Literature summary for 1.11.1.19 extracted from

Yoshida, T.; Tsuge, H.; Konno, H.; Hisabori, T.; Sugano, Y.
The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue (2011), FEBS J., 278, 2387-2394.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Aspergillus oryzae	Bjerkandera adusta

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of native enzyme, the D171N mutant, the native enzyme complexed with cyanide, and the D171N mutant associated with cyanide, to 1.4 A, 1.42 A, 1.45 and 1.4 A resolution, respectively. Structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. The structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron	Bjerkandera adusta

Crystallization (Comment)

Organism

structures of native enzyme, the D171N mutant, the native enzyme complexed with cyanide, and the D171N mutant associated with cyanide, to 1.4 A, 1.42 A, 1.45 and 1.4 A resolution, respectively. Structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. The structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron

Bjerkandera adusta

Organism

Organism	UniProt	Comment	Textmining
Bjerkandera adusta	Q8WZK8	-	-

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Release 2023.1 (January 2023)