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Information on EC 1.14.14.155 - 3,6-diketocamphane 1,2-monooxygenase
for references in articles please use BRENDA:EC1.14.14.155
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.155 3,6-diketocamphane 1,2-monooxygenase
IUBMB Comments
A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (–)-camphor. Requires a dedicated NADH—FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1,2]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
The expected taxonomic range for this enzyme is: Pseudomonas putida
- 1.14.14.155
- putida
- camphor
- flavin
-
ncimb
- ketone
-
two-component
-
bicyclic
- reductases
- norcamphor
-
supplier
-
requisite
- fad
- putidaredoxin
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biooxidation
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isofunctional
- synthesis
showSynonyms
3,6-dkcmo, 3,6-diketocamphane monooxygenase, type ii baeyer-villiger 3,6-diketocamphane monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3,6-diketocamphane 1,6-monooxygenase
3,6-diketocamphane lactonizing enzyme
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-
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3,6-diketocamphane monooxygenase
3,6-diketocamphane-monooxygenase
3,6-DKCMO
3,6-DKMO
camE36
DKCMO
type II Baeyer-Villiger 3,6-diketocamphane monooxygenase
additional information
3,6-diketocamphane 1,6-monooxygenase
-
different enzyme with similar biochemical properties, immunological cross-reactivity
3,6-diketocamphane 1,6-monooxygenase
-
isoform, which is probably a different enzyme
3,6-diketocamphane 1,6-monooxygenase
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isozyme, enantiocomplementary and isofunctional isozymes 2,5-DKCMO EC 1.14.15.2 and 3,6-DKCMO EC 1.14.15.x
3,6-diketocamphane 1,6-monooxygenase
Pseudomonas putida C1 / ATCC 17453
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different enzyme with similar biochemical properties, immunological cross-reactivity
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3,6-diketocamphane 1,6-monooxygenase
Pseudomonas putida C1 / ATCC 17453
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isoform, which is probably a different enzyme
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3,6-diketocamphane 1,6-monooxygenase
-
isoform, which is probably a different enzyme
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3,6-diketocamphane 1,6-monooxygenase
-
isozyme, enantiocomplementary and isofunctional isozymes 2,5-DKCMO EC 1.14.15.2 and 3,6-DKCMO EC 1.14.15.x
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3,6-DKCMO
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additional information
-
2 diketocamphane monooxygenases in Pseudomonas putida
additional information
-
lower regio- and enatioselectivity than isoform 2,5-diketocamphane-1,2-monooxygenase
additional information
-
lower regio- and enatioselectivity than isoform 2,5-diketocamphane-1,2-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(-)-bornane-2,5-dione + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
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-
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
mechanism
-
(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
catalysis of 2 mechanistically different types of biochemical reactions within the confines of the same active site
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
cubic space active site model, topography
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
isozyme, enantiocomplementary and isofunctional isozymes 2,5-DKCMO EC 1.14.15.2 and 3,6-DKCMO EC 1.14.15.x
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
higher activity in oxidation of sulfides to the corresponding sulfoxides than in lactonization of ketones
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
i.e. cyclopentaneacetic acid, 3-hydroxy-2,2,3-trimethyl-5-oxo, delta-lactone, reacts sponaneously to (2,2-dimethyl-5-oxo-cyclopent-3-en-1-yl)acetic acid
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
mechanism
-
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(-)-bornane-2,5-dione + reduced rubredoxin + O2 + FMNH2 = (-)-5-oxo-1,2-campholide + FMN + H2O
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Baeyer-Villiger reaction
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(-)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (-)-camphor. Requires a dedicated NADH---FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1,2]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
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CAS REGISTRY NUMBER
COMMENTARY
151616-60-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-bornane-2,5-dione + FMNH2 + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + FMN + H2O
(-)-bornanone + FMNH2 + O2
?
-
Substrates: i.e. (-)-camphor
Products: -
Products: -
?
2-cyclohexen-1-one + FMNH2 + O2
?
Substrates: 50% conversion
Products: -
Products: -
?
2-cyclopenten-1-one + FMNH2 + O2
?
Substrates: 48% conversion
Products: -
Products: -
?
3,5,5-trimethyl-2-cyclohexen-1-one + FMNH2 + O2
?
Substrates: 21% conversion
Products: -
Products: -
?
3-methyl-2-cyclohexen-1-one + FMNH2 + O2
?
Substrates: 20% conversion
Products: -
Products: -
?
3-methyl-2-cyclopenten-1-one + FMNH2 + O2
?
Substrates: 10% conversion
Products: -
Products: -
?
4-phenyl-2-butanone + FMNH2 + O2
?
Substrates: 48% conversion
Products: -
Products: -
?
acetophenone + FMNH2 + O2
?
