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Information on EC 1.13.11.85 - exo-cleaving rubber dioxygenase
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1.13.11.85 exo-cleaving rubber dioxygenaseIUBMB Comments
The enzyme, studied mainly from the bacterium Xanthomonas sp. 35Y, catalyses the cleavage of the double bonds in natural and synthetic rubber (cis-1,4-polyisoprene polymers), generating ends that contain ketone and aldehyde groups. The enzyme from Xanthomonas sp. 35Y contains two c-type cytochromes. It attacks the substrate from its end, producing a single product of 15 carbons.
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Word Map
- 1.13.11.85
- xanthomonas
- latex
-
c-type
-
polycis-1,4-isoprene
- oxygenases
-
dihaem
-
rubber-degrading
- gordonia
-
steroidobacter
-
latex-clearing
- waste
- peroxidases
- analysis
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
cis-1,4-polyisoprene
+
n
=
n
Synonyms
rubber oxygenase, rubber oxygenase a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heme-dependent rubber oxygenase
-
-
ambiguous
-
LATA
poly(cis-1,4-isoprene)-cleavage enzyme
roxA
RubA
rubber oxygenase
rubber oxygenase A
roxA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cis-1,4-polyisoprene + n O2 = n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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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]
The enzyme, studied mainly from the bacterium Xanthomonas sp. 35Y, catalyses the cleavage of the double bonds in natural and synthetic rubber (cis-1,4-polyisoprene polymers), generating ends that contain ketone and aldehyde groups. The enzyme from Xanthomonas sp. 35Y contains two c-type cytochromes. It attacks the substrate from its end, producing a single product of 15 carbons.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal + ?
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al
-
-
-
?
cis-1,4-polyisoprene + n O2
n 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al
-
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
exo-type cleavage mechanism. RoxA is able to cleave isolated latex-clearing protein-derived oligo-isoprenoid molecules to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal groups
-
-
?
poly(cis-1,4-isoprene) + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
?
poly(cis-1,4-isoprene) + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
12-oxo-4,8-dimethyltrideca-4,8-diene-1-al is the main cleavage product in the absence of (18)O-compounds. Incorporation of one (18)O atom in 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al is found if the cleavage reaction is performed in the presence of (18)O2 and H2(16)O. Incubation of poly(cis-1,4-isoprene) (with RoxA) or of isolated unlabeled 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al (without RoxA) with H2(18)O in the presence of (16)O2 indicates that the carbonyl oxygen atoms of 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al is significantly exchanged with oxygen atoms derived from water. The isotope exchange is avoided by simultaneous enzymatic reduction of both carbonyl functions of 12-Oxo-4,8-dimethyltrideca-4,8-diene-1-al to the corresponding dialcohol 12-hydroxy-4,8-dimethyltrideca-4,8-diene-1-ol during RoxA-mediated in vitro cleavage of poly(cis-1,4-isoprene)
-
-
?
poly(cis-1,4-isoprene) + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
degradation by oxidative cleavage of the double bonds of poly(cis-1,4-isoprene). 12-Oxo-4,8-dimethyltrideca-4,8-diene-1-al is identified as the major cleavage product. There is a homologous series of minor metabolites that differ from the major degradation product only in the number of repetitive isoprene units between terminal functions, CHO-CH2O and OCH2-COCH3
-
-
?
rubber latex + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
the enzyme is excreted by Xanthomonas to functionalize and cleave the inert latex biopolymer poly(cis-1,4-isoprene) into the more soluble (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal units
-
-
?
rubber latex + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
degradation by oxidative cleavage of the double bonds of poly(cis-1,4-isoprene). 12-Oxo-4,8-dimethyltrideca-4,8-diene-1-al is identified as the major cleavage product. There is a homologous series of minor metabolites that differ from the major degradation product only in the number of repetitive isoprene units between terminal functions, CHO-CH2O and OCH2-COCH3. Enzymatic cleavage of rubber by the purified protein is strictly dependent on the presence of oxygen
-
-
?
rubber latex + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
RoxA cleaves rubber by a dioxygenase mechanism
-
-
?
rubber latex + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
the enzyme incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal. Activation and cleavage of O2 require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage
-
-
?
