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Literature summary for 4.2.2.3 extracted from

  • Thomas, F.; Lundqvist, L.C.; Jam, M.; Jeudy, A.; Barbeyron, T.; Sandstroem, C.; Michel, G.; Czjzek, M.
    Comparative characterization of two marine alginate lyases from Zobellia galactanivorans reveals distinct modes of action and exquisite adaptation to their natural substrate (2013), J. Biol. Chem., 288, 23021-23037.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.2.3

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis, recombinant expression of His-tagged AlyA5 in Escherichia coli strain BL21(DE3) Zobellia galactanivorans

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Zobellia galactanivorans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information dimeric AlyA5 shows two-phase kinetics with alginate, overview Zobellia galactanivorans

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ at least 2 mM Ca2+ in the reaction mixture is essential for the activity Zobellia galactanivorans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38300
-
 monomeric recombinant His-tagged enzyme, gel filtration Zobellia galactanivorans
42000
-
 x * 42000, recombinant His-tagged enzyme, SDS-PAGE Zobellia galactanivorans
69500
-
 dimeric recombinant His-tagged enzyme, gel filtration Zobellia galactanivorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sodium alginate Zobellia galactanivorans AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11 ?
-
 ?
sodium alginate Zobellia galactanivorans DSM 12802 AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Zobellia galactanivorans G0L2Y1
-
-
Zobellia galactanivorans DSM 12802 G0L2Y1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity Zobellia galactanivorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure Zobellia galactanivorans ?
-
 ?
additional information the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure Zobellia galactanivorans DSM 12802 ?
-
 ?
poly(beta-D-manuronate)
-
 Zobellia galactanivorans ?
-
 ?
poly(beta-D-manuronate)
-
 Zobellia galactanivorans DSM 12802 ?
-
 ?
sodium alginate AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11 Zobellia galactanivorans ?
-
 ?
sodium alginate LC mass and NMR spectrometris product analysis Zobellia galactanivorans ?
-
 ?
sodium alginate AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11 Zobellia galactanivorans DSM 12802 ?
-
 ?
sodium alginate LC mass and NMR spectrometris product analysis Zobellia galactanivorans DSM 12802 ?
-
 ?

Subunits

Subunits Comment Organism
monomer or dimer x * 42000, recombinant His-tagged enzyme, SDS-PAGE Zobellia galactanivorans

Synonyms

Synonyms Comment Organism
AlyA5
-
 Zobellia galactanivorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Zobellia galactanivorans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 45 temperature profile, overview Zobellia galactanivorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Zobellia galactanivorans

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 pH profile, narrow activity range, overview Zobellia galactanivorans

General Information

General Information Comment Organism
evolution AlyA5 belongs to the PL7 family, subfamily 5, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism Zobellia galactanivorans
additional information secondary structure comparison of AlyA5 and AlyA1PL7 Zobellia galactanivorans