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Information on EC 1.14.13.B28 - monooxygenase CYP119A2 Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Sulfolobus tokodaii
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1.14.13.B28
preliminary BRENDA-supplied EC number
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styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released
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styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
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P450st
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SwissProt
brenda
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SwissProt
brenda
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styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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?
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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?
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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NADH
the initial rate of catalysis with NADH is slightly higher than with NADPH
NADPH
the initial rate of catalysis with NADH is slightly higher than with NADPH
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7
NADH
pH 7, 25°C, mutant enzyme delLL151-E156
13
NADH
pH 7, 25°C, wild-type enzyme
0.29
Styrene
pH 7, 25°C, wild-type enzyme
0.52
Styrene
pH 7, 25°C, mutant enzyme delLL151-E156
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0.000057 - 0.000061
Styrene
0.000076
NADH
pH 7, 25°C, wild-type enzyme
0.000079
NADH
pH 7, 25°C, mutant enzyme delLL151-E156
0.000057
Styrene
pH 7, 25°C, mutant enzyme delLL151-E156
0.000061
Styrene
pH 7, 25°C, wild-type enzyme
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43000
F-G loop deletion mutant enzyme delLL151-E156
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vapour diffusion method, X-ray crystallography at a resolution of 1.94 A reveals a sufficiently large heme pocket for NAD(P)H binding and a novel contiguous channel from the active site to bulk solvent in the distal heme pocket. The mutant shows a higher affinity for NADH compared with the wild-type because the mutant has a more widely open distal pocket for NAD(P)H binding
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wild-type enzyme and F-G loop deletion mutant enzyme delLL151-E156, overexpression in Escherichia coli
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delL151-E156
the Km value of the mutant is about 2times lower than that of the wild-type.
delL151-E156
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the Km value of the mutant is about 2times lower than that of the wild-type.
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CP119_SULTO
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
367
42324
Swiss-Prot
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Matsumura, H.; Matsuda, K.; Nakamura, N.; Ohtaki, A.; Yoshida, H.; Kamitori, S.; Yohda, M.; Ohno, H.
Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH
Metallomics
3
389-395
2011
Sulfolobus tokodaii (Q972I2), Sulfolobus tokodaii 7 (Q972I2)
brenda
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