Substrates: 80% conversion
Products: -
Products: -
?
cyclobutanone + FMNH2 + O2
?
Substrates: 13% conversion
Products: -
Products: -
?
cyclohexanone + FMNH2 + O2
?
Substrates: 3% conversion
Products: -
Products: -
?
cyclopentanone + FMNH2 + O2
?
Substrates: 24% conversion
Products: -
Products: -
?
(+)-camphor + FMNH2 + O2
? + FMN + H2O
Substrates: 88% conversion
Products: -
Products: -
?
(+)-camphor + FMNH2 + O2
? + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
(+)-camphor + FMNH2 + O2
? + FMN + H2O
Substrates: 88% conversion
Products: -
Products: -
?
(+/-)-cis-bicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
Substrates: 99% conversion
Products: -
Products: -
?
(+/-)-cis-bicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
Substrates: 99% conversion
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + FMN + H2O
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Substrates: 6-dione i.e. 3,6-diketocamphane
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + FMN + H2O
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Substrates: 6-dione i.e. 3,6-diketocamphane
Products: i.e. cyclopentaneacetic acid, 3-hydroxy-2,2,3-trimethyl-5-oxo, delta-lactone, i.e. 3,4,4-trimethyl-6-carboxy-methyl-DELTA3-cyclopentenone, product is an unstable lactone-intermediate and forms spontaneously (2,2-dimethyl-5-oxo-cyclopent-3-en-1-yl)acetic acid, i.e. 2-oxo-DELTA3-4,5,5-trimethylcyclopentenyl acetic acid
Products: i.e. cyclopentaneacetic acid, 3-hydroxy-2,2,3-trimethyl-5-oxo, delta-lactone, i.e. 3,4,4-trimethyl-6-carboxy-methyl-DELTA3-cyclopentenone, product is an unstable lactone-intermediate and forms spontaneously (2,2-dimethyl-5-oxo-cyclopent-3-en-1-yl)acetic acid, i.e. 2-oxo-DELTA3-4,5,5-trimethylcyclopentenyl acetic acid
?
(-)-bornane-2,5-dione + FMNH2 + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + FMN + H2O
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Substrates: 6-dione i.e. 3,6-diketocamphane
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
?
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Substrates: inducible by growth on (+)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
?
-
Substrates: inducible by growth on racemic camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
?
-
Substrates: inducible by growth on (+)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + O2 + FMNH2
(-)-5-oxo-1,2-campholide + FMN + H2O
Substrates: the enzyme is involved in the degradation of (-)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + O2 + FMNH2
(-)-5-oxo-1,2-campholide + FMN + H2O
Substrates: the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system
Products: -
Products: -
?
(-)-bornane-2,5-dione + O2 + FMNH2
(-)-5-oxo-1,2-campholide + FMN + H2O
Substrates: the enzyme is involved in the degradation of (-)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + O2 + FMNH2
(-)-5-oxo-1,2-campholide + FMN + H2O
Substrates: the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system
Products: -
Products: -
?
(-)-camphor + FMNH2 + O2
?
Substrates: conversion to lactone, no conversion of (+)-camphor
Products: -
Products: -
?
(-)-camphor + FMNH2 + O2
?
Substrates: conversion to lactone, no conversion of (+)-camphor
Products: -
Products: -
?
(-)-camphor + FMNH2 + O2
? + FMN + H2O
Substrates: 91% conversion
Products: -
Products: -
?
(-)-camphor + FMNH2 + O2
? + FMN + H2O
Substrates: 91% conversion
Products: -
Products: -
?
(R,R)-bicyclo[2.2.1]heptane-2,5-dione + FMNH2 + O2
?
Substrates: 26% conversion
Products: -
Products: -
?
(R,R)-bicyclo[2.2.1]heptane-2,5-dione + FMNH2 + O2
?
Substrates: 26% conversion
Products: -
Products: -
?
2,3,4,5-tetramethyl-2-cyclopenten-1-one + FMNH2 + O2
?
Substrates: 43% conversion
Products: -
Products: -
?
2,3,4,5-tetramethyl-2-cyclopenten-1-one + FMNH2 + O2
?
Substrates: 43% conversion
Products: -
Products: -
?
3,6-diketocamphane + FMNH2 + O2
? + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
3,6-diketocamphane + FMNH2 + O2
? + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
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Substrates: enzyme is associated with a NADH oxidase
Products: -
Products: -
?
additional information
?
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Substrates: enzyme is associated with a NADH oxidase
Products: -
Products: -
?
additional information
?
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Substrates: several sulfides and bicyclo[3,2,0]hept-2-en-6-one are enantioselectively oxidized to the corresponding sulfoxides and oxa lactones, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: rubredoxin not mentioned
Products: -
Products: -
?
additional information
?