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme does not feature a peroxidase activity
-
-
-
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme has no peroxidase activity
-
-
-
additional information
?
-
-
the enzyme does not feature a peroxidase activity
-
-
-
additional information
?
-
RoxA does not show any peroxidase activity
-
-
?
additional information
?
-
-
RoxA does not show any peroxidase activity
-
-
?
additional information
?
-
enzyme degrades both natural rubber latex and chemosynthetic poly(cis-1,4-isoprene) in vitro by oxidative cleavage of the double bonds of poly(cis-1,4-isoprene). Enzymatic cleavage of rubber by the purified protein is strictly dependent on the presence of oxygen
-
-
?
additional information
?
-
substrates are the latices of natural and synthetic isoprene rubber, but also some kinds of low-MW polyisoprene compounds of cis-1,4 type. No substrates: solanesol and squalene
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rubber latex + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
the enzyme is excreted by Xanthomonas to functionalize and cleave the inert latex biopolymer poly(cis-1,4-isoprene) into the more soluble (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal units
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + n O2
n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
?
cis-1,4-polyisoprene + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
1.9 heme per mol of protein, presence of two heme-binding motifs (CXXCH) for covalent attachment of heme to the protein
heme
presence of two c-type heme centers that show two distinct alpha-bands at 549 and 553 nm in the dithionite-reduced state. One heme shows a midpoint potential of 65 mV. One of the two haems is reduced by NADH (549 nm alpha-band)
heme
presence of two slightly different heme centers with absorption maxima between 549 and 553 nm
heme
presence of two slightly different heme centers with absorption maxima between 549 and 553 nm
heme
the enzyme contains approximately 2 mol of heme per mol of RoxA
additional information
catalytic reaction does not require addition of any soluble cofactors or metal ions
-
additional information
enzymatic cleavage of rubber by the purified proteindoes not require addition of any soluble cofactors or metal ions
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
catalytic reaction does not require addition of any soluble cofactors or metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
5 mM, 2% residual activity; 5 mM, complete inhibition
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
0.5%, complete inhibition
CO
carbon monoxide strongly inhibits the polyisoprene cleavage reaction of RoxAXsp
Dithionite
reduction of RoxA results in a reversible inactivation of the enzyme
N-ethylmaleimide
10 mM, 31% residual activity; 10 mM, 69% inhibition
NADH
reduction of RoxA results in a reversible inactivation of the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzymatic cleavage of rubber by the purified proteindoes not require addition of any soluble cofactors or metal ions
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
in potassium phosphate buffer or in HEPES buffer. Other buffers (Tris, carbonate-ammonium acetate, and glycylglycine) result in poor activities
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
pH values below pH 6 or above 8.5 result in only poor activities
6.5 - 7.5
pH 6.5: about 60% of maximal activity, pH 7.5: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 30
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23 - 30
at 30°C, the specific activity of RoxA is almost double as high as at 23°C
30 - 50
30°C: about 55% of maximal activity, 50°C: about 60% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
malfunction
-
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
metabolism
the enzyme is excreted by Xanthomonas to functionalize and cleave the inert latex biopolymer poly(cis-1,4-isoprene) into the more soluble (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal units
metabolism
-
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain
metabolism
-
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain
metabolism
-
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain
metabolism
-
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain
metabolism
-
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain
metabolism
-
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain
-
physiological function
expression of gene functionally complements a Xanthomonas sp. 35Y RoxA deletion mutant
physiological function
expression of gene functionally complements a Xanthomonas sp. 35Y RoxA deletion mutant
physiological function
