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

BRENDA support

Literature summary extracted from

  • Robinson, R.; Sobrado, P.
    Substrate binding modulates the activity of Mycobacterium smegmatis G, a flavin-dependent monooxygenase involved in the biosynthesis of hydroxamate-containing siderophores (2011), Biochemistry, 50, 8489-8496.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.59 expression in Escherichia coli Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.59 0.2 1 L-lysine pH 7.5, 25°C Mycolicibacterium smegmatis
1.14.13.59 1.1
-
NADH pH 7.5, 25°C Mycolicibacterium smegmatis
1.14.13.59 2.4
-
NADPH pH 7.5, 25°C Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.59 Mycolicibacterium smegmatis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.59 L-lysine + NADH + H+ + O2
-
Mycolicibacterium smegmatis N6-hydroxy-L-lysine + NAD+ + H2O
-
?
1.14.13.59 L-lysine + NADPH + H+ + O2
-
Mycolicibacterium smegmatis N6-hydroxy-L-lysine + NADP+ + H2O
-
?
1.14.13.59 additional information enzyme functions as an oxidase when the activity of MbsG is measured by monitoring oxygen consumption in the absence of L-lysine, oxidizing NADH and NADPH with kcat values of 59 and 49 per min, respectively. Under these conditions, both hydrogen peroxide and superoxide are produced Mycolicibacterium smegmatis ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.59 0.08
-
L-lysine pH 7.5, 25°C Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.59 FAD tigtly bound cofactor Mycolicibacterium smegmatis
1.14.13.59 NADH
-
Mycolicibacterium smegmatis
1.14.13.59 NADPH
-
Mycolicibacterium smegmatis