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(+)-alpha-pinene + putidaredoxin + O2
(+)-cis-verbenol + (+)-myrtenol + (+)-verbenone + oxidized putidaredoxin + H2O
-
-
-
?
(+)-alpha-pinene + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(+)-camphor + reduced putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
(+)-exo-5-hydroxycamphor + reduced putidaredoxin + O2
5-oxocamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(1R)-5,5-difluorocamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
(1R)-5-exo-methoxycamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
(1R)-5-methylenylcamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
(1R)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
(1R)-camphor enol ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-camphor N-methyl imine + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-camphor oxime + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-endo-borneol allyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-endo-borneol methyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-endo-borneol propyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-iso-borneol methyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-norcamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
(1S)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
(4S)-limonene + putidaredoxin + O2
?
-
the 7-position is the major site of hydroxylation by P450cam
-
-
?
(R)-2-ethylhexanol + reduced putidaredoxin + O2
(R)-2-ethylhexanoic acid + oxidized putidaredoxin + H2O
-
-
-
-
r
(R)-3-ethylhexanol + putidaredoxin + O2
2-ethylhexanoic acid + 2-ethyl-1,2-hexanediol + 2-ethyl-1,3-hexanediol + 2-ethyl-1,4-hexanediol + oxidized putidaredoxin + H2O
-
-
ratio: 50:13:15:8
?
(R)-exo-5-hydroxycamphor + O2 + reduced putidaredoxin
2,5-diketocamphane + oxidized putidaredoxin + H2O
-
-
-
-
?
(S)-2-ethylhexanol + reduced putidaredoxin + O2
(S)-2-ethylhexanoic acid + oxidized putidaredoxin + H2O
-
-
-
-
r
(S)-3-ethylhexanol + putidaredoxin + O2
2-ethylhexanoic aicd + 2-ethyl-1,2-hexanediol + 2-ethyl-1,3-hexanediol + 2-ethyl-1,4-hexanediol + oxidized putidaredoxin + H2O
-
the (S)-isomer is turned over 1.4times faster than the (R)-isomer
ratio: 15:53:28:10
?
1,2,4,5-tetrachlorobenzene + putidaredoxin + O2
2,3,5,6-tetrachlorophenol + oxidized putidaredoxin + H2O
-
-
-
?
1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
1,2-dibromo-3-chloropropane + O2 + reduced putidaredoxin
1-bromo-3-chloroacetone + allyl chloride + H2O + putidaredoxin + Br-
-
dehalogenation, bromochloroacetone is the major conversion product when the incubation medium is saturated with oxygen, while allyl chloride is the sole product in the absence of oxygen
a number of bromochloropropene are also formed to a minor extent by an elimination mechanism, product determination
-
?
1,2-dichlorobenzene + putidaredoxin + O2
2,3-dichlorophenol + 3,4-dichlorophenol + oxidized putidaredoxin + H2O
-
-
-
?
1,3,5-trichlorobenzene + putidaredoxin + O2
2,4,6-trichlorophenol + oxidized putidaredoxin + H2O
-
-
-
?
1,3,5-trichlorobenzene + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
1,3-dichlorobenzene + putidaredoxin + O2
2,6-dichlorophenol + 2,4-dichlorophenol + 2,5-dichlorophenol + 2,3-dichlorophenol + oxidized putidaredoxin + H2O
-
-
-
?
1,4-dichlorobenzene + putidaredoxin + O2
2,5-dichlorophenol + oxidized putidaredoxin + H2O
-
-
-
?
1-dehydrocamphor + putidaredoxin + O2
exo-5,6-epoxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
1-ethyl-2-methylbenzene + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
the S-enantiomer is preferred by the wild-type enzyme
-
-
?
1-ethyl-3-methylbenzene + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
the S-enantiomer is preferred by the wild-type enzyme
-
-
?
1-ethyl-4-methylbenzene + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
the S-enantiomer is preferred by the wild-type enzyme
-
-
?
1-methylimidazole + O2 + reduced putidaredoxin
?
-
-
-
?
2-adamantanone + O2 + reduced putidaredoxin
5-hydroxy-2-adamantanone + oxidized putidaredoxin + H2O
3 2-methylpentane + 3 reduced ferreredoxin + O2
2-methyl-pentan-2-ol + 2-methyl-pentan-3-ol + 2-methyl-pentan-4-ol + 3 oxidized ferredoxin
-
52.5% 2-methyl-pentan-2-ol + 13% 2-methyl-pentan-3-ol, and 3% 2-methyl-pentan-4-ol for the wild-type enzyme, 5% + 12% + 30% for the mutant Y96A
-
?
