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1.14.13.59: L-lysine N6-monooxygenase (NADPH)

This is an abbreviated version!
For detailed information about L-lysine N6-monooxygenase (NADPH), go to the full flat file.

Word Map on EC 1.14.13.59

Reaction

L-lysine
+
NADPH
 +
H+
 +
O2
=
N6-hydroxy-L-lysine
 +
NADP+
 +
H2O

Synonyms

EC 1.13.12.10, EC 13.12.10, flavin-dependent lysine monooxygenase, flavin-dependent N6-lysine monooxygenase, IucD, LH, lysine monooxygenase, Lysine N(6)-hydroxylase, Lysine N6-hydroxylase, lysine N6-monooxygenase, lysine: N6-hydroxylase, lysine:N(6)-hydroxylase, Lysine:N6-hydroxylase, MbsG, N-hydroxylating monooxygenase, NbtG, Oxygenase, lysine N6-mono-

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.59 L-lysine N6-monooxygenase (NADPH)

Engineering

Engineering on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C146A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C158A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C166A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C31A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C31A/C51A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A
-
site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A rlucD
-
activity of the genetically engineered enzyme forms C51A rIucD, C51A/C158A eIucD is 1.5times that of the parent rIucD. The activity of C158A rIucD is similar to that of the parent enzyme form
C51A/C158A
-
site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A/C158A rlucD
-
activity of the genetically engineered enzyme forms C51A rIucD, C51A/C158A eIucD is 1.5times that of the parent rIucD. The activity of C158A rIucD is similar to that of the parent enzyme form
C51A/C166A
-
site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
E216Q
mutation increases the Km value for L-Lys by 30fold with very little change on the kcat value or in the binding of NAD(P)H
K184A
-
site-directed mutagenesis
K200A
-
site-directed mutagenesis
K202A
-
site-directed mutagenesis
K64A
-
site-directed mutagenesis, the K64A variant support a conserved amino acid substrate binding site among members of the NMO group of enzymes, crystal structure analysis, overview
M239R
mutation results in high production of hydrogen peroxide and little hydroxylation with no change in coenzyme selectivity
P238R
-
site-directed mutagenesis, substitution of Pro to an Arg at position 238 converts NbtG into a NADPH-specific monooxygenase but increases the Km value for NADPH. The P238R enzyme is as uncoupled as wild-type NbtG
R301A
mutation causes a 300fold decrease on kcat/Km value with NADPH but no change with NADH
E216Q
-
mutation increases the Km value for L-Lys by 30fold with very little change on the kcat value or in the binding of NAD(P)H
-
M239R
-
mutation results in high production of hydrogen peroxide and little hydroxylation with no change in coenzyme selectivity
-
R301A
-
mutation causes a 300fold decrease on kcat/Km value with NADPH but no change with NADH
-
additional information