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(+)-alpha-pinene + putidaredoxin + O2
(+)-cis-verbenol + (+)-myrtenol + (+)-verbenone + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(+)-alpha-pinene + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-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
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
(+)-exo-5-hydroxycamphor + reduced putidaredoxin + O2
5-oxocamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(1R)-5,5-difluorocamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(1R)-5-exo-methoxycamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(1R)-5-methylenylcamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(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
-
Substrates: -
Products: -
?
(1R)-camphor N-methyl imine + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-camphor oxime + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-endo-borneol allyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-endo-borneol methyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-endo-borneol propyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-iso-borneol methyl ether + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(1R)-norcamphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(1S)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(4S)-limonene + putidaredoxin + O2
?
-
Substrates: the 7-position is the major site of hydroxylation by P450cam
Products: -
?
(R)-2-ethylhexanol + reduced putidaredoxin + O2
(R)-2-ethylhexanoic acid + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
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
-
Substrates: -
Products: ratio: 50:13:15:8
?
(R)-exo-5-hydroxycamphor + O2 + reduced putidaredoxin
2,5-diketocamphane + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(S)-2-ethylhexanol + reduced putidaredoxin + O2
(S)-2-ethylhexanoic acid + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
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
-
Substrates: the (S)-isomer is turned over 1.4times faster than the (R)-isomer
Products: ratio: 15:53:28:10
?
1,2,4,5-tetrachlorobenzene + putidaredoxin + O2
2,3,5,6-tetrachlorophenol + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
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-
-
Substrates: 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
Products: 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
-
Substrates: -
Products: -
?
1,3,5-trichlorobenzene + putidaredoxin + O2
2,4,6-trichlorophenol + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
1,3,5-trichlorobenzene + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
1,3-dichlorobenzene + putidaredoxin + O2
2,6-dichlorophenol + 2,4-dichlorophenol + 2,5-dichlorophenol + 2,3-dichlorophenol + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
1,4-dichlorobenzene + putidaredoxin + O2
2,5-dichlorophenol + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
1-dehydrocamphor + putidaredoxin + O2
exo-5,6-epoxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
1-ethyl-2-methylbenzene + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: the S-enantiomer is preferred by the wild-type enzyme
Products: -
?
1-ethyl-3-methylbenzene + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: the S-enantiomer is preferred by the wild-type enzyme
Products: -
?
1-ethyl-4-methylbenzene + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: the S-enantiomer is preferred by the wild-type enzyme
Products: -
?
1-methylimidazole + O2 + reduced putidaredoxin
?
Substrates: -
Products: -
?
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
Substrates: -
Products: 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 + ?
Substrates: no substrate of wild-type, substrate of mutants E156G/V247F/V253G/F256S, T56A/N116H/D297N and G60S/Y75H
Products: -
?
3-chloroperbenzoic acid + O2 + reduced putidaredoxin
?
5,5-difluorocamphor + O2 + reduced putidaredoxin
?
-
Substrates: -
Products: -
?
5,5-difluorocamphor + putidaredoxin + O2
5,5-difluoro-9-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
5-exo-bromocamphor + putidaredoxin + O2
5-ketocamphor + oxidized putidaredoxin + Br- + H2O
-
Substrates: (+)- and (-)-enantiomer
Products: -
?
5-methylenyl-camphor + O2 + reduced putidaredoxin
?
adamantane + reduced ferreredoxin + O2
1-adamantol + 2-adamantol + oxidized ferredoxin + H2O
Substrates: -
Products: 98% 1-adamantol + 2% 2-adamantol for the wild-type enzyme, 97% + 3% for the mutant Y96A
?
adamantanone + O2 + reduced putidaredoxin
?
-
Substrates: -
Products: -
?
adamantanone + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
adamantenone + reduced putidaredoxin + O2
?
