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Literature summary for 3.2.1.4 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
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Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Trichoderma reesei
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellulose + H2O
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 Trichoderma reesei ?
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 ?
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

Synonyms Comment Organism
Cel7A
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 Trichoderma reesei
family 7 cellobiohydrolase
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 Trichoderma reesei