expression of gene functionally complements a Xanthomonas sp. 35Y RoxA deletion mutant
physiological function
inactivation of the chromosomal roxA gene results in inability of Xanthomonas sp. to produce active RoxA and to utilize rubber as a sole source of carbon and energy
physiological function
RoxA is isolated with O2 stably bound to the active site heme iron. Activation and cleavage of O2 require binding of polyisoprene, and the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. Both residues H312 and Y462 are ideally positioned to form hydrogen bonds that arrest the substrate chain, so that the bond connecting the third and fourth monomer is in close proximity to the O2 ligand at heme 1. After oxidative cleavage, the resulting 2-oxo-4,8-dimethyl-trideca-4,8-diene-1-al product dissociates, and RoxA slides along the isoprene chain until the terminus is again arrested by hydrogen bonds
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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
71500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the preprotein has a MW of 74700 Da, the mature protein has MW of 71500 Da
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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
sitting drop vapor diffusion method, structural analysis of RoxA from Xanthomonas sp. strain 35Y at a resolution of 1.8 A
space group P2, unit cell parameters a = 72.4, b = 97.1, c = 101.1 A,beta 98.39°
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F317A
-
polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
F317L
-
polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
F317Y
-
polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
F317A
-
polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
-
F317L
-
polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
-
F317Y
-
polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
-
F317A
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
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
mutation in residue located in close proximity to the N-terminal heme that presumably represents the active site, inactive
F317Y
mutation in residue located in close proximity to the N-terminal heme that presumably represents the active site, inactive
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54.3
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
reoxygenation of the enzyme, that is deoxygenated by the addition of stoichiometric amounts of the reductant dithionite, can be achieved simply by incubation under an oxygen-containing gas atmosphere. Oxidized (deoxygenated) enzyme can also be reoxygenated by the presence of a slight molar excess of H2O2 within minutes. The enzyme retains its activity in the fully oxidized low-spin state
-
763872
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and hydroxyapatite column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the roxA gene is upregulated during growth on polyisoprene
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoffmann, M.; Braaz, R.; Jendrossek, D.; Einsle, O.
Crystallization of the extracellular rubber oxygenase RoxA from Xanthomonas sp. strain 35Y
Acta Crystallogr. Sect. F
64
123-125
2008
Xanthomonas sp. 35Y (Q7X0P3)
brenda
Tsuchii, A.; Takeda, K.
Rubber-degrading enzyme from a bacterial culture
Appl. Environ. Microbiol.
56
269-274
1990
Xanthomonas sp. 35Y (Q7X0P3)
brenda
Braaz, R.; Fischer, P.; Jendrossek, D.
Novel type of heme-dependent oxygenase catalyzes oxidative cleavage of rubber (poly-cis-1,4-isoprene)
Appl. Environ. Microbiol.
70
7388-7395
2004
Xanthomonas sp. 35Y (Q7X0P3)
brenda
Braaz, R.; Armbruster, W.; Jendrossek, D.
Heme-dependent rubber oxygenase RoxA of Xanthomonas sp. cleaves the carbon backbone of poly(cis-1,4-Isoprene) by a dioxygenase mechanism
Appl. Environ. Microbiol.
71
2473-2478
2005
Xanthomonas sp. 35Y (Q7X0P3)
brenda
Birke, J.; Hambsch, N.; Schmitt, G.; Altenbuchner, J.; Jendrossek, D.
Phe317 is essential for rubber oxygenase RoxA activity
Appl. Environ. Microbiol.
78
7876-7883
2012
Xanthomonas sp. 35Y (Q7X0P3)
brenda
Birke, J.; Rther, W.; Schmitt, G.; Jendrossek, D.
Functional identification of rubber oxygenase (RoxA) in soil and marine myxobacteria
Appl. Environ. Microbiol.
79
6391-6399
2013
Myxococcus fulvus (S5Y7P9), Myxococcus fulvus, Haliangium ochraceum (S5YEK5), Haliangium ochraceum, Corallococcus coralloides (S5YYL9), Corallococcus coralloides
brenda
Birke, J.; Jendrossek, D.
Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms
Appl. Environ. Microbiol.
80
5012-5020
2014
Xanthomonas sp. 35Y (Q7X0P3)
brenda
Birke, J.; Rther, W.; Jendrossek, D.
Latex clearing protein (Lcp) of Streptomyces sp. strain K30 is a b-type cytochrome and differs from rubber oxygenase A (RoxA) in its biophysical properties
Appl. Environ. Microbiol.
