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4.2.2.3: mannuronate-specific alginate lyase

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

Word Map on EC 4.2.2.3

Reaction

R2-beta-D-mannuronic acid-R1
=
R2-OH
 +
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1

Synonyms

(poly alpha-l-guluronate) lyase, A1 alginate lyase, A1-II, A1-III, A1-IV', A1m, A1mU, A9mC, A9mL, A9mT, AAlyase, AkAly30, AL2, alg, ALG-5, Alg-A, Alg17C, Alg2A, Alg7D, AlgA, AlgB, AlgE7, AlgI, alginase I, alginate lyase, alginate lyase A, alginate lyase A1-II, alginate lyase A1-II', alginate lyase A1-III, alginate lyase AlyPEEC, alginate lyase Atu3025, alginate lyase B, alginate lyase C, alginate lyase I, alginate lyase VI, alginate lyase1-III, AlgL, ALY, ALY-1, Aly-SJ02, Aly1, Aly2, Aly28, Aly30, Aly32, Aly33, Aly35, Aly7B, AlyA, AlyA1, AlyA2, AlyA3, AlyA5, AlyB, AlyDW11, ALYIII, alyPEEC, AlyPI, AlyPM, AlyQ, AlyV5, AlyVI, Atu3025, AXE80_11190, CL2, EC 4.2.99.4, endo-type alginate lyase, endolytic poly(M) lyase, endolytic polymannuronate lyase, exotype alginate lyase, HdAlex, hdalex-1, HdAly, KJ-2 alginate lyase, LbAly28, lyase AlyA, lyase, alginate, Lysis protein, M block-specific polymannuronate lyase, mannuronate alginate lyase, MJ-3 alginate lyase, More, MY04_2544, NIS_0185, Oal17A, oligoalginate lyase, PL-5 alginate lyase, PM lyase, poly(1,4-beta-D-mannuronide) lyase, poly(beta-D-1,4-mannuronide) lyase, Poly(beta-D-mannuronate) lyase, poly(M) lyase, poly(M)lyase, Poly(mana) alginate lyase, poly(mana)alginate lyase, polymannuronate lyase, polyMG-specific alginate lyase, protein PA1167, SP2, V12B01_24254, V12B01_24259, WP_053404615

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.3 mannuronate-specific alginate lyase

Crystallization

Crystallization on EC 4.2.2.3 - mannuronate-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
crystallization at 20°C by sitting-drop vapour diffusion with polyethylene glycol 4000 as a precipitant. X-ray analysis shows that the Atu3025 crystal belong to space group P2(1) and diffracted to 2.8 A resolution, with unit cell parameters a = 107.7, b = 108.3, c = 149.5 A, beta = 91.5°
-
wild type and mutant enzyme H531A in complex with alginate trisaccharide, sitting drop vapor diffusion method, using 80 mM Tris-HCl (pH 8.5), 24% (w/v) polyethylene glycol 4,000, 0.16 M magnesium chloride, and 20% (v/v) glycerol
crystal structure at 1.77 A resolution and putative substrate-binding model. The enzyme adopts a beta-jelly roll fold at the core of the structure and residues Lys99, Tyr140, and Tyr142 form catalytic residues in the active site
hanging-drop vapour-diffusion method, 1.2 A resolution
-
structure at 1.54 A resolution and modeling of binding of 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-Gluc-Man-Gluc and Man-Gluc-Man
hanging-drop vapour diffusion method, crystal structure determined at 2.0 A resolution. PA1167 forms a glove-like beta-sandwich composed of 15 beta-strands and 3 alpha-helices
-
purified recombinant His-tagged AlgL28-362 protein, hanging drop vapour diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate, pH 4.6, 28% w/v PEG 4000, 0.3 M PIPES, method optimization, 4 days, 20°C, X-ray diffraction structure determination and analysis at 1.64 A resolution
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
8 mg/ml purified isozyme A1-III complexed with trisaccharide product 4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid, hanging drop vapour diffusion method, 0.1 M HEPES, pH 7.5, containg 48% PEG w/v saturated ammonium sulfate, 290 mM trisaccharide, 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
hanging drop vapour diffusion method, 0.003 ml protein solution: 17.2 mg/ml protein, 0.1 M HEPES, pH 7.5, + 0.003 ml bottom solution: 47-49% saturated ammonium sulfate, 0.1 M HEPES, pH 7.5, 20°C, 1 month, for large crystals micro- and macroseeding is used, crystal are soaked in heavy-atom derivatives for 1-4 h for X-ray diffraction structure determination and analysis at 1.78-10.0 A resolution
-
purified isozyme A1-II, hanging drop vapour diffusion method, 0.003 ml protein solution: 38 mg/ml protein, 50 mM Tris-HCl, pH 7.5, + 0.003 ml bottom solution: 0.1 M Tris-HCl, pH 8.5, 43% saturated ammonium sulfate, 8% PEG 4000, 0.2 M Li2SO4, 20°C, 1 month, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
purified recombinant mutants H192A and Y246F complexed with substrate 4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)2-mannuronic acid, hanging drop vapour diffusion method, 10 mg/ml protein in solution is mixed with reservoir solution containing 24% w/v PEG 4000, 0.3 M ammonium acetate, 0.1 M sodium citrate pH 5.5, 20°C, 1 month, X-ray diffraction structure determination and analysis at 2.2 resolution, final models of the complex forms, which comprise two monomers (of 353 amino-acid residues each), 268-287 water molecules and two tetrasaccharide substrates
recombinant
-
recombinant, alginate lyase A1-II and alginate lyase A1-II'. Both proteins are crystallized at 20°C using hanging-drop vapour-diffusion method. A crystal of A-1II belongs to space group P2(1) and diffracts to 2.2 A resolution, with unit-cell parameters a = 51.3 A, b = 30.1 A, c = 101.6 A, beta = 100.2°. Crystals of A1-II' belong to space group P2(1)2(1)2(1) and diffract to 1.0 A resolution, with unit-cell parameters a = 34.6, b = 68.5, c = 80.3 A
-
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 0.2 ml reservoir solution, 21°C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution