Cloned (Comment) | Organism |
---|---|
wild-type and mutant enzyme | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
enzyme in complex with pyridoxal 5'-phosphate, space group C2, 2.07 A resolution | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D49A | decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
H199A | decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
H199N | little decrease in pyridoxine 5'-phosphate turnover | Escherichia coli |
R14E | decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
R14M | decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
R197E | strong decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
R197M | catalyzes removal of the proS hydrogen atom from (4'R)-3H-pyridoxamine 5'-phosphate, decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
Y17F | decrease in affinity for pyridoxine 5'-phosphate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0003 | - |
pyridoxine 5'-phosphate | - |
Escherichia coli | |
0.0003 | - |
pyridoxine 5'-phosphate | H199N mutant enzyme | Escherichia coli | |
0.001 | - |
pyridoxine 5'-phosphate | D49A and Y17F mutant enzyme | Escherichia coli | |
0.002 | - |
pyridoxine 5'-phosphate | R14E mutant enzyme | Escherichia coli | |
0.0026 | - |
pyridoxine 5'-phosphate | R14M mutant enzyme | Escherichia coli | |
0.07 | - |
pyridoxine 5'-phosphate | H199A mutant enzyme | Escherichia coli | |
0.09 | - |
pyridoxine 5'-phosphate | R197M mutant enzyme | Escherichia coli | |
2.4 | - |
pyridoxine 5'-phosphate | R197M mutant enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AFI7 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2 | enzyme is specific for removal of the pro-R hydrogen atom from the prochiral C4' carbon atom of pyridoxamine 5'-phosphate, hydride ion mechanism is suggested | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyridoxamine 5'-phosphate + H2O + O2 | - |
Escherichia coli | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.008 | - |
pyridoxine 5'-phosphate | R197M mutant enzyme | Escherichia coli | |
0.03 | - |
pyridoxine 5'-phosphate | H199N mutant enzyme | Escherichia coli | |
0.03 | - |
pyridoxine 5'-phosphate | R197M mutant enzyme | Escherichia coli | |
0.06 | - |
pyridoxine 5'-phosphate | D49A mutant enzyme | Escherichia coli | |
0.13 | - |
pyridoxine 5'-phosphate | - |
Escherichia coli | |
0.14 | - |
pyridoxine 5'-phosphate | H199A mutant enzyme | Escherichia coli | |
0.14 | - |
pyridoxine 5'-phosphate | R14M mutant enzyme | Escherichia coli | |
0.16 | - |
pyridoxine 5'-phosphate | R14E mutant enzyme | Escherichia coli | |
0.6 | - |
pyridoxine 5'-phosphate | Y17F mutant enzyme | Escherichia coli |