81
3793-3799
2015
Xanthomonas sp. (Q7X0P3), Xanthomonas sp. 35Y (Q7X0P3)
brenda
Hambsch, N.; Schmitt, G.; Jendrossek, D.
Development of a homologous expression system for rubber oxygenase RoxA from Xanthomonas sp.
J. Appl. Microbiol.
109
1067-1075
2010
Streptomyces sp. K30 (Q3L8N0)
brenda
Schmitt, G.; Seiffert, G.; Kroneck, P.; Braaz, R.; Jendrossek, D.
Spectroscopic properties of rubber oxygenase RoxA from Xanthomonas sp., a new type of dihaem dioxygenase
Microbiology
156
2537-2548
2010
Xanthomonas sp. (Q7X0P3), Xanthomonas sp.
brenda
Seidel, J.; Schmitt, G.; Hoffmann, M.; Jendrossek, D.; Einsle, O.
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp
Proc. Natl. Acad. Sci. USA
110
13833-13838
2013
Streptomyces sp. K30 (Q3L8N0), Xanthomonas sp. 35Y (Q7X0P3)
brenda
Birke, J.; Roether, W.; Jendrossek, D.
RoxB Is a Novel Type of Rubber Oxygenase That Combines Properties of Rubber Oxygenase RoxA and Latex Clearing Protein (Lcp)
Appl. Environ. Microbiol.
83
e00721-17
2017
Xanthomonas sp. 35Y (A0A1Y0DKQ1)
brenda
Birke, J.; Roether, W.; Jendrossek, D.
Rhizobacter gummiphilus NS21 has two rubber oxygenases (RoxA and RoxB) acting synergistically in rubber utilisation
Appl. Microbiol. Biotechnol.
102
10245-10257
2018
Rhizobacter gummiphilus, Rhizobacter gummiphilus NS21
brenda
Jendrossek, D.; Birke, J.
Rubber oxygenases
Appl. Microbiol. Biotechnol.
103
125-142
2019
Corallococcus coralloides, Haliangium ochraceum, Myxococcus fulvus, Rhizobacter gummiphilus, Steroidobacter cummioxidans, Rhizobacter gummiphilus NS21, Steroidobacter cummioxidans 35Y, Corallococcus coralloides 35
brenda
Roether, W.; Birke, J.; Grond, S.; Beltran, J.M.; Jendrossek, D.
Production of functionalized oligo-isoprenoids by enzymatic cleavage of rubber
Microb. Biotechnol.
10
1426-1433
2017
Steroidobacter cummioxidans, Steroidobacter cummioxidans 35Y
brenda
Sharma, V.; Mobeen, F.; Prakash, T.
In silico functional and evolutionary analyses of rubber oxygenases (RoxA and RoxB)
3 Biotech
10
376
2020
Steroidobacter cummioxidans, Steroidobacter cummioxidans 35Y
brenda
Schmitt, G.; Birke, J.; Jendrossek, D.
Towards the understanding of the enzymatic cleavage of polyisoprene by the dihaem-dioxygenase RoxA
AMB Express
9
166
2019
Steroidobacter cummioxidans, Steroidobacter cummioxidans 35Y
brenda
Kasai, D.; Imai, S.; Asano, S.; Tabata, M.; Iijima, S.; Kamimura, N.; Masai, E.; Fukuda, M.
Identification of natural rubber degradation gene in Rhizobacter gummiphilus NS21
Biosci. Biotechnol. Biochem.
81
614-620
2017
Rhizobacter gummiphilus (A0A0M4UPQ3), Rhizobacter gummiphilus, Rhizobacter gummiphilus NS21 (A0A0M4UPQ3)
brenda
Kasai, D.
Poly(cis-1,4-isoprene)-cleavage enzymes from natural rubber-utilizing bacteria
Biosci. Biotechnol. Biochem.
84
1089-1097
2020
Corallococcus coralloides, Haliangium ochraceum, Myxococcus fulvus, Rhizobacter gummiphilus, Chondromyces apiculatus, Rhizobacter gummiphilus NS21
brenda
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Release 2023.1 (January 2023)
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