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4.2.2.11: guluronate-specific alginate lyase

This is an abbreviated version!
For detailed information about guluronate-specific alginate lyase, go to the full flat file.

Word Map on EC 4.2.2.11

Reaction

[alpha-1,4-L-guluronate]n
=
alpha-L-guluronate
 +
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2

Synonyms

A1m, A9mC, A9mL, A9mT, Alg17C, Alg2A, Alg7D, AlgB, alginase II, alginate (poly-alpha-L-guluronate) lyase, alginate lyase, AlgL, AlgL5, AlgMytC, alkaliphilic alginate lyase, ALY, Aly-SJ02, Aly1, Aly5, AlyA, AlyA1PL7, AlyA5, AlyD, AlyDW11, AlyE, AlyQ, AlyV5, AXE80_11190, endo-type alginate lyase, guluronate lyase, KJ-2 alginate lyase, L-guluronan lyase, L-guluronate lyase, lyase, polyguluronate, Oal17A, oligoalginate lyase, poly(1,4-alpha-L-guluronide)lyase, poly(alpha-L-guluronate) lyase, poly-alpha-L-guluronate lyase, polyguluronate-specific alginate lyase, polyMG-specific alginate lyase, V12B01_09446, V12B01_24274, WP_053404615, xadAly7B

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.11 guluronate-specific alginate lyase

Crystallization

Crystallization on EC 4.2.2.11 - guluronate-specific alginate lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging-drop vapour-diffusion, structure at 1.2 A resolution
20°C, drop solution comprising 1.4 M NaCl, 0.1 M potassium sodium phosphate and 0.1 M 2-morpholinoethanesulfonate-sodium hydroxide pH 6.5, vapor-diffusion method, monoclinic cristals
-
homology modeling of structure. Residues Asn198, His199, Arg246, and Tyr253 are conserved for the catalytic active site
purified recombinant soluble His-tagged wild-type and selenomethionine-labeled enzyme, and two mutant enzymes H202L and Y258A, and Y258A DELTAMMG variant, free or in complex with an alginate trisaccharide, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in in 20 mM HEPES, pH 7.5, 100 mM KCl, with 0.1 M Tris, pH 8.0, 5% 2-methyl-2,4-pentanediol, 10% PEG 6000, 3 days, 16°C, X-ray diffraction structure determination and analysis at 1.85 A, 1.7 A, 2.45 A, and 1.9 A resolution, respectively
hanging-drop vapour-diffusion, A1-II structure at 2.2 A resolution, A1-II' structure at 1.0 A resolution
-
purified recombinant catalytic domain of AlyA1PL7, hanging drop vapor diffusion method, 0.002 ml of 11.3 mg/ml protein solution with 0.1 mg/ml oligoguluronate, are mixed with 0.001 ml of reservoir solution containing 0.2 M KSCN and 28% PEG-MME 2000, and equilibration against 0.5 ml reservoir solution, 21°C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.43 A resolution
purified recombinant full-length dimeric AlyA5, hanging drop vapor diffusion method, 0.002 ml of 7.7 mg/ml protein solution with 0.1 mg/ml oligoglucuronate, are mixed with 0.001 ml of reservoir solution containing PEG 3350 and 0.2 M sodium/potassium tartrate, and equilibration against 02 ml reservoir solution, 21°C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution