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Literature summary for 3.2.1.176 extracted from

  • Guimaraes, B.G.; Souchon, H.; Lytle, B.L.; David Wu, J.H.; Alzari, P.M.
    The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome (2002), J. Mol. Biol., 320, 587-596.
    View publication on PubMed
Search for more literature for 3.2.1.176

Crystallization (Commentary)

Crystallization (Comment) Organism
catalytic domain in complex with cellohexaose and cellobiose Acetivibrio thermocellus
crystals of truncated CelS in complex with cellobiose are obtained by ammonium sulfate precipitation, crystal structure of the catalytic domain of Clostridium thermocellum CelS in complex with oligosaccharides Acetivibrio thermocellus

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Acetivibrio thermocellus role in the cellusome, an active cellulase system ?
-
 ?

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
-
-
Acetivibrio thermocellus P0C2S5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Acetivibrio thermocellus

Reaction

Reaction Comment Organism Reaction ID
2 cellohexaose + 2 H2O = 2 cellotriose + cellotetraose + cellobiose mechanism Acetivibrio thermocellus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellohexaose + H2O
-
 Acetivibrio thermocellus cellobiose + cellotetraose
-
 ?
additional information role in the cellusome, an active cellulase system Acetivibrio thermocellus ?
-
 ?

Synonyms

Synonyms Comment Organism
celS
-
 Acetivibrio thermocellus