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Literature summary extracted from

  • Buschmann, J.; Moritz, B.; Jeske, M.; Lilie, H.; Schierhorn, A.; Wahle, E.
    Identification of Drosophila and human 7-methyl GMP-specific nucleotidases (2013), J. Biol. Chem., 288, 2441-2451.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.91 phosphate stimulation Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.91 expression in Escherichia coli Homo sapiens
3.1.3.91 expression in S2 cell Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.91 AMP
-
Drosophila melanogaster
3.1.3.91 KCl
-
Drosophila melanogaster
3.1.3.91 potassium acetate
-
Drosophila melanogaster
3.1.3.91 potassium phosphate
-
Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.91 0.0078
-
N7-methyl-GMP pH 7.5, 37°C Homo sapiens
3.1.3.91 0.013
-
N7-methyl-GMP pH 7.5, 25°C Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.91 34000
-
analytical ultracentrifugation Homo sapiens
3.1.3.91 34400
-
34400, calculated Homo sapiens
3.1.3.91 36000
-
PAGE Drosophila melanogaster
3.1.3.91 36300
-
1 * 40000, SDS-PAGE, 1 * 36300, calculated Drosophila melanogaster
3.1.3.91 40000
-
gel filtration Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.91 Drosophila melanogaster Q9W197
-
-
3.1.3.91 Homo sapiens Q9H0P0
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.91 embryo
-
Drosophila melanogaster
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.91 additional information enzyme also efficiently dephosphorylates CMP, although with lower apparent affinity, Reaction of EC 3.1.3.5. UMP and the purine nucleotides are poor substrates Drosophila melanogaster ?
-
?
3.1.3.91 additional information enzyme also efficiently dephosphorylates CMP, Reaction of EC 3.1.3.5. UMP is a reasonable substrate, and the purine nucleotides are poor substrates Homo sapiens ?
-
?
3.1.3.91 N7-methyl-GDP + H2O
-
Drosophila melanogaster N7-methyl-guanosine + 2 phosphate 37fold less efficient than reaction with N7-methyl-GMP ?
3.1.3.91 N7-methyl-GDP + H2O
-
Homo sapiens N7-methyl-guanosine + 2 phosphate 37fold less efficient than reaction with N7-methyl-GMP ?
3.1.3.91 N7-methyl-GMP + H2O
-
Drosophila melanogaster N7-methyl-guanosine + phosphate enzyme cleaves m7GMP to 7-methylguanosine and phosphate ?
3.1.3.91 N7-methyl-GMP + H2O
-
Homo sapiens N7-methyl-guanosine + phosphate enzyme cleaves m7GMP to 7-methylguanosine and phosphate ?

Subunits

EC Number Subunits Comment Organism
3.1.3.91 monomer 1 * 40000, SDS-PAGE, 1 * 36300, calculated Drosophila melanogaster
3.1.3.91 monomer 34400, calculated Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.3.91 CG3362
-
Drosophila melanogaster
3.1.3.91 cytosolic 5'-nucleotidase 3
-
Homo sapiens
3.1.3.91 NT5C3A
-
Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.91 0.24
-
N7-methyl-GMP pH 7.5, 37°C Homo sapiens
3.1.3.91 6.3
-
N7-methyl-GMP pH 7.5, 25°C Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.91 7.5
-
-
Drosophila melanogaster

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.1.3.91 0.06
-
pH 7.5, 25°C Drosophila melanogaster potassium phosphate
3.1.3.91 0.52
-
pH 7.5, 25°C Drosophila melanogaster KCl
3.1.3.91 0.65
-
pH 7.5, 25°C Drosophila melanogaster potassium acetate
3.1.3.91 2
-
pH 7.5, 25°C Drosophila melanogaster AMP

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.3.91 0.3
-
N7-methyl-GMP pH 7.5, 37°C Homo sapiens
3.1.3.91 460
-
N7-methyl-GMP pH 7.5, 25°C Drosophila melanogaster