EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.4.3.5 | structures are defined at 2.0-2.1 A resolution | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.5 | additional information | pyridoxamine 5'-phosphate shows no substrate inhibition | Escherichia coli | |
1.4.3.5 | pyridoxal 5'-phosphate | - |
Escherichia coli | |
1.4.3.5 | pyridoxine 5'-phosphate | substrate inhibition | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.5 | additional information | - |
additional information | KM-values of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M | Escherichia coli | |
1.4.3.5 | 0.002 | - |
pyridoxine 5'-phosphate | pH 8.5, 37°C | Escherichia coli | |
1.4.3.5 | 0.105 | - |
pyridoxamine 5'-phosphate | - |
Escherichia coli | |
1.4.3.5 | 0.18 | - |
O2 | - |
Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.5 | pyridoxamine 5'-phosphate + H2O + O2 | Escherichia coli | terminal step in de novo biosynthesis of pyridoxal 5'-phosphate | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? | |
1.4.3.5 | pyridoxine 5'-phosphate + H2O + O2 | Escherichia coli | terminal step in de novo biosynthesis of pyridoxal 5'-phosphate | pyridoxal 5'-phosphate + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.5 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.5 | pyridoxamine 5'-phosphate + H2O + O2 | terminal step in de novo biosynthesis of pyridoxal 5'-phosphate | Escherichia coli | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? | |
1.4.3.5 | pyridoxamine 5'-phosphate + H2O + O2 | the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate | Escherichia coli | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? | |
1.4.3.5 | pyridoxine 5'-phosphate + H2O + O2 | terminal step in de novo biosynthesis of pyridoxal 5'-phosphate | Escherichia coli | pyridoxal 5'-phosphate + H2O2 | - |
? | |
1.4.3.5 | pyridoxine 5'-phosphate + H2O + O2 | the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate | Escherichia coli | pyridoxal 5'-phosphate + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.5 | PNPOx | - |
Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.5 | additional information | - |
additional information | turnover numbers of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M | Escherichia coli | |
1.4.3.5 | 0.13 | - |
pyridoxine 5'-phosphate | pH 8.5, 37°C | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.5 | FMN | two molecules of FMN are noncovalently bound to the dimeric form of oxidase | Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.5 | 0.008 | - |
pyridoxal 5'-phosphate | - |
Escherichia coli | |
1.4.3.5 | 0.05 | - |
pyridoxine 5'-phosphate | substrate inhibition | Escherichia coli |