-
Substrates: -
Products: -
?
benzo[a]pyrene + putidaredoxin + O2
3-hydroxybenzo[a]pyrene + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
beta-ionone + O2 + reduced putidaredoxin
4-hydroxy-beta-ionone + oxidized putidaredoxin + H2O
camphane + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
cyclooctane + reduced ferreredoxin + O2
cyclooctanol + cyclooctanone + oxidized ferredoxin + H2O
Substrates: -
Products: 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
Substrates: -
Products: -
?
ethylbenzene + putidaredoxin + O2
1-phenylethanol + oxidized putidaredoxin + H2O
-
Substrates: at 5% of the reaction with (+)-camphor
Products: ratio of (R)- to (S)-1-phenylethanol produced depends on mutant form
?
fluoranthene + putidaredoxin + O2
3-fluoranthol + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
hexane + reduced ferreredoxin + O2
hexan-2-ol + hexan-3-ol + oxidized ferredoxin + H2O
Substrates: -
Products: 56% hexan-2-ol + 44% hexan-3-ol for the wild-type enzyme and mutant Y96A
?
imidazole + O2 + reduced putidaredoxin
?
Substrates: -
Products: -
?
indole + O2 + reduced putidaredoxin
3-hydroxyindole + oxidized putidaredoxin + H2O
-
Substrates: no substrate of the wild-type enzyme, but a good substrate for Y96 mutants, mutant screening, overview
Products: 3-hydroxyindole undergoes spontaneous air oxidation to produce the insoluble dye indigo
?
isoborneol + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
linalool + O2 + reduced putidaredoxin
8-hydroxy-linalool + oxidized putidaredoxin + H2O
norcamphor + O2 + reduced putidaredoxin
?
-
Substrates: -
Products: -
?
norcamphor + reduced putidaredoxin + O2
?
-
Substrates: -
Products: -
?
norcamphor + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
peracetic acid + O2 + reduced putidaredoxin
?
phenanthrene + putidaredoxin + O2
1-phenanthrol + 2-phenanthrol + 3-phenanthrol + 4-phenanthrol + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
pyrene + putidaredoxin + O2
1-pyrenol + 2-pyrenol + 1,6-pyrenequinone + 1,8-pyrenequinone + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
thiocamphor + reduced putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
additional information
?
-
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: CYP101D1, CYP101D2
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: CYP101D1, CYP101D2
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
671535, 672100, 672115, 672742, 672760, 673037, 673071, 674152, 674438, 674474, 674516, 674959, 675234, 676280 Substrates: -
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: analysis of protein-protein interactions between enzyme and cofactor, overview
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: mechanism of camphor hydroxylation incorporating an NADH-regeneration system, overview
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: regio- and stereoselective C-H bond hydroxylation, rebound mechanism, overview
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: regio- and stereospecific hydroxylation
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: second reductive step of the mechanism of interaction and electron transfer, overview
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: wild-type enzyme, but not mutant T252A
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: conformational change in CYP101 upon binding of putidaredoxin that re-orients bound camphor appropriately for hydroxylation
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: 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
Products: -
?
(+)-camphor + O2 + reduced putidaredoxin
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
347690, 347691, 347692, 347693, 347694, 347695, 347697, 347701, 347702, 347704, 347705, 347706, 347707, 347708, 347710, 347713 Substrates: -
Products: i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: the (+)- and (-)-enantiomers serve as substrates
Products: i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: when deuterated at either 5-exo- or 5-endo-position, only 5-exo-hydroxycamphor is the product
Products: i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + putidaredoxin + O2
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: i.e. (+)-exo-5-hydroxycamphor
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
Substrates: -
Products: 99% 5-exo-hydroxycamphor by wild-type enzyme and 92% by Y96A mutant
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
Substrates: substrate of CYP101D1 and CYP101D2
Products: -
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + reduced ferredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized ferredoxin + H2O
Substrates: substrate of CYP101D1 and CYP101D2
Products: -
?
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
Substrates: 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
Products: -
?
(+)-camphor + reduced putidaredoxin + NADH + H+ + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
r
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: 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
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
Substrates: -
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
-
Substrates: under low oxygen conditions borneol is formed instead of 5-ketocamphor
Products: -
?
