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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

Reaction

cis-1,4-polyisoprene
+ 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

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.85 exo-cleaving rubber dioxygenase

Engineering

Engineering on EC 1.13.11.85 - exo-cleaving rubber dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F301L
-
the mutant shows 14% of wild type activity
F301Y
-
the mutant shows 21% of wild type activity
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
F301L
-
the mutant shows 14% of wild type activity
-
F301Y
-
the mutant shows 21% of wild type activity
-
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