EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.11.81 | Y53F | the substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin | Escherichia coli |
1.13.11.81 | Y54F | the substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin | Staphylococcus aureus |
4.1.2.25 | Y53F | the mutation converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin | Escherichia coli |
4.1.2.25 | Y54F | the mutation converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin | Staphylococcus aureus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.81 | 7,8-dihydroneopterin + O2 | Staphylococcus aureus | - |
7,8-dihydroxanthopterin + formate + glycolaldehyde | - |
? | |
1.13.11.81 | 7,8-dihydroneopterin + O2 | Escherichia coli | - |
7,8-dihydroxanthopterin + formate + glycolaldehyde | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.81 | Escherichia coli | P0AC16 | - |
- |
1.13.11.81 | Staphylococcus aureus | - |
- |
- |
4.1.2.25 | Escherichia coli | - |
- |
- |
4.1.2.25 | Staphylococcus aureus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.2.25 | DEAE-cellulose column chromatography and Bio-Gel A-0.5m gel filtration | Escherichia coli |
4.1.2.25 | Ni-NTA column chromatography and Bio-Gel A-0.5m gel filtration | Staphylococcus aureus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.81 | 7,8-dihydroneopterin + O2 | - |
Staphylococcus aureus | 7,8-dihydroxanthopterin + formate + glycolaldehyde | - |
? | |
1.13.11.81 | 7,8-dihydroneopterin + O2 | - |
Escherichia coli | 7,8-dihydroxanthopterin + formate + glycolaldehyde | - |
? | |
4.1.2.25 | 7,8-dihydroneopterin | - |
Staphylococcus aureus | 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde | - |
? | |
4.1.2.25 | 7,8-dihydroneopterin | - |
Escherichia coli | 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.81 | dihydroneopterin oxygenase | - |
Staphylococcus aureus |
1.13.11.81 | dihydroneopterin oxygenase | - |
Escherichia coli |
1.13.11.81 | Y53F mutant of dihydroneopterin aldolase | substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin | Escherichia coli |
1.13.11.81 | Y54F mutant of dihydroneopterin aldolase | substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin | Staphylococcus aureus |
4.1.2.25 | DHNA | - |
Staphylococcus aureus |
4.1.2.25 | DHNA | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.81 | additional information | cofactor-independent | Staphylococcus aureus | |
1.13.11.81 | additional information | cofactor-independent | Escherichia coli |