1.14.15.1: camphor 5-monooxygenase
This is an abbreviated version!
For detailed information about camphor 5-monooxygenase, go to the full flat file.
Word Map on EC 1.14.15.1
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1.14.15.1
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heme
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ferrous
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substrate-free
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camphor-bound
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substrate-bound
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low-spin
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high-spin
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dioxygen
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p450terp
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soret
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chloroperoxidase
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p450eryf
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self-sufficient
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adrenodoxin
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aromaticivorans
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monoxygenase
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novosphingobium
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monooxygenation
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ferryl
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thiolate-ligated
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i-helix
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oxyferrous
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analysis
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synthesis
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electron-electron
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biotechnology
- 1.14.15.1
- heme
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ferrous
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substrate-free
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camphor-bound
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substrate-bound
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low-spin
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high-spin
- dioxygen
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p450terp
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soret
- chloroperoxidase
- p450eryf
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self-sufficient
- adrenodoxin
- aromaticivorans
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monoxygenase
- novosphingobium
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monooxygenation
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ferryl
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thiolate-ligated
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i-helix
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oxyferrous
- analysis
- synthesis
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electron-electron
- biotechnology
Reaction
Synonyms
2-bornanone 5-exo-hydroxylase, bornanone 5-exo-hydroxylase, CamC, camphor 5-exo-hydroxylase, camphor 5-exo-methylene hydroxylase, camphor 5-exohydroxylase, camphor 5-hydroxylase, Camphor 5-monooxygenase, camphor hydroxylase, camphor hydroxylase cytochrome P450cam, camphor methylene hydroxylase, camphor monooxygenase, class I cytochrome P450, CYP101, CYP101A1, CYP101B1, CYP101C1, CYP101D1, CYP101D2, CYP111A2, Cyt P450cam, cytochrome P-450-CAM, cytochrome P450 cam, cytochrome P450(cam), cytochrome p450cam, cytochrome P450cam monooxygenase, d-camphor monooxygenase, D-camphor-exo-hydroxylase, haem mono-oxygenase CYP101, methylene hydroxylase, methylene monooxygenase, moe, oxygenase, camphor 5-mono-, P450cam, P450cam monooxygenase, P450tcu
ECTree
1.14.15.1 camphor 5-monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.15.1 - camphor 5-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L253V
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme, crystal structure analysis of mutant enzyme with bound substrate
M98F
site-directed mutagensis, the mutant shows 85% reduced activity compared to the wild-type enzyme, crystal structure analysis of mutant enzyme with bound substrate
Y96A
site-directed mutagensis, the mutant shows increased affinity for hydrocarbon substrates including adamantane, cyclooctane, hexane and 2-methylpentane, the monooxygenase activity of the mutant towards alkane substrates is enhanced compared to the wild-type enzyme, crystal structure analysis of mutant enzyme with bound substrate
C136S
site-directed mutagenesis, putidaredoxin binding compared to wild-type
C285S
site-directed mutagenesis, putidaredoxin binding compared to wild-type
C334A
C357M
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site-directed mutagenesis, comparison of the mutant structure to the wild-type one
C357U
C357U/R365L/E366Q
site-directed mutagenesis, structural, electronic, and catalytic properties of cytochrome P450cam are subtly altered when the cysteine that coordinates to the heme iron is replaced with a selenocysteine, mapping of the effects of the sulfur-to-selenium substitution on the individual steps of the catalytic cycle. The more electron-donating selenolate ligand has only negligible effects on substrate, product, and oxygen binding, electron transfer, catalytic turnover, and coupling efficiency. Off-pathway reduction of oxygen to give superoxide is the only step significantly affected by the mutation. Incorporation of selenium accelerates this uncoupling reaction approximately 50fold compared to sulfur, but because the second electron transfer step is much faster, the impact on overall catalytic turnover is minimal. Quantum mechanical calculations, overview. Steady-state kinetic analysis revealed that the selenocysteine substitution has essentially no effect on the specific catalytic activity or the binding interaction with the electron donor Pdx, as both kcat and KM,Pdx are very similar for wild-type and mutant enzymes
