Literature summary extracted from
Omidinia, E.; Mahdizadehdehosta, R.; Mohammadi, H.S.
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)
EC Number |
Cloned (Comment) |
Organism |
---|
1.5.5.2 |
gene ProDH, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)plysS |
Pseudomonas putida |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.5.5.2 |
additional information |
the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity |
Pseudomonas putida |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.5.5.2 |
Pseudomonas putida |
I2D0K8 |
- |
- |
1.5.5.2 |
Pseudomonas putida POS-F84 |
I2D0K8 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.5.5.2 |
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography |
Pseudomonas putida |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.5.5.2 |
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 |
? |
- |
? |
|
1.5.5.2 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
1.5.5.2 |
? |
x * 40000, recombinant His-tagged enzyme, SDS-PAGE |
Pseudomonas putida |
1.5.5.2 |
More |
Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview |
Pseudomonas putida |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.5.5.2 |
L-proline:FAD oxidoreductase |
- |
Pseudomonas putida |
1.5.5.2 |
PRODH |
- |
Pseudomonas putida |
1.5.5.2 |
PutA |
- |
Pseudomonas putida |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.5.5.2 |
30 |
- |
- |
Pseudomonas putida |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
1.5.5.2 |
25 |
70 |
recombinant ProDH, highest activity at 30°C, loss of activity above 30°C, near inactivation at 70°C |
Pseudomonas putida |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.5.5.2 |
8.5 |
- |
assay at |
Pseudomonas putida |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
1.5.5.2 |
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
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.5.5.2 |
FAD |
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252 |
Pseudomonas putida |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.5.5.2 |
additional information |
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252 |
Pseudomonas putida |