3-chloroindole + O2 + reduced putidaredoxin
isatin + H2O + Cl- + oxidized putidaredoxin + ?
no substrate of wild-type, substrate of mutants E156G/V247F/V253G/F256S, T56A/N116H/D297N and G60S/Y75H
-
-
?
3-chloroperbenzoic acid + O2 + reduced putidaredoxin
?
5,5-difluorocamphor + O2 + reduced putidaredoxin
?
-
-
-
-
?
5,5-difluorocamphor + putidaredoxin + O2
5,5-difluoro-9-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
5-exo-bromocamphor + putidaredoxin + O2
5-ketocamphor + oxidized putidaredoxin + Br- + H2O
-
(+)- and (-)-enantiomer
-
?
5-methylenyl-camphor + O2 + reduced putidaredoxin
?
adamantane + reduced ferreredoxin + O2
1-adamantol + 2-adamantol + oxidized ferredoxin + H2O
-
98% 1-adamantol + 2% 2-adamantol for the wild-type enzyme, 97% + 3% for the mutant Y96A
-
?
adamantanone + O2 + reduced putidaredoxin
?
-
-
-
-
?
adamantanone + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
adamantenone + reduced putidaredoxin + O2
?
-
-
-
-
?
benzo[a]pyrene + putidaredoxin + O2
3-hydroxybenzo[a]pyrene + oxidized putidaredoxin + H2O
-
-
-
-
?
beta-ionone + O2 + reduced putidaredoxin
4-hydroxy-beta-ionone + oxidized putidaredoxin + H2O
camphane + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
cyclooctane + reduced ferreredoxin + O2
cyclooctanol + cyclooctanone + oxidized ferredoxin + H2O
-
99% cyclooctanol + 1% cyclooctanone for the wild-type enzyme, 97% + 3% for the mutant Y96A
-
?
DL-camphor + reduced putidaredoxin + NADH + H+ + O2
exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
-
-
-
?
ethylbenzene + putidaredoxin + O2
1-phenylethanol + oxidized putidaredoxin + H2O
-
at 5% of the reaction with (+)-camphor
ratio of (R)- to (S)-1-phenylethanol produced depends on mutant form
?
fluoranthene + putidaredoxin + O2
3-fluoranthol + oxidized putidaredoxin + H2O
-
-
-
-
?
hexane + reduced ferreredoxin + O2
hexan-2-ol + hexan-3-ol + oxidized ferredoxin + H2O
-
56% hexan-2-ol + 44% hexan-3-ol for the wild-type enzyme and mutant Y96A
-
?
imidazole + O2 + reduced putidaredoxin
?
-
-
-
?
indole + O2 + reduced putidaredoxin
3-hydroxyindole + oxidized putidaredoxin + H2O
-
no substrate of the wild-type enzyme, but a good substrate for Y96 mutants, mutant screening, overview
3-hydroxyindole undergoes spontaneous air oxidation to produce the insoluble dye indigo
-
?
isoborneol + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
linalool + O2 + reduced putidaredoxin
8-hydroxy-linalool + oxidized putidaredoxin + H2O
norcamphor + O2 + reduced putidaredoxin
?
-
-
-
-
?
norcamphor + reduced putidaredoxin + O2
?
-
-
-
-
?
norcamphor + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
peracetic acid + O2 + reduced putidaredoxin
?
phenanthrene + putidaredoxin + O2
1-phenanthrol + 2-phenanthrol + 3-phenanthrol + 4-phenanthrol + oxidized putidaredoxin + H2O
-
-
-
-
?
pyrene + putidaredoxin + O2
1-pyrenol + 2-pyrenol + 1,6-pyrenequinone + 1,8-pyrenequinone + oxidized putidaredoxin + H2O
-
-
-
-
?
thiocamphor + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
additional information
?