C58S
site-directed mutagenesis, putidaredoxin binding compared to wild-type
C85S
site-directed mutagenesis, putidaredoxin binding compared to wild-type
D251N
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site-directed mutagenesis, the mutant shows altered conformation of the I helix groove and misses the catalytically important water molecules in the dioxygen complex leading to lower catalytic activity and slower proton transfer to the dioxygen ligand compared to the wild-type enzyme
D38A
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site-directed mutagenesis, the mutant shows altered electron transfer activity with higher Kd values for ferric P450cam and about 20% of the first electron transferring ability compared to the wild-type enzyme, the mutant forms a complex with 1,3-dimethoxy-5-methyl-1,4-benzoquinone
D38N
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site-directed mutagenesis, the mutant shows altered electron transfer activity with higher Kd values for ferric P450cam and about 20% of the first electron transferring ability compared to the wild-type enzyme
D97F/P122L/Q183L/L244Q
mutant isolated by Sequence Saturation Mutagenesis, converts 3-chloroindole to isatin
E14C/S29C/C85S/C73S
site-directed mutagenesis, putidaredoxin binding compared to wild-type
E156G/V247F/V253G/F256S
mutant isolated by Sequence Saturation Mutagenesis, shows the highest maximal velocity in the conversion of 3-chloroindole to isatin
E195C/A199C/C334A
site-directed mutagenesis, substrate and cofactor binding of the mutant compared to the wild-type, overview
F87A/Y96F
F87L/Y96F
F87W/Y96F/L244A
enhanced binding and oxidation of (+)-alpha-pinene, production of 86% (+)-cis-verbenol + 5% (+)-verbenone
F87W/Y96F/L244A/V247L
enhanced binding and oxidation of (+)-alpha-pinene
F87W/Y96F/V247L
G120A/Y179H/G248S/D297H
mutant isolated by Sequence Saturation Mutagenesis, converts 3-chloroindole to isatin
G248E
low catalytic activity, incubation with camphor, putidaredoxin reductase, and NADH results in partial covalent binding of heme to protein, pronase digestion of heme-bound protein releases 5-hydroxyheme
G326A
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site-directed mutagenesis in order to decrease the flexibility of the polypeptide at that point, spin state fractions with different substrates and compared to the wild-type enzyme. The mutant shows 40% reduced activity compared to the wild-type enzyme
G60S/Y75H
mutant isolated by Sequence Saturation Mutagenesis, shows highest Km/kcat values for the conversion of 3-chloroindole to isatin
G93C/K314R/L319M
mutant isolated by Sequence Saturation Mutagenesis, converts 3-chloroindole to isatin
I396A
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
I396G
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
I396V
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
L244A/C334A
site-directed mutagenesis, mutation C334A prevents adventitious dimerization to facilitate crystallization but has no further effect on structure or activity of the enzyme, the L244A mutation leads to a highly increased Km and reduced activity for imidazole, but not for for 1-methylimidazole, and altered binding of imidazole to the active site and the active site heme involving residue Val247, overview
L244F/V247L
site-directed mutagenesis, the mutant exhibits moderate to high R-selectivity toward ethylmethylbenzene substrates and shows a narrow width of the binding pocket
L244N/V247L
site-directed mutagenesis, the mutant displays the highest S-selectivity toward substrates 1-ethyl-2-methylbenzene and 1-ethyl-3-methylbenzene, and low R-selectivity toward 1-ethyl-4-methylbenzene and shows a narrow width of the binding pocket
L358P
M184V/T185F
site-directed mutagenesis, the mutation introduces changes above the heme plane, prefers S-orientation of 1-ethyl-4-methylbenzene in the binding pocket of mutant, enantioselectivities of 1-ethyl-2-methylbenzene and 1-ethyl-3-methylbenzene are similar to the wild-type enzyme
M395I
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
M96Y
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
N244L
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
P89I
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yields a mixture of both bound camphor orientations, that seen in putidaredoxin-free and that seen in putidaredoxin-bound CYP101. A mutation in CYP101 that destabilizes the cis conformer of the Ile-88-Pro-89 amide bond results in weaker binding of putidaredoxin
Q227C
Q272C
R365L/E366Q
R66A
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site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme
R66E
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site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme
S190C
S190D
does not show any significant change in the rate constants of the substrate association, has almost no effect on the activation energy of substrate binding to the enzyme
S48C
T101M
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 89:11
T101M/T185F/V247M
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 87:13
T101V
site-directed mutagenesis, the mutant shows decreased thermal stability of the heme active site and reaction intermediates in the reaction, equilibrium unfolding compared to the wild-type enzyme
T185F
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 78:22
T185L
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 80:20
T185V
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 74:26
T192E
