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Literature summary extracted from

  • Hashimoto, W.; Miyake, O.; Momma, K.; Kawai, S.; Murata, K.
    Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate (2000), J. Bacteriol., 182, 4572-4577.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.2.3 Ca2+ 1.4-2fold increase in activity of oligoalginate lyase at 1 mM Sphingomonas sp.
4.2.2.3 Fe2+ 1.4-2fold increase in activity of oligoalginate lyase at 1 mM Sphingomonas sp.
4.2.2.3 Mg2+ 1.4-2fold increase in activity of oligoalginate lyase at 1 mM Sphingomonas sp.
4.2.2.3 Mn2+ 1.4-2fold increase in activity of oligoalginate lyase at 1 mM Sphingomonas sp.
4.2.2.3 additional information oligoalginate lyase is not affected by addition of 1 mM EDTA, GSH, 2-mercaptoethanol, iodoacetic acid, N-ethylmaleimide, and sugars at 5 mM, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on oligoalginate lyase by Cu2+, Co2+, and Hg2+ at 1 mM Sphingomonas sp.
4.2.2.26 dithiothreitol 1 mM, 7fold stimulation Sphingomonas sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.3 gene encoding the oligoalginate lyase, DNA sequence determination and analysis, genetic mapping Sphingomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.2.3 additional information oligoalginate lyase is not affected by addition of 1 mM EDTA, GSH, 2-mercaptoethanol, iodoacetic acid, N-ethylmaleimide, and sugars at 5 mM, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on oligoalginate lyase by Cu2+, Co2+, and Hg2+ at 1 mM Sphingomonas sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.2.3 cytosol
-
 Sphingomonas sp. 5829
-
4.2.2.26 cytoplasm
-
 Sphingomonas sp. 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.2.26 Ca2+ 1.4- to 2fold stimulation Sphingomonas sp.
4.2.2.26 Fe2+ 1.4- to 2fold stimulation Sphingomonas sp.
4.2.2.26 Mg2+ 1.4- to 2fold stimulation Sphingomonas sp.
4.2.2.26 Mn2+ 1.4- to 2fold stimulation Sphingomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.2.3 83000
-
 oligoalginate lyase, native PAGE Sphingomonas sp.
4.2.2.3 85000
-
 1 * 85000, oligoalginate lyase, SDS-PAGE Sphingomonas sp.
4.2.2.26 85000
-
 x * 86543, calculated, x * 85000, SDS-PAGE Sphingomonas sp.
4.2.2.26 86543
-
 x * 86543, calculated, x * 85000, SDS-PAGE Sphingomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.2.3 alginate Sphingomonas sp. incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III ?
-
 ?
4.2.2.3 disaccharides of alginate Sphingomonas sp. oligoalginate lyase, complete depolymerization of alginate monosaccharides of alginate
-
 ?
4.2.2.3 trisaccharides of alginate Sphingomonas sp. oligoalginate lyase, complete depolymerization of alginate monosaccharides of alginate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Sphingomonas sp.
-
 isoforms A1-I, A1-II, and A1-III of alginate lyase, 1 oligoalginate lyase
-
4.2.2.26 Sphingomonas sp.
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.2.2.3 proteolytic modification A1-I is autolytically cleaved into A1-II and A1-III, which shows different substrate specificities, therfore A1-I possesses 3 active sites, 1 protease and 2 alginate lyase sites Sphingomonas sp.

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.2.3 40.8fold Sphingomonas sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.2.3 additional information
-
-
 Sphingomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.3 alginate substrate of alginate lyase isozymes A1-I, A1-II, and A1-III Sphingomonas sp. ?
-
 ?
4.2.2.3 alginate incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III Sphingomonas sp. ?
-
 ?
4.2.2.3 disaccharides of alginate oligoalginate lyase Sphingomonas sp. monosaccharides of alginate
-
 ?
4.2.2.3 disaccharides of alginate oligoalginate lyase, complete depolymerization of alginate Sphingomonas sp. monosaccharides of alginate
-
 ?
4.2.2.3 additional information oligoalginate lyase substrate specificity Sphingomonas sp. ?
-
 ?
4.2.2.3 trisaccharides of alginate oligoalginate lyase Sphingomonas sp. monosaccharides of alginate
-
 ?
4.2.2.3 trisaccharides of alginate oligoalginate lyase, complete depolymerization of alginate Sphingomonas sp. monosaccharides of alginate
-
 ?
4.2.2.26 algino-oligosaccharide
-
 Sphingomonas sp. unsaturated algino-monosaccharides
-
 ?
4.2.2.26 algino-polysaccharide
-
 Sphingomonas sp. unsaturated algino-monosaccharides
-
 ?
4.2.2.26 additional information no substrates: alginate, poly(beta-(1->4)-D-mannuronate), poly(alpha-(1->4)-L-guluronate) Sphingomonas sp. ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.2.3 monomer 1 * 85000, oligoalginate lyase, SDS-PAGE Sphingomonas sp.
4.2.2.26 ? x * 86543, calculated, x * 85000, SDS-PAGE Sphingomonas sp.

Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 oligoalginate lyase
-
 Sphingomonas sp.
4.2.2.26 oligoalginate lyase
-
 Sphingomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.2.3 37
-
-
 Sphingomonas sp.
4.2.2.26 37
-
-
 Sphingomonas sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.2.3 40
-
 stable below, 10 min, pH 7.2 Sphingomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.2.3 8
-
-
 Sphingomonas sp.
4.2.2.26 8
-
-
 Sphingomonas sp.