Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.10 extracted from

  • van Hellemond, E.W.; Mazon, H.; Heck, A.J.; van den Heuvel, R.H.; Heuts, D.P.; Janssen, D.B.; Fraaije, M.W.
    ADP competes with FAD binding in putrescine oxidase (2008), J. Biol. Chem., 283, 28259-28264.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Top10 cells Rhodococcus erythropolis

Protein Variants

Protein Variants Comment Organism
A394C active mutant with covalently bound FAD Rhodococcus erythropolis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100100
-
mass spectrometry Rhodococcus erythropolis

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis
-
-
-
Rhodococcus erythropolis NCIMB 11540
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rhodococcus erythropolis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
putrescine + O2 + H2O
-
Rhodococcus erythropolis 4-aminobutanal + NH3 + H2O2
-
?
putrescine + O2 + H2O
-
Rhodococcus erythropolis NCIMB 11540 4-aminobutanal + NH3 + H2O2
-
?

Subunits

Subunits Comment Organism
homodimer
-
Rhodococcus erythropolis

Synonyms

Synonyms Comment Organism
PuO
-
Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme is isolated as a mixture of dimers containing two molecules of FAD, two molecules ADP, or one FAD and one ADP molecule, the low FAD:protein ratio is the result of tight binding of ADP thereby competing with FAD binding Rhodococcus erythropolis