rate constants of the substrate association is much lower compared to the wild-type, activation energy for the substrate association is significantly higher in the T192E mutant compared to the S190D mutant or the wild-type enzyme
T252A
T252N
has comparable turnover number but higher Km value relative to the wild-type enzyme, due to a decrease in the camphor binding affinity, non-productive H2O2 generation is negligible
T252N/V253T
has comparable turnover number but higher Km value relative to the wild-type enzyme, due to a decrease in the camphor binding affinity, non-productive H2O2 generation is negligible
T297D
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
T56A/N116H/D297N
mutant isolated by Sequence Saturation Mutagenesis, shows highest Km/kcat values for the conversion of 3-chloroindole to isatin
V247A
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 87:13
V247M
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 83:17
V295I
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ratio of (R)- to (S)-1-phenylethanol produced from ethylbenzene is 76:24
V87F
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
W106A
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site-directed mutagenesis, the mutant shows altered electron transfer activity with higher Kd values for ferric P450cam and about 20% of the first electron transferring ability compared to the wild-type enzyme
W106F
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site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme
Y179H
mutant isolated by Sequence Saturation Mutagenesis, converts 3-chloroindole to isatin
Y29F
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the cis conformer is destabilized by the absence of the hydrogen bond between the carbonyl oxygen of Ile-88 and the Tyr-29 hydroxyl group
Y33A
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site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme
Y33F
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site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme
Y75F
Y96A
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
Y96C
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
Y96C/C334A
site-directed mutagenesis, substrate recognition and binding compared to the wild-type, conformational selection mechanism
Y96F
Y96F/C334A
site-directed mutagenesis, substrate recognition and binding compared to the wild-type, conformational selection mechanism
Y96F/L244A/V247L
enhanced binding and oxidation of (+)-alpha-pinene, production of 55% (+)-cis-verbenol + 32% (+)-verbenone
Y96F/Y75F
Y96G
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
Y96M
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
Y96N/C334A
site-directed mutagenesis, substrate recognition and binding compared to the wild-type, conformational selection mechanism
Y96Q
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
Y96S
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
Y96T
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site-directed mutagenesis, the mutant gains the ability to hydroxylate indole to 3-hydroxyindole
C357U
C357U/R365L/E366Q
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site-directed mutagenesis, structural, electronic, and catalytic properties of cytochrome P450cam are subtly altered when the cysteine that coordinates to the heme iron is replaced with a selenocysteine, mapping of the effects of the sulfur-to-selenium substitution on the individual steps of the catalytic cycle. The more electron-donating selenolate ligand has only negligible effects on substrate, product, and oxygen binding, electron transfer, catalytic turnover, and coupling efficiency. Off-pathway reduction of oxygen to give superoxide is the only step significantly affected by the mutation. Incorporation of selenium accelerates this uncoupling reaction approximately 50fold compared to sulfur, but because the second electron transfer step is much faster, the impact on overall catalytic turnover is minimal. Quantum mechanical calculations, overview. Steady-state kinetic analysis revealed that the selenocysteine substitution has essentially no effect on the specific catalytic activity or the binding interaction with the electron donor Pdx, as both kcat and KM,Pdx are very similar for wild-type and mutant enzymes
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R365L/E366Q
M96Y
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
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N244L
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
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T297D
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
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V87F
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site-directed mutagenesis, the substrate specificity is altered compared to the wild-type enzyme
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additional information
C334A
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identical with the wild-type monomer in terms of optical spectra, camphor-binding and turnover
C334A
spectroscopically and enzymatically identical to wild-type, but does not form dimers in solution
C334A
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is identical spectroscopically and enzymatically to wild-type but does not dimerize in solution at high concentrations
C334A
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mutant, that is spectroscopically and enzymatically identical to wild-type CYP101 enzyme, but does not form dimers in solution, and so is more suitable for solution NMR studies than wild-type enzyme
C334A
the mutation of P450cam increases the protein stability compared to the wild-type enzyme
C334A
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the mutation of P450cam increases the protein stability compared to the wild-type enzyme
C334A
