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Literature summary for 1.14.13.B28 extracted from

  • 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 (2011), Metallomics, 3, 389-395.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type enzyme and F-G loop deletion mutant enzyme delLL151-E156, overexpression in Escherichia coli Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
delL151-E156 the Km value of the mutant is about 2times lower than that of the wild-type. Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.29
-
Styrene pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii
0.52
-
Styrene pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii
7
-
NADH pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii
13
-
NADH pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
F-G loop deletion mutant enzyme delLL151-E156 Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii Q972I2
-
-
Sulfurisphaera tokodaii 7 Q972I2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sulfurisphaera tokodaii

Reaction

Reaction Comment Organism Reaction ID
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
styrene + NADH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii styrene epoxide + NAD+ + H2O
-
?
styrene + NADH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii 7 styrene epoxide + NAD+ + H2O
-
?
styrene + NADPH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii styrene epoxide + NADP+ + H2O
-
?
styrene + NADPH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii 7 styrene epoxide + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
P450st
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000057
-
Styrene pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii
0.000061
-
Styrene pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii
0.000076
-
NADH pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii
0.000079
-
NADH pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Sulfurisphaera tokodaii

Cofactor

Cofactor Comment Organism Structure
NADH the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii
NADPH the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii