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Literature summary for 4.2.2.25 extracted from

  • Derekova, A.; Atanassova, M.; Christova, P.; Tchorbanov, B.; Shosheva, A.; Mandeva, R.; Rodríguez-Alonso, P.; Garabal, J.I.; Kambourova, M.
    Physicochemical characteristics of a thermostable gellan lyase from Geobacillus stearothermophilus 98 (2010), Z. Naturforsch. C, 65, 231-238.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method at 18°C Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
216000
-
capillary gel electrophoresis Geobacillus stearothermophilus
220000
-
x * 220000, SDS-PAGE Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
gellan Geobacillus stearothermophilus gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination. Gellan is depolymerized first by gellan lyase and the received tetrasaccharide further hydrolyzed by certain exoenzymes which are found outside the cell in the stationary phase ?
-
?
gellan Geobacillus stearothermophilus 98 gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination. Gellan is depolymerized first by gellan lyase and the received tetrasaccharide further hydrolyzed by certain exoenzymes which are found outside the cell in the stationary phase ?
-
?

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P85513
-
-
Geobacillus stearothermophilus 98 P85513
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gellan gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination. Gellan is depolymerized first by gellan lyase and the received tetrasaccharide further hydrolyzed by certain exoenzymes which are found outside the cell in the stationary phase Geobacillus stearothermophilus ?
-
?
gellan gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination Geobacillus stearothermophilus ?
-
?
gellan gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination. Gellan is depolymerized first by gellan lyase and the received tetrasaccharide further hydrolyzed by certain exoenzymes which are found outside the cell in the stationary phase Geobacillus stearothermophilus 98 ?
-
?
gellan gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination Geobacillus stearothermophilus 98 ?
-
?

Subunits

Subunits Comment Organism
? x * 220000, SDS-PAGE Geobacillus stearothermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
at pH 7.2 and a protein concentration above 1 mg/ml large exothermic aggregation occurrs near Tm (75°C) rendering that the unfolding transition is irreversible Geobacillus stearothermophilus