Literature summary for 1.11.1.21 extracted from

Yamada, Y.; Fujiwara, T.; Sato, T.; Igarashi, N.; Tanaka, N.
The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui (2002), Nat. Struct. Biol., 9, 691-695.

Search for more literature for 1.11.1.21

Crystallization (Commentary)

Crystallization (Comment)	Organism
the 2.0 A crystal structure of the enzyme reveals that it is a dimer of two identical subunits. Each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase. The active site is in the N-terminal domain. Although the arrangement of the catalytic residues and the cofactor heme b in the active site is virtually identical to that of class I peroxidases, the heme moiety is buried inside the domain, similar to that in a typical catalase. In the vicinity of the active site, novel covalent bonds are formed among the side chains of three residues, including that of a tryptophan on the distal side of the heme. Together with the C-terminal domain, these covalent bonds fix two long loops on the surface of the enzyme that cover the substrate access channel to the active site. These features provide an explanation for the dual activities of this enzyme	Haloarcula marismortui

Crystallization (Comment)

Organism

the 2.0 A crystal structure of the enzyme reveals that it is a dimer of two identical subunits. Each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase. The active site is in the N-terminal domain. Although the arrangement of the catalytic residues and the cofactor heme b in the active site is virtually identical to that of class I peroxidases, the heme moiety is buried inside the domain, similar to that in a typical catalase. In the vicinity of the active site, novel covalent bonds are formed among the side chains of three residues, including that of a tryptophan on the distal side of the heme. Together with the C-terminal domain, these covalent bonds fix two long loops on the surface of the enzyme that cover the substrate access channel to the active site. These features provide an explanation for the dual activities of this enzyme

Haloarcula marismortui

Organism

Organism	UniProt	Comment	Textmining
Haloarcula marismortui	O59651	-	-
Haloarcula marismortui DSM 3752	O59651	-	-

Subunits

Subunits	Comment	Organism
homodimer	each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase	Haloarcula marismortui

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)