Information on EC 1.13.11.85 - exo-cleaving rubber dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.85
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RECOMMENDED NAME
GeneOntology No.
exo-cleaving rubber dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cis-1,4-polyisoprene + n O2 = n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rubber degradation I
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SYSTEMATIC NAME
IUBMB Comments
cis-1,4-polyisoprene:oxygen dioxygenase [(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal-forming]
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal + ?
show the reaction diagram
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?
cis-1,4-polyisoprene + n O2
n 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al
show the reaction diagram
dolichol + O2
?
show the reaction diagram
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?
ficaprenol + O2
?
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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catalytic reaction does not require addition of any soluble cofactors or metal ions
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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presence of two low-spin Fe(III) heme centers
additional information
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catalytic reaction does not require addition of any soluble cofactors or metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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5 mM, 2% residual activity
alpha,alpha-bipyridyl
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10 mM, 15% residual activity
carbon monoxide
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Dithionite
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reduction of RoxA results in a reversible inactivation of the enzyme
dithiothreitol
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5 mM, 6% residual activity
imidoazole
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presence results in a reversible inactivation of the enzyme
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N-ethylmaleimide
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10 mM, 31% residual activity
NADH
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reduction of RoxA results in a reversible inactivation of the enzyme
octyl beta-glucoside
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0.5% mM, 2% residual activity
SDS
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0.5%, 2% residual activity
Tween 80
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0.5% mM, 2% residual activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
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37°C, pH 7.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 30
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 65000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.8 A resolution. The enzyme shows an unusually low degree of secondary structure. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al
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space group P2, unit cell parameters a = 72.4, b = 97.1, c = 101.1 A,beta 98.39°
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54.3
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melting point
100
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10 min, complete loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from culture fluid
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F317A
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about 3% residual activiy. Both heme groups are present in an oxidized form, spectral responses to the addition ligand molecules such as imidazole and pyridine are different from those of wild-type
F317L
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about 10% residual activiy. Both heme groups are present in an oxidized form, spectral responses to the addition ligand molecules such as imidazole and pyridine are different from those of wild-type
F317W
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mutation in residue located in close proximity to the N-terminal heme that presumably represents the active site, inactive
F317Y
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mutation in residue located in close proximity to the N-terminal heme that presumably represents the active site, inactive
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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development of an in vitro enzyme assay for oxidative rubber degradation based on high-performance liquid chromatography analysis and spectroscopic detection of product carbonyl functions after derivatization with dinitrophenylhydrazone
synthesis
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optimization of a transformation system via electroporation, and a conjugation system for expression of RoxA in Xanthomonas sp. About 6 mg purified RoxA are obtained from 1 l of cell-free culture fluid