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Literature summary for 4.2.2.11 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Agrobacterium tumefaciens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of native protein and its inactive mutant H531A in complex with alginate trisaccharide, at 2.10 and 2.99 A resolutions with final R-factors of 18.3 and 19.9%, respectively. The enzyme is comprised of an alpha/alpha-barrel plus anti-parallel beta-sheet as a basic scaffold. His311 and Tyr365 are 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
H311A 0.3% of wild-type activity Agrobacterium tumefaciens
H531A inactive Agrobacterium tumefaciens
R199A 4.3% of wild-type activity Agrobacterium tumefaciens
W467A 0.45% of wild-type activity Agrobacterium tumefaciens
Y365F 0.011% of wild-type activity Agrobacterium tumefaciens

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens A9CEJ9 polysaccharide lyase family 15
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14
-
wild-type, pH 7.5, 30°C Agrobacterium tumefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-L-guluronosyl linkage in alginate
-
Agrobacterium tumefaciens ?
-
?