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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 .
    View publication on PubMedView publication on EuropePMC

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