(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
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Substrates: 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)
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(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
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Substrates: under low oxygen conditions
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(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
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Substrates: under low oxygen conditions borneol is formed instead of 5-ketocamphor
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(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
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Substrates: 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)
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(+)-camphor + reduced putidaredoxin + O2
borneol + oxidized putidaredoxin + H2O
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Substrates: under low oxygen conditions
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(1R)-(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
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(1R)-(+)-camphor + reduced putidaredoxin + O2
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
Substrates: -
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(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
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Substrates: putidaredoxin transfers electrons from NADH to P450cam in a coupled assay method
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(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
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Substrates: putidaredoxin transfers electrons from NADH to P450cam
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(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
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Substrates: putidaredoxin transfers electrons from NADH to P450cam in a coupled assay method
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(1R)-camphor + putidaredoxin + O2
5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O
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Substrates: putidaredoxin transfers electrons from NADH to P450cam
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(1R)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
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Substrates: -
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(1R)-camphor + putidaredoxin + O2
? + oxidized putidaredoxin + H2O
Substrates: -
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1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
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Substrates: -
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1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
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Substrates: -
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1,2-campholide + putidaredoxin + O2
5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
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Substrates: -
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2-adamantanone + O2 + reduced putidaredoxin
5-hydroxy-2-adamantanone + oxidized putidaredoxin + H2O
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Substrates: CYP101D1 and CYP101D2
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2-adamantanone + O2 + reduced putidaredoxin
5-hydroxy-2-adamantanone + oxidized putidaredoxin + H2O
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Substrates: CYP101D1 and CYP101D2
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3-chloroperbenzoic acid + O2 + reduced putidaredoxin
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Substrates: compound I, ferryl iron plus a porphyrin pi-cation radical (Fe(IV)=O/Por(+)), and compound ES, Fe(IV)=O/Tyr(), in reactions of substrate-free ferric enzyme with 3-chloroperbenzoic acid, compound ES arises by intramolecular electron transfer from nearby tyrosines to the porphyrin pi-cation radical of compound I, active site changes influence electron transfer from nearby tyrosines and affect formation of intermediates, the tyrosyl radical is assigned to Tyr96 for wild type or to Tyr75 for the Y96F variant, overview
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3-chloroperbenzoic acid + O2 + reduced putidaredoxin
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Substrates: reaction mechanism of substrate-free ferric cytochrome P450cam, via FeIV-O plus porphyrin Pi-cation radical, overview
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5-methylenyl-camphor + O2 + reduced putidaredoxin
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Substrates: -
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5-methylenyl-camphor + O2 + reduced putidaredoxin
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Substrates: wild-type enzyme and mutant T252A, in absence of the primary oxidant species of P450, the precursor species FeOOH can effect double bond activation of 5-methylenyl-camphor initiated by a homolytic cleavage of the O-O-bond and formation of an OH radical bound to the secondary oxidant by hydrogen bonding interaction, overview
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beta-ionone + O2 + reduced putidaredoxin
4-hydroxy-beta-ionone + oxidized putidaredoxin + H2O
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Substrates: CYP101C1 and CYP101B1. CYP101C1 oxidizes beta-ionone to 4-hydroxy-beta-ionone (75%) with one other, unidentified product. This latter compound is the major product of beta-ionone oxidation by CYP101B1 (90%) where 4-hydroxy-beta-ionone is the minor product (10%)
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beta-ionone + O2 + reduced putidaredoxin
4-hydroxy-beta-ionone + oxidized putidaredoxin + H2O
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Substrates: CYP101C1 and CYP101B1. CYP101C1 oxidizes beta-ionone to 4-hydroxy-beta-ionone (75%) with one other, unidentified product. This latter compound is the major product of beta-ionone oxidation by CYP101B1 (90%) where 4-hydroxy-beta-ionone is the minor product (10%)
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linalool + O2 + reduced putidaredoxin
8-hydroxy-linalool + oxidized putidaredoxin + H2O
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Substrates: CYP111A2 and CYP111A1
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linalool + O2 + reduced putidaredoxin
8-hydroxy-linalool + oxidized putidaredoxin + H2O
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Substrates: CYP111A2 and CYP111A1
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peracetic acid + O2 + reduced putidaredoxin
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Substrates: -
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peracetic acid + O2 + reduced putidaredoxin
