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Literature summary extracted from

  • Abdelwahab, H.; Robinson, R.; Rodriguez, P.; Adly, C.; El-Sohaimy, S.; Sobrado, P.
    Identification of structural determinants of NAD(P)H selectivity and lysine binding in lysine N(6)-monooxygenase (2016), Arch. Biochem. Biophys., 606, 180-188 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.59 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 Nocardia farcinica
1.14.13.59 M239R mutation results in high production of hydrogen peroxide and little hydroxylation with no change in coenzyme selectivity Nocardia farcinica
1.14.13.59 R301A mutation causes a 300fold decrease on kcat/Km value with NADPH but no change with NADH Nocardia farcinica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.59 0.08
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.09
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.14
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.4
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.4
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 1.5
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 2.6
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption Nocardia farcinica

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.59 Nocardia farcinica Q5Z1T5
-
-
1.14.13.59 Nocardia farcinica IFM 10152 Q5Z1T5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.59 L-lysine + NADH + H+ + O2 the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction Nocardia farcinica N6-hydroxy-L-lysine + NAD+ + H2O
-
 ?
1.14.13.59 L-lysine + NADH + H+ + O2 the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction Nocardia farcinica IFM 10152 N6-hydroxy-L-lysine + NAD+ + H2O
-
 ?
1.14.13.59 L-lysine + NADPH + H+ + O2 the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction Nocardia farcinica N6-hydroxy-L-lysine + NADP+ + H2O
-
 ?
1.14.13.59 L-lysine + NADPH + H+ + O2 the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH, while E216 plays a role in L-Lys binding and FAD reduction Nocardia farcinica IFM 10152 N6-hydroxy-L-lysine + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.59 lysine N6-monooxygenase
-
 Nocardia farcinica
1.14.13.59 NbtG
-
 Nocardia farcinica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.59 25
-
 assay at Nocardia farcinica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.59 0.7
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.8
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.98
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 1.08
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 1.29
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 2.4
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption Nocardia farcinica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.59 7.5
-
 assay at Nocardia farcinica

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.59 FAD E216 plays a role in L-Lys binding and FAD reduction Nocardia farcinica
1.14.13.59 NADH the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH Nocardia farcinica
1.14.13.59 NADPH the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH Nocardia farcinica

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.13.59 0.026
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.545
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 0.94
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 3.3
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 5.95
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 7.7
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 8.9
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption Nocardia farcinica
1.14.13.59 10.7
-
 NADPH pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption Nocardia farcinica