1.13.11.85: exo-cleaving rubber dioxygenase
This is an abbreviated version!
For detailed information about exo-cleaving rubber dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.85
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1.13.11.85
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xanthomonas
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latex
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c-type
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polycis-1,4-isoprene
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oxygenases
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dihaem
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rubber-degrading
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gordonia
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steroidobacter
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latex-clearing
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waste
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peroxidases
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analysis
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synthesis
- 1.13.11.85
- xanthomonas
- latex
-
c-type
-
polycis-1,4-isoprene
- oxygenases
-
dihaem
-
rubber-degrading
- gordonia
-
steroidobacter
-
latex-clearing
- waste
- peroxidases
- analysis
- synthesis
Reaction
+ n O2 = n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
Synonyms
heme-dependent rubber oxygenase, LATA, poly(cis-1,4-isoprene)-cleavage enzyme, roxA, RoxB, RubA, rubber oxygenase, rubber oxygenase A
ECTree
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Engineering
Engineering on EC 1.13.11.85 - exo-cleaving rubber dioxygenase
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F317A
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polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
F317L
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polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
F317Y
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polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
F317A
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polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
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F317L
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polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
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F317Y
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polyisoprene-cleaving activity of the variant is drastically reduced compared to the wild type enzyme
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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