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Literature summary extracted from

  • Kim, J.; Park, S.I.; Ahn, C.; Kim, H.; Yim, J.
    Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin, a minor red eye pigment of Drosophila (2009), J. Biol. Chem., 284, 23426-23435.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.4.3 expressed in Escherichia coli BL21 cells Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.3 4-chloromercuribenzoate the deaminase activities for both 7,8-dihydropterin and guanine are completely inhibited in the presence of 1 mM 4-chloromercuribenzoate Drosophila melanogaster
3.5.4.3 adenine at concentrations of 1 and 10 mM, adenine shows weak inhibitory effect on both, guanine deaminase activity (7.1 and 24% inhibition) and dihydropterin deaminase activity (10.3 and 14.1% inhibition) Drosophila melanogaster
3.5.4.3 adenosine at concentrations of 1 and 10 mM, adenosine shows weak inhibitory effec on both, guanine deaminase activity (5.6 and 22.7% inhibition) and dihydropterin deaminase activity (11.5 and 16.7% inhibition) Drosophila melanogaster
3.5.4.3 allopurinol at concentrations of 1 and 10 mM, potassium fluoride shows weak inhibitory effect on both, guanine deaminase activity (5.2 and 11% inhibition) and dihydropterin deaminase activity (6.2 and 10.1% inhibition) Drosophila melanogaster
3.5.4.3 guanosine at concentrations of 1 and 10 mM, guanosine shows weak inhibitory effect on both, guanine deaminase activity (1.8 and 12.5% inhibition) and dihydropterin deaminase activity (3.8 and 5.1% inhibition) Drosophila melanogaster
3.5.4.3 KCN KCN inhibits dihydropterin deaminase activity strongly 98.6% inhibition at 10 mM whereas it has almost no inhibitory effect on guanine deaminase activity at the same concentration Drosophila melanogaster
3.5.4.3 lumazine at concentrations of 1 and 10 mM, allopurinol shows weak inhibitory effect on both, guanine deaminase activity (4.5 and 17.8% inhibition) and dihydropterin deaminase activity (3.2 and 10% inhibition) Drosophila melanogaster
3.5.4.3 potassium fluoride at concentrations of 1 and 10 mM, potassium fluoride shows weak inhibitory effect on both, guanine deaminase activity (3.6 and 8.1% inhibition) and dihydropterin deaminase activity (0 and 1.2% inhibition) Drosophila melanogaster
3.5.4.3 pterin pterin strongly inhibits guanine deaminase activity (57.8% inhibition at 1 mM), whereas it has a weak effect on dihydropterin deaminase activity Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.3 0.0757
-
guanine in 100 mM potassium phosphate buffer (pH 7.5), at 40°C Drosophila melanogaster
3.5.4.3 1.621
-
7,8-dihydropterin in 100 mM potassium phosphate buffer (pH 7.5), at 40°C Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.4.3 48000
-
gel filtration Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.3 Drosophila melanogaster
-
-
-
3.5.4.3 Drosophila melanogaster Oregon-R
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.4.3 ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Sephacryl HR S 300 gel filtration Drosophila melanogaster

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.4.3 0.00011
-
crude extract, at 50°C, using 7,8-dihydropterin as substrate, pH not specified in the publication Drosophila melanogaster
3.5.4.3 0.6435
-
after 5850fold purification, at 50°C, using 7,8-dihydropterin as substrate, pH not specified in the publication Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.3 7,8-dihydropterin + H2O the enzyme exhibits 40fold higher activity for guanine than for 7,8-dihydropterin. Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin Drosophila melanogaster 7,8-dihydrolumazine + NH3
-
?
3.5.4.3 7,8-dihydropterin + H2O the enzyme exhibits 40fold higher activity for guanine than for 7,8-dihydropterin. Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin Drosophila melanogaster Oregon-R 7,8-dihydrolumazine + NH3
-
?
3.5.4.3 8-azaguanine + H2O the enzyme shows 60% activity for 8-azaguanine relative to 7,8-dihydropterin Drosophila melanogaster ?
-
?
3.5.4.3 8-azaguanine + H2O the enzyme shows 60% activity for 8-azaguanine relative to 7,8-dihydropterin Drosophila melanogaster Oregon-R ?
-
?
3.5.4.3 guanine + H2O
-
Drosophila melanogaster xanthine + NH3
-
?
3.5.4.3 guanine + H2O
-
Drosophila melanogaster Oregon-R xanthine + NH3
-
?
3.5.4.3 guanosine + H2O the enzyme shows 5% activity for guanosine relative to 7,8-dihydropterin Drosophila melanogaster ?
-
?
3.5.4.3 guanosine + H2O the enzyme shows 5% activity for guanosine relative to 7,8-dihydropterin Drosophila melanogaster Oregon-R ?
-
?
3.5.4.3 additional information the enzyme has no deaminase activities for other dihydropteridines such as 7,8-dihydrobiopterin, 7,8-dihydroneopterin, and sepiapterin, it also does not show deaminase activity with fully oxidized pteridines such as pterin, biopterin, neopterin, monapterin, xanthopterin, isoxanthopterin, aminopterin, 6-formylpterin, 6-carboxypterin, and 6-hydroxymethylpterin. Moreover the enzyme does not use folic acid, pyrimidodiazepine, drosopterin, or isodrosopterin as a substrate. No activity is found for adenine and adenosine Drosophila melanogaster ?
-
?
3.5.4.3 additional information the enzyme has no deaminase activities for other dihydropteridines such as 7,8-dihydrobiopterin, 7,8-dihydroneopterin, and sepiapterin, it also does not show deaminase activity with fully oxidized pteridines such as pterin, biopterin, neopterin, monapterin, xanthopterin, isoxanthopterin, aminopterin, 6-formylpterin, 6-carboxypterin, and 6-hydroxymethylpterin. Moreover the enzyme does not use folic acid, pyrimidodiazepine, drosopterin, or isodrosopterin as a substrate. No activity is found for adenine and adenosine Drosophila melanogaster Oregon-R ?
-
?

Subunits

EC Number Subunits Comment Organism
3.5.4.3 monomer 1 * 48000, native enzyme, SDS-PAGE and gel filtration Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.3 40
-
-
Drosophila melanogaster

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.4.3 16.3
-
7,8-dihydropterin in 100 mM potassium phosphate buffer (pH 7.5), at 40°C Drosophila melanogaster
3.5.4.3 649
-
guanine in 100 mM potassium phosphate buffer (pH 7.5), at 40°C Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.3 7.5
-
-
Drosophila melanogaster

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.4.3 Drosophila melanogaster isoelectric focusing
-
5.7

General Information

EC Number General Information Comment Organism
3.5.4.3 metabolism guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin Drosophila melanogaster

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.4.3 10
-
7,8-dihydropterin in 100 mM potassium phosphate buffer (pH 7.5), at 40°C Drosophila melanogaster
3.5.4.3 8600
-
guanine in 100 mM potassium phosphate buffer (pH 7.5), at 40°C Drosophila melanogaster