EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.4.3 | expressed in Escherichia coli BL21 cells | Drosophila melanogaster |
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 |
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 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.4.3 | 48000 | - |
gel filtration | Drosophila melanogaster |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.4.3 | Drosophila melanogaster | - |
- |
- |
3.5.4.3 | Drosophila melanogaster Oregon-R | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.4.3 | ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Sephacryl HR S 300 gel filtration | Drosophila melanogaster |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
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 |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.4.3 | monomer | 1 * 48000, native enzyme, SDS-PAGE and gel filtration | Drosophila melanogaster |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.4.3 | 40 | - |
- |
Drosophila melanogaster |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.4.3 | 7.5 | - |
- |
Drosophila melanogaster |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.5.4.3 | Drosophila melanogaster | isoelectric focusing | - |
5.7 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.4.3 | metabolism | guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin | Drosophila melanogaster |
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 |