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Literature summary extracted from

  • Pellis, A.; Ferrario, V.; Zartl, B.; Brandauer, M.; Gamerith, C.; Herrero Acero, E.; Ebert, C.; Gardossi, L.; Guebitz, G.
    Enlarging the tools for efficient enzymatic polycondensation Structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica (2016), Catal. Sci. Technol., 6, 3430-3442 .
No PubMed abstract available

Application

EC Number Application Comment Organism
3.1.1.74 synthesis use of enzyme for polycondensation. Under thin film conditions the covalently immobilized enzyme catalyzes the synthesis of oligoesters of dimetil adipate with different polyols leading to Mw of about 1900 and Mn of about 1000. Immobilized Cut1 retains 37% of hydrolytic activity Thermobifida cellulosilytica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.74 homology modeling of structure Thermobifida cellulosilytica

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Thermobifida cellulosilytica E9LVH8 isoform Cut1
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 dimethyl adipate + 1,4-butanediol
-
 Thermobifida cellulosilytica ?
-
 ?
3.1.1.74 dimethyl adipate + 1,4-decanediol
-
 Thermobifida cellulosilytica ?
-
 ?
3.1.1.74 dimethyl adipate + 1,4-hexanediol
-
 Thermobifida cellulosilytica ?
-
 ?
3.1.1.74 dimethyl adipate + 1,4-octanediol
-
 Thermobifida cellulosilytica ?
-
 ?