Literature summary for 1.13.11.92 extracted from

Goulah, C.C.; Zhu, G.; Koszelak-Rosenblum, M.; Malkowski, M.G.
The crystal structure of alpha-dioxygenase provides insight into diversity in the cyclooxygenase-peroxidase superfamily (2013), Biochemistry, 52, 1364-1372 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure to 1.5 A resolution. The structure is monomeric, predominantly helical-helical, and comprised of two domains. Helices H2, H6, H8, and H17 form the heme binding cleft and walls of the active site channel. Residues His318, Thr323, and Arg566 are located near the catalytic tyrosine, Tyr386, at the apex of the channel, where they interact with a chloride ion. Two extended inserts are present on the surface of the enzyme that restrict access to the distal face of the heme	Arabidopsis thaliana

Crystallization (Comment)

Organism

structure to 1.5 A resolution. The structure is monomeric, predominantly helical-helical, and comprised of two domains. Helices H2, H6, H8, and H17 form the heme binding cleft and walls of the active site channel. Residues His318, Thr323, and Arg566 are located near the catalytic tyrosine, Tyr386, at the apex of the channel, where they interact with a chloride ion. Two extended inserts are present on the surface of the enzyme that restrict access to the distal face of the heme

Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9SGH6	-	-

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)