-
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
CYP101D1, CYP101D2
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
CYP101D1, CYP101D2
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
671535, 672100, 672115, 672742, 672760, 673037, 673071, 674152, 674438, 674474, 674516, 674959, 675234, 676280 -
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
terminal monooxygenase in a three-component camphor-hydroxylating system from Pseudomonas putida, the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
analysis of protein-protein interactions between enzyme and cofactor, overview
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
binding of camphor is strongly dependent on the concentration of alcohols, alcohol expels camphor out of the heme cavity of the enzyme by affecting tertiary structure of Cyt P450cam as well as by modifying the solubility properties of camphor in aqueous medium, overview
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
determination of appearance of transient intermediates at 3°C by double mixing rapid scanning stopped-flow spectroscopy, electron transfer from reduced putidaredoxin gives high spin deoxyferrous P-450, substrate-free enzyme also binds the cofactor, but the cofactor does not deliver the electrons to the substrate-free oxyferrous enzyme, binding structure of camphor-bound oxyferrous P450-CAM with reduced putidaredoxin, functional implications of the formation of the perturbed oxyferrous intermediate, overview
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
mechanism of camphor hydroxylation incorporating an NADH-regeneration system, overview
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
regio- and stereoselective C-H bond hydroxylation, rebound mechanism, overview
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
regio- and stereospecific hydroxylation
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
second reductive step of the mechanism of interaction and electron transfer, overview
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
wild-type dioxygen complex structure: high occupancy and a ordered structure of the iron-linked dioxygen and two 'catalytic' water molecules that form part of a proton relay system to the iron-linked dioxygen, Thr252 accepts a hydrogen bond from the hydroperoxy (Fe(III)-OOH) intermediate that promotes the second protonation on the distal oxygen atom, leading to O-O bond cleavage and compound I formation
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
wild-type enzyme, but not mutant T252A
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
the reduced enzyme exhibits lower-amplitude motions of secondary structural features than the oxidized enzyme on all of the time scales accessible, and these differences are more pronounced in regions of the enzyme involved in substrate access to the active site (B' helix and beta3 and beta5 sheets) and binding of putidaredoxin (C and L helices), the iron-sulfur protein that acts as the effector and reductant of CYP101 in vivo
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
though the active site of the enzyme resides deep inside the protein matrix, the substrate is recognized at the surface of the enzyme and directed towards the active site through the access channel. The threonine 192 that resides on the F-G loop and directed towards the putative substrate access channel of the enzyme, plays an important role in recognition of the substrate at the surface of the enzyme
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
conformational change in CYP101 upon binding of putidaredoxin that re-orients bound camphor appropriately for hydroxylation
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
ferric hydroperoxo complex, elusive reactive species of cytochrome P450cam, and the hydroxo intermediate (formed during camphor hydroxylation) in the catalytic cycle of cytochrome P450cam all have a doublet ground state which have a pronounced multiconfigurational character in the case of compound I and the hydroxo intermediate
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
the 7-propionate side chain plays a role in maintaining the high affinity of cytochrome P450cam for its substrate, the Asp297 and Gln322 residues are capable of undergoing a 7-propionate-associated conformational change in the protein interior
-
-
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
the Cpd II-like species is ineffective at hydroxylating camphor, but can be readily reduced by ascorbate to ferric P450cam, which can then bind camphor to form the high-spin heme
-
-
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
the (+)- and (-)-enantiomers serve as substrates
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
when deuterated at either 5-exo- or 5-endo-position, only 5-exo-hydroxycamphor is the product
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
-
-
-
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
-
99% 5-exo-hydroxycamphor by wild-type enzyme and 92% by Y96A mutant
-
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
substrate of CYP101D1 and CYP101D2
-
-
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
-
-
-
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
substrate of CYP101D1 and CYP101D2
-
-
?
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
-
-
-
?
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, overview
-
-
?
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
r
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
the enzyme shows regio- and stereospecific hydroxylation. Activation and cleavage of the oxygen molecule in the P450cam catalytic cycle is accompanied by two electron transfers from putidaredoxin. Ferric P450cam can accept the first electron from diverse chemical reductants and putidaredoxin homologues, but the second requires putidaredoxin as donor
-
-
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
under low oxygen conditions borneol is formed instead of 5-ketocamphor
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
the hydroxylation reaction proceeds via a catalytic cycle in which the reduction of dioxygen is coupled to the oxidation of the substrate. A key intermediate in the catalytic cycle is the iron-oxo species (Fe(IV)=O)
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
under low oxygen conditions
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
under low oxygen conditions borneol is formed instead of 5-ketocamphor
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
the hydroxylation reaction proceeds via a catalytic cycle in which the reduction of dioxygen is coupled to the oxidation of the substrate. A key intermediate in the catalytic cycle is the iron-oxo species (Fe(IV)=O)
-
-
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
under low oxygen conditions
-
-
?
(1R)-(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(1R)-(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
-
-
?
(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
-
putidaredoxin transfers electrons from NADH to P450cam in a coupled assay method
-
-
?
(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
-
putidaredoxin transfers electrons from NADH to P450cam
-
-
?
(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
-
putidaredoxin transfers electrons from NADH to P450cam in a coupled assay method
-
-
?
(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
-
putidaredoxin transfers electrons from NADH to P450cam
-
-
?
(1R)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
-
?
(1R)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
-
-
?
1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
-
-
-
?
1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
-
-
-
?
1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
-
-
-
?
1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
1.14.15.1 camphor 5-monooxygenase
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