EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.5.2 | - |
Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.5.5.2 | sitting-drop vaor diffusion method, structures of the PutA PRODH domain complexed with competitive inhibitors, acetate, L-lactate and L-tetrahydro-2-furoic acid | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.5.5.2 | L432P | mutant form of PutA86-669, 5fold decrease in turnover-number and a severe loss in thermostability | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.5.2 | acetate | competitive | Escherichia coli | |
1.5.5.2 | L-lactate | competitive | Escherichia coli | |
1.5.5.2 | L-tetrahydro-2-furoic acid | competitive | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.5.2 | 0.06 | - |
L-proline | 25°C, wild-type PutA86-669 | Escherichia coli | |
1.5.5.2 | 0.13 | - |
L-proline | 25°C, L432P mutant form of PutA86-669 | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 76000 | - |
gel electrophoresis | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + acceptor + H2O | Escherichia coli | the enzyme catalyzes the first step of proline catabolism | (S)-1-pyrroline-5-carboxylate + reduced acceptor | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.5.2 | Escherichia coli | P09546 | PutA86-669 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.5.2 | - |
Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + acceptor + H2O | the enzyme catalyzes the first step of proline catabolism | Escherichia coli | (S)-1-pyrroline-5-carboxylate + reduced acceptor | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.5.2 | PRODH | - |
Escherichia coli |
1.5.5.2 | PutA proline dehydrogenase | - |
Escherichia coli |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 45 | - |
50% loss of activity of wild-type PutA86-669 after 1 h, 50% loss of of L432P mutant form of PutA86-669 after 8 min | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.5.2 | 3 | - |
L-proline | 25°C, L432P mutant form of PutA86-669 | Escherichia coli | |
1.5.5.2 | 17 | - |
L-proline | 25°C, wild-type PutA86-669 | Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.5.2 | 0.2 | - |
L-tetrahydro-2-furoic acid | - |
Escherichia coli | |
1.5.5.2 | 1 | - |
L-lactate | - |
Escherichia coli | |
1.5.5.2 | 30 | - |
acetate | - |
Escherichia coli |