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Literature summary extracted from

  • Hoidal, H.K.; Ertesvag, H.; Skjak-Braek, G.; Stokke, B.T.; Valla, S.
    The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism (1999), J. Biol. Chem., 274, 12316-12322.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.37 expression in Escherichia coli Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.37 EDTA 1 mM, complete loss of activity Azotobacter vinelandii
5.1.3.37 NaCl additions up to 0.1 M do not reduce the activity much, at 0.5 M NaCl less than 10% of the activity is retained Azotobacter vinelandii
5.1.3.37 Zn2+ 1.5 mM, complete inhibition Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.37 0.018
-
 [alginate]-beta-D-mannuronate pH 6.8, 37°C Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.3.37 Ca2+ required, optimum concentration 1-3 mM Azotobacter vinelandii
5.1.3.37 Sr2+ may substitute for Ca2+ with an efficiency of about 30% Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.3.37 57700
-
 x * 57700, calculated, x * 79000, SDS-PAGE Azotobacter vinelandii
5.1.3.37 79000
-
 x * 57700, calculated, x * 79000, SDS-PAGE Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.37 Azotobacter vinelandii Q44493
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
5.1.3.37 epimerase activity of AlgE4 preincubated with 1 mM Na2EDTA can be restored by the addition of a molar excess of Ca2+ Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.37 additional information the enzyme either slides along the alginate chain during catalysis or recognizes a pre-existing G residue as a preferred substrate in its consecutive attacks Azotobacter vinelandii ?
-
 ?
5.1.3.37 [alginate]-beta-D-mannuronate
-
 Azotobacter vinelandii [alginate]-alpha-L-guluronate during epimerization of alginate, the fraction of GMG blocks increases linearly as a function of the total fraction of G residues and comparably much faster than that of MMG blocks ?

Subunits

EC Number Subunits Comment Organism
5.1.3.37 ? x * 57700, calculated, x * 79000, SDS-PAGE Azotobacter vinelandii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.3.37 37
-
-
 Azotobacter vinelandii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.3.37 50
-
 stable up to Azotobacter vinelandii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.3.37 14
-
 [alginate]-beta-D-mannuronate pH 6.8, 37°C Azotobacter vinelandii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.3.37 6.5 7
-
 Azotobacter vinelandii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.3.37 8
-
 complete loss of activity above Azotobacter vinelandii