-
-
Substrates: rubredoxin not mentioned
Products: -
Products: -
?
additional information
?
-
-
Substrates: rubredoxin not mentioned
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes stereoselective electrophilic biooxidation of a wide range of prochiral organic sulfoxides to the corresponding chiral sulfoxides as well as the nucleophilic biooxidation of ketones to lactones with different enantio- and stereoselectivity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: mechanism of enantioselectivity for the hydroxyl-peroxide rearrangement taking place in the BVMO active site
Products: -
Products: -
?
additional information
?
-
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Substrates: mechanism of enantioselectivity for the hydroxyl-peroxide rearrangement taking place in the BVMO active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: rubredoxin not mentioned
Products: -
Products: -
?
additional information
?
-
Substrates: mechanism of enantioselectivity for the hydroxyl-peroxide rearrangement taking place in the BVMO active site
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: catalyzes stereoselective electrophilic biooxidation of a wide range of prochiral organic sulfoxides to the corresponding chiral sulfoxides as well as the nucleophilic biooxidation of ketones to lactones with different enantio- and stereoselectivity, overview
Products: -
Products: -
?
(+)-camphor + FMNH2 + O2
? + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
?
-
Substrates: inducible by growth on (+)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
?
-
Substrates: inducible by growth on racemic camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + FMNH2 + O2
?
-
Substrates: inducible by growth on (+)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + O2 + FMNH2
(-)-5-oxo-1,2-campholide + FMN + H2O
Substrates: the enzyme is involved in the degradation of (-)-camphor
Products: -
Products: -
?
(-)-bornane-2,5-dione + O2 + FMNH2
(-)-5-oxo-1,2-campholide + FMN + H2O
Substrates: the enzyme is involved in the degradation of (-)-camphor
Products: -
Products: -
?
3,6-diketocamphane + FMNH2 + O2
? + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
3,6-diketocamphane + FMNH2 + O2
? + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
dependent on, FMN cofactor modelling. Type II Baeyer-Villiger monooxygenases are attributed to the R group in relation to the re-face attachment of the hydroperoxide to the flavin coenzyme. The FMN cofactor binds in the cleft formed at the C-terminal side of the TIM barrel, with the phosphate group involved in hydrogen bonding at the edge of the cleft and the isoalloxazine ring located deep inside of the cleft
additional information
-
interaction of inducible NADH dehydrogenase component via bound FMN with oxygenating component
-
additional information
-
usage of immobilized macromolecular cofactor in a membrane reactor
-
additional information
-
purified NADH dehydrogenase component from 2,5-diketocamphane-1,2-monooxygenase can be used as electron donor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 isozymes termed 2,5-diketocamphane-1,2-monooxygenase and 3,6-diketocamphane-1,6-monooxygenase
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
growth on (+)-, (-)- and (rac)-camphor. The two DKCMO isoenzymes, 2,5- and 3,6-diketocamphane monooxygenase, are highly selective towards their respective antipodes when serving as substrates for biooxygenation, nevertheless a small but significant cross-inducibility of the enantiomerically redundant DKCMO isoenzyme by both camphor antipodes exists
brenda
-
growth on (+)-, (-)- and (rac)-camphor. The two DKCMO isoenzymes, 2,5- and 3,6-diketocamphane monooxygenase, are highly selective towards their respective antipodes when serving as substrates for biooxygenation, nevertheless a small but significant cross-inducibility of the enantiomerically redundant DKCMO isoenzyme by both camphor antipodes exists
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
NADH dehydrogenase component forming a loosely complex with the oxygenating component
brenda
Pseudomonas putida C1 / ATCC 17453
-
NADH dehydrogenase component forming a loosely complex with the oxygenating component
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the orientation of the isoalloxazine ring of the FMN cofactor in the active site of the TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a beta-bulge at the C-terminus of beta-strand 3, which is a feature observed in many proteins of this superfamily. Both the 2,5-DKMO and 3,6-DKMO oxygenating components have sequence similarity to bacterial luciferases and bear little similarity to type I Baeyer-Villiger monooxygenase, type I BVMOs
evolution
-
type 2 Baeyer-Villiger monooxygenases (type 2 BVMOs) are a subgroup of the NAD(P)H:FMN-dependent two-component monooxygenases (TCMOs). They can alternatively be classed as a subgroup of the NAD(P)H:FMN-dependent class C flavoprotein monooxygenases
evolution
-
type 2 Baeyer-Villiger monooxygenases (type 2 BVMOs) are a subgroup of the NAD(P)H:FMN-dependent two-component monooxygenases (TCMOs). They can alternatively be classed as a subgroup of the NAD(P)H:FMN-dependent class C flavoprotein monooxygenases
-
evolution
-
the orientation of the isoalloxazine ring of the FMN cofactor in the active site of the TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a beta-bulge at the C-terminus of beta-strand 3, which is a feature observed in many proteins of this superfamily. Both the 2,5-DKMO and 3,6-DKMO oxygenating components have sequence similarity to bacterial luciferases and bear little similarity to type I Baeyer-Villiger monooxygenase, type I BVMOs
