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Literature summary for 1.5.5.2 extracted from
- Expression, purification and characterization of the proline dehydrogenase domain of PutA from Pseudomonas putida POS-F84 (2013), Indian J. Microbiol., 53, 297-302 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ProDH, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)plysS | Pseudomonas putida |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity | Pseudomonas putida |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | I2D0K8 | - |
- |
| Pseudomonas putida POS-F84 | I2D0K8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography | Pseudomonas putida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier | Pseudomonas putida | ? | - |
? |  |
| additional information | the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier | Pseudomonas putida POS-F84 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, recombinant His-tagged enzyme, SDS-PAGE | Pseudomonas putida |
| More | Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview | Pseudomonas putida |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| L-proline:FAD oxidoreductase | - |
Pseudomonas putida |
| PRODH | - |
Pseudomonas putida |
| PutA | - |
Pseudomonas putida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
- |
Pseudomonas putida |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 70 | recombinant ProDH, highest activity at 30°C, loss of activity above 30°C, near inactivation at 70°C | Pseudomonas putida |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Pseudomonas putida |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9 | enzyme ProDH shows a good activity in the range of pH 7.0-9.0, and optimum pH at pH 8.5 | Pseudomonas putida |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252 | Pseudomonas putida | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252 | Pseudomonas putida |
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