Any feedback?
Information on EC 1.13.11.85 - exo-cleaving rubber dioxygenase
for references in articles please use BRENDA:EC1.13.11.85Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cis-1,4-polyisoprene + n O2 = n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
catalytic reaction does not require addition of any soluble cofactors or metal ions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 30
40
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE