Literature summary for 4.2.2.B7 extracted from

Ochiai, A.; Yamasaki, M.; Mikami, B.; Hashimoto, W.; Murata, K.
Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens (2010), J. Biol. Chem., 285, 24519-24528 .

Search for more literature for 4.2.2.B7

Cloned(Commentary)

Cloned (Comment)	Organism
-	Agrobacterium tumefaciens

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and mutant H531A, in complex with alginate trisaccharide, to 2.1 A and 2.99 A resolution, respectively. Residues H311 and Y365 act as the catalytic base and acid, respectively. A short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains are essential for the exolytic mode of action	Agrobacterium tumefaciens

Protein Variants

Protein Variants	Comment	Organism
H351A	inactive	Agrobacterium tumefaciens

Organism

Organism	UniProt	Comment	Textmining
Agrobacterium tumefaciens	A9CEJ9	-	-
Agrobacterium tumefaciens C58/ATCC 33970	A9CEJ9	-	-

Synonyms

Synonyms	Comment	Organism
Atu 3025	-	Agrobacterium tumefaciens

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)