Isomerases;
Racemases and epimerases;
Acting on carbohydrates and derivatives
BRITE hierarchy

[mannuronan]-beta-D-mannuronate 5-epimerase

[mannuronan]-beta-D-mannuronate = [alginate]-alpha-L-guluronate

(other) R08693
Reaction

[mannuronan]-beta-D-mannuronate

The enzyme epimerizes the C-5 bond in some beta-D-mannuronate residues in mannuronan, converting them to alpha-L-guluronate residues, and thus modifying the mannuronan into alginate. It is found in brown algae and alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.

EC 5.1.3.37 created 2015

1  [PMID:8144447]

Franklin MJ, Chitnis CE, Gacesa P, Sonesson A, White DC, Ohman DE

Pseudomonas aeruginosa AlgG is a polymer level alginate C5-mannuronan epimerase.

J Bacteriol 176:1821-30 (1994)
DOI:10.1128/JB.176.7.1821-1830.1994

[pae:PA3545]

2  [PMID:11707327]

Morea A, Mathee K, Franklin MJ, Giacomini A, O'Regan M, Ohman DE

Characterization of algG encoding C5-epimerase in the alginate biosynthetic gene  cluster of Pseudomonas fluorescens.

Gene 278:107-14 (2001)
DOI:10.1016/S0378-1119(01)00685-0

3  [PMID:14526115]

Nyvall P, Corre E, Boisset C, Barbeyron T, Rousvoal S, Scornet D, Kloareg B, Boyen C

Characterization of mannuronan C-5-epimerase genes from the brown alga Laminaria  digitata.

Plant Physiol 133:726-35 (2003)
DOI:10.1104/pp.103.025981

4  [PMID:12581364]

Jain S, Franklin MJ, Ertesvag H, Valla S, Ohman DE

The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa.

Mol Microbiol 47:1123-33 (2003)
DOI:10.1046/j.1365-2958.2003.03361.x

5  [PMID:15968068]

Douthit SA, Dlakic M, Ohman DE, Franklin MJ

Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed beta-helix.

J Bacteriol 187:4573-83 (2005)
DOI:10.1128/JB.187.13.4573-4583.2005

6  [PMID:24398681]

Wolfram F, Kitova EN, Robinson H, Walvoort MT, Codee JD, Klassen JS, Howell PL

Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG.

J Biol Chem 289:6006-19 (2014)
DOI:10.1074/jbc.M113.533158

[pst:PSPTO_1238]