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Literature summary extracted from

  • Textor, L.C.; Colussi, F.; Silveira, R.L.; Serpa, V.; de Mello, B.L.; Muniz, J.R.; Squina, F.M.; Pereira, N.; Skaf, M.S.; Polikarpov, I.
    Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity (2013), FEBS J., 280, 56-69.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.176 cellobiose competitive inhibition; competitive inhibition Trichoderma harzianum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.176 3.4
-
 4-nitrophenyl D-cellobioside pH 5.0, 50°C Trichoderma harzianum
3.2.1.176 3.4
-
 4-nitrophenyl beta-D-cellobioside 50 mM sodium acetate buffer, pH 5.0, at 50°C Trichoderma harzianum
3.2.1.176 3.7
-
 2-chloro-4-nitrophenyl-beta-lactoside pH 5.0, 50°C Trichoderma harzianum
3.2.1.176 3.7
-
 2-chloro-4-nitrophenyl beta-D-lactoside 50 mM sodium acetate buffer, pH 5.0, at 50°C Trichoderma harzianum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.176 cellulose + H2O Trichoderma harzianum
-
 cellobiose + ?
-
 ?
3.2.1.176 cellulose + H2O Trichoderma harzianum IOC 3844
-
 cellobiose + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.176 Trichoderma harzianum
-
-
-
3.2.1.176 Trichoderma harzianum Q9P8P3
-
-
3.2.1.176 Trichoderma harzianum IOC 3844
-
-
-
3.2.1.176 Trichoderma harzianum IOC 3844 Q9P8P3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.176 glycoprotein predicted N-glycosylation sites at N126, N283 and N397 and the O-glycosylated linker, structure, overview Trichoderma harzianum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.176 2-chloro-4-nitrophenyl beta-D-lactoside + H2O
-
 Trichoderma harzianum 2-chloro-4-nitrophenol + lactose
-
 ?
3.2.1.176 2-chloro-4-nitrophenyl-beta-lactoside + H2O
-
 Trichoderma harzianum 2-chloro-4-nitrophenol + lactose
-
 ?
3.2.1.176 2-chloro-4-nitrophenyl-beta-lactoside + H2O
-
 Trichoderma harzianum IOC 3844 2-chloro-4-nitrophenol + lactose
-
 ?
3.2.1.176 4-nitrophenyl beta-D-cellobioside + H2O
-
 Trichoderma harzianum 4-nitrophenol + cellobiose
-
 ?
3.2.1.176 4-nitrophenyl beta-D-cellobioside + H2O
-
 Trichoderma harzianum IOC 3844 4-nitrophenol + cellobiose
-
 ?
3.2.1.176 4-nitrophenyl D-cellobioside + H2O
-
 Trichoderma harzianum 4-nitrophenol + D-cellobiose
-
 ?
3.2.1.176 4-nitrophenyl D-cellobioside + H2O
-
 Trichoderma harzianum IOC 3844 4-nitrophenol + D-cellobiose
-
 ?
3.2.1.176 avicel + H2O
-
 Trichoderma harzianum ?
-
 ?
3.2.1.176 avicel + H2O
-
 Trichoderma harzianum IOC 3844 ?
-
 ?
3.2.1.176 bacterial microcrystalline cellulose + H2O best substrate Trichoderma harzianum ?
-
 ?
3.2.1.176 bacterial microcrystalline cellulose + H2O best substrate Trichoderma harzianum IOC 3844 ?
-
 ?
3.2.1.176 carboxymethyl cellulose + H2O worst substrate Trichoderma harzianum ?
-
 ?
3.2.1.176 carboxymethyl cellulose + H2O worst substrate Trichoderma harzianum IOC 3844 ?
-
 ?
3.2.1.176 cellulose + H2O
-
 Trichoderma harzianum cellobiose + ?
-
 ?
3.2.1.176 cellulose + H2O
-
 Trichoderma harzianum IOC 3844 cellobiose + ?
-
 ?
3.2.1.176 additional information the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose Trichoderma harzianum ?
-
 ?
3.2.1.176 additional information the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose Trichoderma harzianum IOC 3844 ?
-
 ?
3.2.1.176 sigmacell 20 + H2O
-
 Trichoderma harzianum ?
-
 ?
3.2.1.176 sigmacell 20 + H2O
-
 Trichoderma harzianum IOC 3844 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.176 More enzyme molecular surface and structure analysis, overview Trichoderma harzianum

Synonyms

EC Number Synonyms Comment Organism
3.2.1.176 Cel7A
-
 Trichoderma harzianum
3.2.1.176 cellobiohydrolase I
-
 Trichoderma harzianum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.176 50
-
 assay at Trichoderma harzianum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.176 0.39
-
 4-nitrophenyl D-cellobioside pH 5.0, 50°C Trichoderma harzianum
3.2.1.176 0.39
-
 4-nitrophenyl beta-D-cellobioside 50 mM sodium acetate buffer, pH 5.0, at 50°C Trichoderma harzianum
3.2.1.176 0.74
-
 2-chloro-4-nitrophenyl-beta-lactoside pH 5.0, 50°C Trichoderma harzianum
3.2.1.176 0.74
-
 2-chloro-4-nitrophenyl beta-D-lactoside 50 mM sodium acetate buffer, pH 5.0, at 50°C Trichoderma harzianum

pH Optimum

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.176 0.02
-
 cellobiose pH 5.0, 50°C Trichoderma harzianum
3.2.1.176 7.2
-
 cellobiose 50 mM sodium acetate buffer, pH 5.0, at 50°C Trichoderma harzianum

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.2.1.176 7.2
-
 pH 5.0, 50°C Trichoderma harzianum cellobiose

General Information

EC Number General Information Comment Organism
3.2.1.176 metabolism Trichoderma harzianum secretes an effective and well-balanced enzymatic system that is able to completely hydrolyze cellulosic substrates into monomeric glucose Trichoderma harzianum
3.2.1.176 additional information cellobiohydrolase I has a shortened loop at the entrance of the cellulose-binding tunnel, the flexibility of Tyr260 is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. A larger flexibility in this region might facilitate the entry of the substrate into the tight binding tunnel of the enzyme. Structure analysis and molecular dynamics simulations, overview Trichoderma harzianum