Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kari, J.; Olsen, J.; Borch, K.; Cruys-Bagger, N.; Jensen, K.; Westh, P.
    Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity (2014), J. Biol. Chem., 289, 32459-32468.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.176 gene cel7A, heterologous expression of wild-type and mutant enzymes in Aspergillus oryzae Trichoderma reesei

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.176 W38A site-directed mutagenesis, Trp38 in the middle of the active tunnel is replaced with an alanine. This mutation weakens complex formation, and the population of substrate-bound W38A is only about half of the wild-type. Nevertheless, the maximal, steady-state rate is twice as high for the variant enzyme compared to the wild-type enzyme Trichoderma reesei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.176 additional information
-
 additional information comparative analysis of steady-state kinetics, adsorption, and processivity for wild-type enzyme and the W38A variant, full-length enzymes and catalytic domains with substrate Avicel PH 101, detailed overiew Trichoderma reesei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.176 Avicel PH 101 + H2O Trichoderma reesei cellobiose production is monitored by an amperometric enzyme biosensor based on cellobiose dehydrogenase from Phanerochaete chrysosporium adsorbed onto the surface of a benzoquinone-modified carbon paste electrode ?
-
 ?
3.2.1.176 cellulose + H2O Trichoderma reesei cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. Occuring opposite effects on binding and activity by the enzyme can be reconciled if the rate-limiting step is after the catalysis (i.e. in the dissociation process), analysis of the rate-limiting step for cellobiohydrolases, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.176 Trichoderma reesei G0RVK1 an anamorph of the fungus Hypocrea jecorina, gene cel7A
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.176 Avicel PH 101 + H2O cellobiose production is monitored by an amperometric enzyme biosensor based on cellobiose dehydrogenase from Phanerochaete chrysosporium adsorbed onto the surface of a benzoquinone-modified carbon paste electrode Trichoderma reesei ?
-
 ?
3.2.1.176 cellulose + H2O cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. Occuring opposite effects on binding and activity by the enzyme can be reconciled if the rate-limiting step is after the catalysis (i.e. in the dissociation process), analysis of the rate-limiting step for cellobiohydrolases, overview Trichoderma reesei ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.176 Cel7A
-
 Trichoderma reesei
3.2.1.176 cellobiohydrolase
-
 Trichoderma reesei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.176 25
-
 assay at Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.176 5
-
 assay at Trichoderma reesei

General Information

EC Number General Information Comment Organism
3.2.1.176 additional information enzyme and catalytic tunnel structure, overview Trichoderma reesei