenosine 2',5'-phosphate
-
 ?
TTP + H2O
-
 Triticum aestivum TDP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
NPPr
-
 Triticum aestivum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 assay at Triticum aestivum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.7
-
 assay at Triticum aestivum

General Information

General Information Comment Organism
evolution the enzyme belongs to the superfamily of the alkaline phosphatases Triticum aestivum