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Literature summary for 1.13.11.85 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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Xanthomonas sp. Q7X0P3
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-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
roxA
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Xanthomonas sp.

Cofactor

Cofactor Comment Organism Structure
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 Ā–65 mV. One of the two haems is reduced by NADH (549 nm alpha-band) Xanthomonas sp.