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metabolism
the enzyme is involved in the camphor-degradation pathway, overview
metabolism
the enzyme is involved in the degradation of (-)-camphor
metabolism
-
the enzyme is involved in the degradation of (-)-camphor
-
metabolism
-
the enzyme is involved in the camphor-degradation pathway, overview
-
physiological function
-
2,5- and 3,6-diketocamphane monooxygenase (DKCMO) are two enantiocomplementary isoenzymes that catalyse a key lactone-forming step in the degradation of the (+)- and (-)-camphor antipodes, respectively, in Pseudomonas putida NCIMB 10007. Enzyme 3,6-diketocamphane monooxygenase distributes the flavin nucleotide- and nicotinamide nucleotide-dependent tasks between a homodimeric monooxygenase component and a separate flavin reductase (FR) with unbound FMN, the flavin thus effectively serving as a second substrate to transfer reducing power between the functionally distinct subunits. Various flavin reductases function effectively as sources of the requisite FMNH2 to 3,6-diketocamphane monooxygenase at different times throughout growth on camphor, significant subsequent contribution throughout the mid- to late-exponential phases of growth is also made by the camphor-induced homodimeric 37.0 kDa flavin reductase Fred, possible involvement of camphor-induced putidaredoxin reductase as a contributory activity. Analysis of flavin reductases in Pseudomonas putida NCIMB 10007, overview
physiological function
-
2,5- and 3,6-diketocamphane monooxygenase (DKCMO) are two enantiocomplementary isoenzymes that catalyse a key lactone-forming step in the degradation of the (+)- and (-)-camphor antipodes, respectively, in Pseudomonas putida NCIMB 10007. Enzyme 3,6-diketocamphane monooxygenase distributes the flavin nucleotide- and nicotinamide nucleotide-dependent tasks between a homodimeric monooxygenase component and a separate flavin reductase (FR) with unbound FMN, the flavin thus effectively serving as a second substrate to transfer reducing power between the functionally distinct subunits. Various flavin reductases function effectively as sources of the requisite FMNH2 to 3,6-diketocamphane monooxygenase at different times throughout growth on camphor, significant subsequent contribution throughout the mid- to late-exponential phases of growth is also made by the camphor-induced homodimeric 37.0 kDa flavin reductase Fred, possible involvement of camphor-induced putidaredoxin reductase as a contributory activity. Analysis of flavin reductases in Pseudomonas putida NCIMB 10007, overview
-
additional information
the enzyme is a type II Baeyer-Villiger monooxygenase, enzyme structure modeling, active site structure, overview
additional information
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the enzyme is a type II Baeyer-Villiger monooxygenase, enzyme structure modeling, active site structure, overview
additional information
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the enzyme is a type II Baeyer-Villiger monooxygenase, enzyme structure modeling, active site structure, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
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enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
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analysis of flavin reductases in Pseudomonas putida NCIMB 10007, overview
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
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x * 17000-18000, native flavin reductase subunit of the enzyme and flavin reductase FRED, SDS-PAGE
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x * 17000-18000, native flavin reductase subunit of the enzyme and flavin reductase FRED, SDS-PAGE
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additional information
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enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
Pseudomonas putida C1 / ATCC 17453
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enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
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additional information
Pseudomonas putida C1 / ATCC 17453
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enzyme components from a very loose complex
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
plate shaped crystals from 4.0 M sodium formate and 28% PEG 8000 in 0.2 M sodium acetate, X-ray analysis
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purified recombinant N-terminally His6-tagged enzyme, by Microbatch crystallization, mixing of 7 mg/ml protein in 20 mM FMN, 5 mM NADH and 5 mM (-)-camphor in a 1:1 ration, purified native enzyme, by vapour-diffusion technique, 10 mg/ml protein solution are mixed in equal volumes with 50 mM PIPES pH 6.5, 50% ammonium sulfate, room temperature, best from 100 mM HEPES pH 7.0, 20% PEG 3350 in the presence of 20 mM FMN, 5 mM NADH and 5 mM (-)-camphor, at 18°C, X-ray diffraction structure determination and analysis at 1.9-2.7 A resolution, the enzyme's crystal structure is solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model
vapour-diffusion technique, three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
biooxygenating subunits of both enantiospecific DKCMO isoenzymes to homogeneity by a preparative process involving anion exchange chromatography and ultrafiltration, purification and detection of FMN-reductase activities
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recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration