Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cis-1,4-polyisoprene + n O2
?
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 + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
ficaprenol + O2
?
-
-
-
?
poly(cis-1,4-isoprene) + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
rubber latex + O2
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
additional information
?
-
cis-1,4-polyisoprene + n O2
?
-
-
-
?
cis-1,4-polyisoprene + n O2
?
-
-
-
?
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 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.
cis-1,4-polyisoprene + n O2
?
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
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
?
-
-
-
?
cis-1,4-polyisoprene + n O2
?
-
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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