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site-directed mutagenesis, the C334A mutant is spectroscopically and enzymatically identical to the wild type but does not form dimers in solution, and so is more suitable for NMR structure analysis than the wild type enzyme
C334A
site-directed mutagenesis, the mutation reduces protein aggregation, but has no effect on catalytic activity
C357U
site-directed mutagenesis, selenocysteine increases the affinity for oxygen 3-4-fold and accelerates the formation of superoxide 50fold, but the net effect of the C357U mutation on substrate hydroxylation is minimal because the second electron transfer step is much faster than superoxide formation under normal turnover conditions. As a consequence, selenocysteine is an excellent surrogate for the proximal cysteine in P450cam, maintaining both high monooxygenase activity and coupling efficiency
C357U
site-directed mutagenesis, the engineered gene contains the requisite UGA codon for selenocysteine, the sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2fold, whereas substrate oxidation becomes partially uncoupled from electron transfer. The structure of mutant C357U, including the active site, is very similar to that of wild-type enzyme and mutant R365L/E366Q. The specific activity of the selenoenzyme mutant C357U is approximately half that of the mutant R365L/E366Q, which is 2fold less active than the wild-type enzyme
F87W/Y96F/V247L
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enhanced activity for oxidation of 1,3,5-trichlorobenzene or (+)-alpha-pinene, compared to wild-type, analysis of active-site structure, crystallization
L358P
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stereo- and regioselectivity for d-camphor hydroxylation unchanged
L358P
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in absence of putidaredoxin, mutant shows ring-current signals typical for wild-type enzyme in presence of putidaredoxin, heme-environment of mutant mimics that of the putidaredoxin-bound wild-type, mutant accepts nonphysiological electron donors dithionite and ascorbic acid
L358P
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site-directed mutagenesis, spin-state equilibrium in the L358P mutant is more sensitive to K+ than the wild-type enzyme
Q227C
site-directed mutagenesis, putidaredoxin binding compared to wild-type
Q272C
site-directed mutagenesis, putidaredoxin binding compared to wild-type
R365L/E366Q
site-directed mutagenesis, the structure of mutant R365L/E366Q is very similar to that of wild-type enzyme and mutant C357U. The specific activity of the selenoenzyme mutant C357U is approximately half that of the mutant R365L/E366Q, which is 2fold less active than the wild-type enzyme
S190C
mutation used for double electron-electron resonance studies. Residues S48C and S190C are at opposite ends of the substrate access channel to provide a longer distance measurement
S190C
site-directed mutagenesis, putidaredoxin binding compared to wild-type
S48C
mutation used for double electron-electron resonance studies. Residues S48C and S190C are at opposite ends of the substrate access channel to provide a longer distance measurement
S48C
site-directed mutagenesis, putidaredoxin binding compared to wild-type
T252A
about 5% of wild-type activity, similar spectra for oxyferrous mutant and wild-type except for Soret band position blue shifts. Epoxidation substrate 5-methylenylcamphor has a anomalous binding mode for the mutant
T252A
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site-directed mutagenesis, the mutant does not show altered conformation of the I helix groove and the catalytically important water molecules in the dioxygen complex
T252A
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site-sirected mutagenesis, comparison of substrate binding properties to the wild-type enzyme, overview
T252A
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the mutant can epoxidize olefins like 5-methylenyl-camphor, but is ineffective in camphor hydroxylation
T252A
non-productive H2O2 generation is dominant, does not oxidize camphor, substrate binding affinity is similar to that of the wild-type enzyme
T252A
mutant displays an additional coupling pathway responsible for the epoxidation of 5-methylenylcamphor. During the reaction, camphor cannot prevent H2O2 release and hence the T252A mutant does not oxidize camphor
Y75F
the mutant shows an altered active site structure influencing catalysis
Y75F
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reaction with meta-chloroperbenzoic acid at 25°C, pH 8.0, is similar to that with the Y96F variant, although slightly more Cpd I (and possibly some Cpd ES) is present
Y96F
the mutant shows an altered active site structure influencing catalysis
Y96F
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reaction with peracetic acid at pH 8.0, 25°C, is similar to that with meta-chloroperbenzoic acid, except that even with 2.4 mM peracetic acid, all steps are slower than those with 0.150 mM meta-chloroperbenzoic acid
Y96F
site-directed mutagenesis, population and dynamics of the conformational states are largely unaltered by the Y96F mutation compared to the wild-type enzyme
Y96F/Y75F
the mutant shows an altered active site structure influencing catalysis
Y96F/Y75F
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mutants produce changes in hydrogen bonding patterns and increase hydrophobicity that affect the ratio of heterolytic to homolytic pathways in reactions with cumene hydroperoxide, resulting in a shift of this ratio from 84/16 for wild-type to 72/28 for the Y96F/Y75F double mutant
C357U
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site-directed mutagenesis, selenocysteine increases the affinity for oxygen 3-4-fold and accelerates the formation of superoxide 50fold, but the net effect of the C357U mutation on substrate hydroxylation is minimal because the second electron transfer step is much faster than superoxide formation under normal turnover conditions. As a consequence, selenocysteine is an excellent surrogate for the proximal cysteine in P450cam, maintaining both high monooxygenase activity and coupling efficiency
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C357U
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site-directed mutagenesis, the engineered gene contains the requisite UGA codon for selenocysteine, the sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2fold, whereas substrate oxidation becomes partially uncoupled from electron transfer. The structure of mutant C357U, including the active site, is very similar to that of wild-type enzyme and mutant R365L/E366Q. The specific activity of the selenoenzyme mutant C357U is approximately half that of the mutant R365L/E366Q, which is 2fold less active than the wild-type enzyme
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R365L/E366Q
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site-directed mutagenesis, the structure of mutant R365L/E366Q is very similar to that of wild-type enzyme and mutant C357U. The specific activity of the selenoenzyme mutant C357U is approximately half that of the mutant R365L/E366Q, which is 2fold less active than the wild-type enzyme
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additional information
substitutions at Tyr96, Met98 and Leu253 in CYP101D2 analogously to closely related CYP101A1 from Pseudomonas putida, reduce both the spin state shift on camphor binding and the camphor oxidation activity
additional information
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substitutions at Tyr96, Met98 and Leu253 in CYP101D2 analogously to closely related CYP101A1 from Pseudomonas putida, reduce both the spin state shift on camphor binding and the camphor oxidation activity
additional information
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a facile way to significantly enhance the catalytic efficiency of the P450cam system by the coupling of its native electron transfer system with enzymatic NADH regeneration catalyzed by glycerol dehydrogenase in Escherichia coli whole cell biocatalysts, production of (+)-exo-5-hydroxycamphor and 5-keto-camphor, overview
additional information
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construction of a catalytically active recombinant Escherichia coli whole cell biocatalyst harboring a cytochrome P450cam monooxygenase system from Pseudomonas putida coupled with enzymatic cofactor putidaredoxin mutant C73S/C85S regeneration, the cofactor mutant is 2fold more effective than the wild-type putidaredoxin
additional information
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construction of the deletion mutant DELTA106, the mutant shows reduced electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme
additional information
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establishment of a functional CYP101-system in a cell-like aqueous compartment build by a stable water-oil emulsion with the non-ioninc surfactant tetraethylene glycol dodecyl ether in micro-scale, the enzyme is not active in an organic-aqueous biphasic system, e.g. with etahnol or glycol, incorporating an NADH-regeneration system using recombinant His-tagged bacterial glycerol dehydrogenase, method optimization, overview
additional information
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in contrast to the wild-type, the more hydrophobic sites of the Tyr-to-Phe variants, compared to that of wild-type, favor homolysis more strongly and lead to considerable fractions of the Cpd II like species in reactions with peracids, especially at higher pH
additional information
removal of heme-7-propionate decreases the (+)-camphor affinity by approximately 3fold, but exerts less of an influence on the other steps of the catalytic cycle of the monooxygenation reaction catalyzed by P450cam, does not exert an influence on the structure and electronic properties of the heme
additional information
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establishment of an in vitro screening system for P450cam selecting variants by the activity on NADH
additional information
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generation of a G327 insertion mutant in order to determine whether the length of the helix played a role in the sensitivity of the K' helix to substrate, the insertion mutant fails to express
additional information
construction of a fusion enzyme composed of enzyme P450cam and putidaroxin reductase, i.e. P450cam-PdR, kinetic model based on two-site binding of putidaredoxin by P450cam-PdR and inactive dimer formation of the fusion protein. Fusion co-expression with putidaredoxin results in a functional system with in vivo camphor oxidation activity comparable to the wild-type system , but P450cam-PdR is a class I P450 fusion protein that exhibits significantly more favorable catalytic behavior than that of the wild-type system. Further oxidation of 5-exo-hydroxycamphor to 5-oxo-camphor by the fusion enzyme is 39% lower than for the native system
additional information
enantioselectivity of a library of active-site mutants of chimeric P450cam-RhFRed towards the benzylic hydroxylation of structurally related regioisomers of ethylmethylbenzene, computational molecular modeling, overview
additional information
interaction analysis of enzyme wild-type and mutant (D125A, H352A, and H361A) proteins with putidaredoxxin wild-type and mutant (Y33A, S42A, and S44A) proteins, kinetics, overview
additional information
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establishment of an in vitro screening system for P450cam selecting variants by the activity on NADH
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