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Literature summary for 1.13.11.85 extracted from

  • Braaz, R.; Fischer, P.; Jendrossek, D.
    Novel type of heme-dependent oxygenase catalyzes oxidative cleavage of rubber (poly-cis-1,4-isoprene) (2004), Appl. Environ. Microbiol., 70, 7388-7395 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
EDTA 10 mM, 1.1fold activation Xanthomonas sp. 35Y
additional information enzymatic cleavage of rubber by the purified proteindoes not require addition of any soluble cofactors or metal ions Xanthomonas sp. 35Y

Application

Application Comment Organism
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 Xanthomonas sp. 35Y

Inhibitors

Inhibitors Comment Organism Structure
1-S-octyl-beta-D-thioglucopyranoside 0.5%, complete inhibition Xanthomonas sp. 35Y
2,2'-dipyridyl 10 mM, 85% inhibition Xanthomonas sp. 35Y
2-mercaptoethanol 5 mM, 2% residual activity; 5 mM, complete inhibition Xanthomonas sp. 35Y
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate 0.5%, complete inhibition Xanthomonas sp. 35Y
alpha,alpha-bipyridyl 10 mM, 15% residual activity Xanthomonas sp. 35Y
carbon monoxide
-
Xanthomonas sp. 35Y
cyanide
-
Xanthomonas sp. 35Y
dithiothreitol 5 mM, 6% residual activity; 5 mM, 94% inhibition Xanthomonas sp. 35Y
N-ethylmaleimide 10 mM, 31% residual activity; 10 mM, 69% inhibition Xanthomonas sp. 35Y
octyl beta-glucoside 0.5% mM, 2% residual activity Xanthomonas sp. 35Y
octyl-beta-glucoside 0.5%, complete inhibition Xanthomonas sp. 35Y
p-chloromercuribenzoate 10 mM, 24% inhibition Xanthomonas sp. 35Y
Plysurf A210G 0.5%, complete inhibition Xanthomonas sp. 35Y
SDS 0.5%, 2% residual activity; 0.5%, complete inhibition Xanthomonas sp. 35Y
sodium cholate 0.5%, 68% inhibition Xanthomonas sp. 35Y
Tiron 10 mM, 27% inhibition Xanthomonas sp. 35Y
Triton X-100 0.5%, complete inhibition Xanthomonas sp. 35Y
Tween 80 0.5%, complete inhibition; 0.5% mM, 2% residual activity Xanthomonas sp. 35Y

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Xanthomonas sp. 35Y
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information catalytic reaction does not require addition of any soluble cofactors or metal ions Xanthomonas sp. 35Y

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
gel filtration Xanthomonas sp. 35Y

Organism

Organism UniProt Comment Textmining
Xanthomonas sp. 35Y Q7X0P3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Xanthomonas sp. 35Y
from culture fluid Xanthomonas sp. 35Y

Source Tissue

Source Tissue Comment Organism Textmining
culture fluid
-
Xanthomonas sp. 35Y
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cis-1,4-polyisoprene + n O2
-
Xanthomonas sp. 35Y n 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al
-
?
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 Xanthomonas sp. 35Y ?
-
?
poly(cis-1,4-isoprene) + O2 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 Xanthomonas sp. 35Y (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
?
rubber latex + O2 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 Xanthomonas sp. 35Y (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
-
?

Subunits

Subunits Comment Organism
monomer 1 * 65000, SDS-PAGE Xanthomonas sp. 35Y

Synonyms

Synonyms Comment Organism
roxA
-
Xanthomonas sp. 35Y

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
40
-
-
Xanthomonas sp. 35Y

Temperature Range [┬░C]

Temperature Minimum [┬░C] Temperature Maximum [┬░C] Comment Organism
30 50 30┬░C: about 55% of maximal activity, 50┬░C: about 60% of maximal activity Xanthomonas sp. 35Y

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Xanthomonas sp. 35Y

pH Range

pH Minimum pH Maximum Comment Organism
6.5 7.5 pH 6.5: about 60% of maximal activity, pH 7.5: about 60% of maximal activity Xanthomonas sp. 35Y

Cofactor

Cofactor Comment Organism Structure
heme 1.9 heme per mol of protein, presence of two heme-binding motifs (CXXCH) for covalent attachment of heme to the protein Xanthomonas sp. 35Y
heme the enzyme contains approximately 2 mol of heme per mol of RoxA Xanthomonas sp. 35Y
additional information catalytic reaction does not require addition of any soluble cofactors or metal ions Xanthomonas sp. 35Y
additional information enzymatic cleavage of rubber by the purified proteindoes not require addition of any soluble cofactors or metal ions Xanthomonas sp. 35Y