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Substrates: reaction mechanism of substrate-free ferric cytochrome P450cam, via FeIV-O plus tyrosyl radical, overview
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additional information
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Substrates: substrate binding and activity data for wild-type CYP101D2 and variants with different substrates, gas chromatography analysis of products, overview
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additional information
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Substrates: substrate binding and activity data for wild-type CYP101D2 and variants with different substrates, gas chromatography analysis of products, overview
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additional information
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Substrates: -
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additional information
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Substrates: -
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additional information
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Substrates: effects of heme environment on the hydrogen abstraction reaction of camphor in catalysis, overview
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additional information
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Substrates: modelling of the hydroxylation of camphor using crystal structure, PDB code 1DZ9, and combined quantum mechanical/molecular mechanical method, heme propionate side chains are not involved in catalysis, Asp297 is important for the reaction mechanism, overview
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additional information
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Substrates: relative stability of dibromochloropropane and products, overview
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additional information
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Substrates: release of the substrate is caused both due to increased solubility of the substrate in solution in presence of alcohol and due to change in the tertiary structure of the active site of the enzyme, addition of alcohols to cytochrome P450cam causes a small change in the secondary structural elements but a significant change in the tertiary structural organization of the enzyme
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additional information
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Substrates: the properties and reactivity of the oxyheme and of both the primary and the annealed intermediates are modulated by a bound substrate, including alterations in the properties of the heme center, the presence of any alternative substrate increases the lifetime of hydroperoxoferri-P450cam no less than about 20fold, especially 5-methylenyl-camphor
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additional information
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Substrates: substrate specificities of wild-type and mutant enzymes, overview
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additional information
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Substrates: under conditions of low oxygen, Pseudomonas putida cells and the isolated P450cam reduce camphor to borneol, product analysis by GC-MS
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additional information
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Substrates: an additional coupling pathway transpires during H2O2 shunting of the cycle of wild-type P450cam and in mutant T252A. The reaction starts with the FeIII(O2H2) intermediate, which transforms to Cpd I via a O-O homolysis/H-abstraction mechanism. The substrate 5-methylenylcamphor prevents H2O2 release, while the protein controls the FeIII(O2H2) conversion to Cpd I by nailing through hydrogen-bonding interactionsthe conformation of the HO radical produced during O-O homolysis. This conformation prevents HO readical attack on the porphyrins meso position, as in heme oxygenase, and prefers H-abstraction from FeIVOH thereby generating H2O + Cpd I. Cpd I then performs substrate oxidations
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additional information
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Substrates: analysis of the molecular substrate recognition of wild-type and mutant P450cams by infrared (IR) spectroscopy, differing conformational heterogeneity in the active site of the P450cam variants and changes in heterogeneity upon binding of different substrates likely contribute to their variable affinities via a conformational selection mechanism, overview. Although P450cam is relatively specific for camphor, it also recognizes a number of small, camphor-like substrates, albeit with variable affinity. Substrate binding and active site structure, overview
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additional information
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Substrates: catalytic turnover in P450cam requires the enzymes putidaredoxin (Pdx) and putidaredoxin reductase (Pdr), which mediate electron transfer from NADH to heme, the process is tightly coupled to substrate hydroxylation
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additional information
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Substrates: comparison of substrate binding and catalytic ability of wild-type enzyme with putidareductase and putidaredoxin (ternary complex), and recombinant fusion enzyme P450cam-putidareductase with putidaredoxin, overview. The wild-type and mutant systems show comparable activity with camphor. Further oxidation of 5-exo-hydroxycamphor to 5-oxo-camphor by the fusion enzyme is 39% lower than for the native system
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additional information
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Substrates: enzyme 450cam binds camphor and converts from the closed to open conformation upon binding putidaredoxin, the binding thermodynamics of Pdx differ when the conformation of P450cam is held in different states, thermodynamic analysis, overview
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additional information
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Substrates: enzyme P450cam catalyzes the regioselective hydroxylation of d-camphor to 5-exo-hydroxycamphor. P450cam hydroxylates thiocamphor with a regioselectivity lower than camphor but higher than norcamphor. The high regioselectivity of camphor hydroxylation, the hydrogen bond (H-bond) between the camphor ketone and the side chain of active site residue Y96 influences the local electrostatics of the active site but has little effect on either the relative populations of conformational states or the nature of the energy landscapes within the conformations. Infrared spectrometric analysis of enzyme-substrate intercations, overview
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additional information
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