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Literature summary extracted from

  • Roussel, X.; Lancelon-Pin, C.; Vikso-Nielsen, A.; Rolland-Sabate, A.; Grimaud, F.; Potocki-Veronese, G.; Buleon, A.; Putaux, J.L.; DHulst, C.
    Characterization of substrate and product specificity of the purified recombinant glycogen branching enzyme of Rhodothermus obamensis (2012), Biochim. Biophys. Acta, 1830, 2167-2177.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expression in Bacillus subtilis Rhodothermus marinus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.18 additional information
-
 additional information Km-value for amylose is 0.7 mg/ml, 30°C, pH 7.0 Rhodothermus marinus
2.4.1.18 additional information
-
 additional information enzyme reaction kinetics with different branched or unbranched alpha-glucans of controlled structure Rhodothermus marinus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.18 additional information Rhodothermus marinus the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Rhodothermus marinus Q93HU3
-
-
2.4.1.18 Rhodothermus marinus Q93HU3 gene glgB
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.18 108
-
 30°C, pH 7.0 Rhodothermus marinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylose potato type III amylose Rhodothermus marinus amylose containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 additional information a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity Rhodothermus marinus ?
-
 ?
2.4.1.18 additional information the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview Rhodothermus marinus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 RoBE
-
 Rhodothermus marinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.18 30
-
 assay at Rhodothermus marinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.18 7
-
 assay at Rhodothermus marinus

General Information

EC Number General Information Comment Organism
2.4.1.18 evolution the enzyme belongs to the glycoside hydrolase family GH13 Rhodothermus marinus
2.4.1.18 metabolism glycogen and starch branching enzymes catalyze the formation of alpha(1->6) linkages in storage polysaccharides by rearrangement of preexisting alpha-glucans. This reaction occurs through the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position. These enzymes define major elements that control the structure of both glycogen and starch Rhodothermus marinus