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Literature summary extracted from

  • Beckham, G.T.; Matthews, J.F.; Bomble, Y.J.; Bu, L.; Adney, W.S.; Himmel, M.E.; Nimlos, M.R.; Crowley, M.F.
    Identification of amino acids responsible for processivity in a family 1 carbohydrate-binding module from a fungal cellulase (2010), J. Phys. Chem. B, 114, 1447-1453.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.4 cellulose + H2O Trichoderma reesei
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Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Trichoderma reesei
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 cellulose + H2O
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 Trichoderma reesei ?
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3.2.1.4 cellulose + H2O the family 1 carbohydrate-binding module, CBM, mediates the interaction between enzyme and crystalline cellulose surface via residues Y5, Q7, N29, and Y32, thus CBM is responsible for anchoring the enzyme at discrete points along a cellulose chain to aid in both recognizing cellulose chain ends for initial attachment to cellulose as well as aid in enzymatic catalysis by diffusing between stable wells on a length scale commensurate with the catalytic, processive cycle of Cel7A during cellulose hydrolysis, molecular-level mechanisms of recognition and interaction, overview Trichoderma reesei ?
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Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 Cel7A
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 Trichoderma reesei
3.2.1.4 family 7 cellobiohydrolase
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 Trichoderma reesei