Literature summary for 1.11.1.21 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.

Search for more literature for 1.11.1.21

Protein Variants

Protein Variants	Comment	Organism
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
D141A/R108A	the reaction with peroxyacetic acid is clearly slower than for mutant D141A	Burkholderia pseudomallei
R108A	the reaction with peroxyacetic acid is clearly slower than for mutant D141A	Burkholderia pseudomallei
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

Organism	UniProt	Comment	Textmining
Burkholderia pseudomallei	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
KatG	-	Burkholderia pseudomallei

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Burkholderia pseudomallei

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Release 2023.1 (January 2023)