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 .

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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	-	-

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	-	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 65 mV. One of the two haems is reduced by NADH (549 nm alpha-band)	Xanthomonas sp.

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Release 2023.1 (January 2023)