Literature summary for 3.2.1.4 extracted from

Batista, P.R.; Costa, M.G.; Pascutti, P.G.; Bisch, P.M.; de Souza, W.
High temperatures enhance cooperative motions between CBM and catalytic domains of a thermostable cellulase: mechanism insights from essential dynamics (2011), Phys. Chem. Chem. Phys., 13, 13709-13720.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Thermobifida fusca	Cel9A presents both exo- and endo-cellulase activities, reaction mode, existence of an active conformer prior to ligand binding, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermobifida fusca	-	the bacterium produces six structurally and functionally distinct cellulases: Cel9B, Cel6A, Cel6B, Cel9A, Cel5A, Cel48A	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	Cel9A presents both exo- and endo-cellulase activities, reaction mode, existence of an active conformer prior to ligand binding, overview	Thermobifida fusca	?	-	?

Synonyms

Synonyms	Comment	Organism
Cel48A	-	Thermobifida fusca
Cel5A	-	Thermobifida fusca
Cel6A	-	Thermobifida fusca
Cel6B	-	Thermobifida fusca
Cel9A	-	Thermobifida fusca
Cel9B	-	Thermobifida fusca

General Information

General Information	Comment	Organism
additional information	mechanochemical model simulations and molecular dynamics of Cel9A, overview. Analysis of the electrostatic surface of the enzyme, overview	Thermobifida fusca

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Release 2023.1 (January 2023)