Literature summary extracted from

Wiseman, B.; Colin, J.; Smith, A.T.; Ivancich, A.; Loewen, P.C.
Mechanistic insight into the initiation step of the reaction of Burkholderia pseudomallei catalase-peroxidase with peroxyacetic acid (2009), J. Biol. Inorg. Chem., 14, 801-811.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.11.1.21	D141A	the mutant lacks an aspartate at the entrance to the heme cavity. The reaction with peroxyacetic acid proceeds much faster than for the wild type enzyme	Burkholderia pseudomallei
1.11.1.21	D141A/R108A	the reaction with peroxyacetic acid is clearly slower than for mutant D141A	Burkholderia pseudomallei
1.11.1.21	R108A	the reaction with peroxyacetic acid is clearly slower than for mutant D141A	Burkholderia pseudomallei
1.11.1.21	W330F	the mutant exhibits slightly reduced catalase- and peroxidase-specific activities but a faster peroxidase turnover rate compared to the wild type enzyme	Burkholderia pseudomallei

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.11.1.21	Burkholderia pseudomallei	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.11.1.21	2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2	-	Burkholderia pseudomallei	oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O	-	?
1.11.1.21	3-chloroperoxybenzoic acid	-	Burkholderia pseudomallei	?	-	?
1.11.1.21	H2O2	-	Burkholderia pseudomallei	O2 + H2O	-	?
1.11.1.21	peroxyacetic acid	-	Burkholderia pseudomallei	?	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.11.1.21	KatG	-	Burkholderia pseudomallei

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.11.1.21	heme	-	Burkholderia pseudomallei

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)