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Literature summary extracted from

  • 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 (2010), Microbiology, 156, 2537-2548 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.85 Dithionite reduction of RoxA results in a reversible inactivation of the enzyme Xanthomonas sp.
1.13.11.85 imidazole presence results in a reversible inactivation of the enzyme Xanthomonas sp.
1.13.11.85 NADH reduction of RoxA results in a reversible inactivation of the enzyme Xanthomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.85 Iron presence of two low-spin Fe(III) heme centers Xanthomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.85 Xanthomonas sp. Q7X0P3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.85 additional information RoxA does not show any peroxidase activity Xanthomonas sp. ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.85 roxA
-
 Xanthomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.85 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) Xanthomonas sp.