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Monooxygenase L-lysine

To clarify the reaction mechanism of monooxygenase, we have recently purified two monooxygenases from pseudomonads. Imidazoleacetate monooxygenase (5) and L-lysine monooxygenase (JO) were obtained in crystalline form, and both were shown to be flavoproteins. The former requires an exogenous hydrogen donor, but the latter utilizes the hydrogen atoms of L-lysine. [Pg.177]

Table I. Estimations of Iron and Copper of Imidazoleacetate and L-Lysine Monooxygenases, /miole... Table I. Estimations of Iron and Copper of Imidazoleacetate and L-Lysine Monooxygenases, /miole...
L-Lysine monooxygenase from a pseudomonad was purified approximately 100-fold, and the enzyme was crystallized (JO) (Figure 4). Its specific activity was 10.5 /xmoles/min./mg. protein. The molecular weight was estimated to be 191,000 and the molecular activity was calculated to be 2082 at 34°C. [Pg.180]

Figure 5. Absorption spectrum of L-lysine monooxygenase. Protein, 0.62% for visible region and 0.048% for ultraviolet region... Figure 5. Absorption spectrum of L-lysine monooxygenase. Protein, 0.62% for visible region and 0.048% for ultraviolet region...

See other pages where Monooxygenase L-lysine is mentioned: [Pg.179]    [Pg.180]    [Pg.183]    [Pg.183]    [Pg.215]    [Pg.179]    [Pg.180]    [Pg.183]    [Pg.183]    [Pg.215]    [Pg.102]    [Pg.132]    [Pg.205]    [Pg.104]    [Pg.38]   
See also in sourсe #XX -- [ Pg.180 ]




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