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Literature summary for 1.5.1.37 extracted from

  • Lee, J.K.; Zhao, H.
    Identification and characterization of the flavin:NADH reductase (PrnF) involved in a novel two-component arylamine oxygenase (2007), J. Bacteriol., 189, 8556-8563.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.37

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli in a soluble form Pseudomonas protegens Pf-5

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0032
-
 FAD pH 7.0, 30°C Pseudomonas protegens Pf-5
0.0286
-
 FMN pH 7.0, 30°C Pseudomonas protegens Pf-5
0.0383
-
 riboflavin pH 7.0, 30°C Pseudomonas protegens Pf-5
0.0431
-
 NADH pH 7.0, 30°C Pseudomonas protegens Pf-5
0.0584
-
 Lumiflavin pH 7.0, 30°C Pseudomonas protegens Pf-5

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 the apparent molecular mass of the PrnD-PrnF complex appears to be approximately 120000 Da (gel filtration), confirming a 1:1 stoichiometry for binding of the two proteins, PrnD (86000 Da) and PrnF (39000 Da) Pseudomonas protegens Pf-5
19000
-
 2 * 19000, calculation from sequence Pseudomonas protegens Pf-5
39000
-
 gel filtration Pseudomonas protegens Pf-5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FAD + NADH + H+ Pseudomonas protegens Pf-5 involved in pyrrolnitrin biosynthesis. PrnF is the flavin:NADH reductase component of the two-component arylamine oxygenase system in Pseudomonas fluorescens Pf-5. PrnF reduces FAD to FADH2, which is then directly transferred to PrnD, where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine FADH2 + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas protegens Pf-5
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas protegens Pf-5

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + NADH + H+ involved in pyrrolnitrin biosynthesis. PrnF is the flavin:NADH reductase component of the two-component arylamine oxygenase system in Pseudomonas fluorescens Pf-5. PrnF reduces FAD to FADH2, which is then directly transferred to PrnD, where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine Pseudomonas protegens Pf-5 FADH2 + NAD+
-
 ?
FAD + NADH + H+ no activity with NADPH. PrnF reduces FAD to FADH2, which is then directly transferred to aminopyrrolnitrin oxygenase (PrnD), where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine. Other flavin reductases present in the host cell would not supplant the role of PrnF. The turnover rate of PrnD in the presence of PrnF is almost two times higher than that in the presence of the Escherichia coli flavin SsuE reductase (EC 1.5.1.29) Pseudomonas protegens Pf-5 FADH2 + NAD+
-
 ?
FMN + NADH + H+ 12% of the activity with FAD Pseudomonas protegens Pf-5 FMNH2 + NAD+
-
 ?
lumiflavin + NADH + H+ 6% of the activity with FAD Pseudomonas protegens Pf-5 reduced lumiflavin + NAD+
-
 ?
additional information methylene blue and ferricyanide are less than 5% as effective as FAD Pseudomonas protegens Pf-5 ?
-
 ?
riboflavin + NADH + H+ 9% of the activity with FAD Pseudomonas protegens Pf-5 reduced riboflavin + NAD+
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 19000, calculation from sequence Pseudomonas protegens Pf-5

Synonyms

Synonyms Comment Organism
flavin:NADH reductase
-
 Pseudomonas protegens Pf-5
PrnF
-
 Pseudomonas protegens Pf-5

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4
-
 pH 7.0, 1 mM dithiothreitol, 50 mM Tris-HCl, 50% loss of activity after 12 days Pseudomonas protegens Pf-5
16
-
 pH 7.0, 1 mM dithiothreitol, 50 mM Tris-HCl, 50% loss of activity after 5 days Pseudomonas protegens Pf-5
30
-
 pH 7.0, 1 mM dithiothreitol, 50 mM Tris-HCl, 50% loss of activity after 1 day Pseudomonas protegens Pf-5
42
-
 pH 7.0, 1 mM dithiothreitol, 50 mM Tris-HCl, 50% loss of activity after 30 min Pseudomonas protegens Pf-5
50
-
 pH 7.0, 1 mM dithiothreitol, 50 mM Tris-HCl, 50% loss of activity after 1 min Pseudomonas protegens Pf-5

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
62.6
-
 NADH pH 7.0, 30°C Pseudomonas protegens Pf-5
65
-
 FAD pH 7.0, 30°C Pseudomonas protegens Pf-5
66.5
-
 Lumiflavin pH 7.0, 30°C Pseudomonas protegens Pf-5
68.2
-
 riboflavin pH 7.0, 30°C Pseudomonas protegens Pf-5
72.4
-
 FMN pH 7.0, 30°C Pseudomonas protegens Pf-5

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Pseudomonas protegens Pf-5

pH Range

pH Minimum pH Maximum Comment Organism
6 8 pH 6.0: 73% of maximal activity, pH 8.0: 81% of maximal activity Pseudomonas protegens Pf-5

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Pseudomonas protegens Pf-5
FMN 12% of the activity with FAD Pseudomonas protegens Pf-5
Lumiflavin 6% of the activity with FAD Pseudomonas protegens Pf-5
NADH no activity with NADPH Pseudomonas protegens Pf-5
riboflavin 9% of the activity with FAD Pseudomonas protegens Pf-5

pI Value

Organism Comment pI Value Maximum pI Value
Pseudomonas protegens Pf-5 calculated from sequence
-
 6.3
Pseudomonas protegens Pf-5 isoelectric focusing
-
 6.5