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Literature summary for 1.18.1.3 extracted from

  • Dutta, T.; Dutta, A.; Chakraborty, J.; Sarkar, J.; Pal Chowdhury, P.; Gunsalus, I.
    Purification and properties of reductase of the three-component p-cymene methyl hydroxylase from Pseudomonas chlororaphis subsp. aureofaciens (2012), Process Biochem., 47, 1263-1267 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
-
Pseudomonas chlororaphis subsp. aureofaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
gel fitlration Pseudomonas chlororaphis subsp. aureofaciens

Organism

Organism UniProt Comment Textmining
Pseudomonas chlororaphis subsp. aureofaciens P95461 enzyme acts as reductase subunit of p-cymene mono-oxygenase, EC 1.14.15.25
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Storage Stability

Storage Stability Organism
70°C, 50 mM potassium phosphate buffer (pH 7.0), 60% glycerol (v/v), subunit CymA is stable for 1 month Pseudomonas chlororaphis subsp. aureofaciens

Subunits

Subunits Comment Organism
? x * 38433, calculated, x * 38000, SDS-PAGE Pseudomonas chlororaphis subsp. aureofaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
10 min, 42% loss of activity Pseudomonas chlororaphis subsp. aureofaciens
50
-
10 min, 98% loss of activity Pseudomonas chlororaphis subsp. aureofaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
-
Pseudomonas chlororaphis subsp. aureofaciens

Cofactor

Cofactor Comment Organism Structure
FAD 1.07 mol/mol of enzyme Pseudomonas chlororaphis subsp. aureofaciens
additional information no activity with NADPH Pseudomonas chlororaphis subsp. aureofaciens
NADH
-
Pseudomonas chlororaphis subsp. aureofaciens
[2Fe-2S]-center presence of one [2Fe-2S] center per enzyme molecule Pseudomonas chlororaphis subsp. aureofaciens

Expression

Organism Comment Expression
Pseudomonas chlororaphis subsp. aureofaciens expression of subunits CymABM is induced by growth on p-cymene up