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Literature summary for 5.1.3.37 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
Search for more literature for 5.1.3.37

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
EDTA 1 mM, complete loss of activity Azotobacter vinelandii
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
Zn2+ 1.5 mM, complete inhibition Azotobacter vinelandii

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii Q44493
-
-

Renatured (Commentary)

Renatured (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
[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

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
 Azotobacter vinelandii

pH Range

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