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Literature summary extracted from

  • Momeni, M.; Ubhayasekera, W.; Sandgren, M.; Stahlberg, J.; Hansson, H.
    Structural insights into the inhibition of cellobiohydrolase Cel7A by xylo-oligosaccharides (2015), FEBS J., 282, 2167-2177 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.91 purified catalytic modules of wild-type enzyme Cel7A and mutants E212Q and E217Q in complex with xylooligosaccharides, hanging drop vapor diffusion method, mixing of equal volumes of 6 mg/ml protein in 10 mM sodium acetate, pH 5.0, with reservoir solution containing 20% PEG 5000 monomethyl ether, 0.1 M MES, pH 6.0, 10 mM CoCl2, and 12.5% glycerol, microseeding, 1-2 days, X-ray diffraction structure determination and analysis at 1.42-1.89 A resolution, structure modelling. Each structure model contains all 434 amino acid residues of the HjeCel7A catalytic module, with an N-terminal pyroglutamate residue and an N-acetyl glucosamine residue bound to Asn270 Trichoderma reesei

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.91 E212Q site-directed mutagenesis, catalytic residue, inactive mutant Trichoderma reesei
3.2.1.91 E217Q site-directed mutagenesis, catalytic residue, inactive mutant Trichoderma reesei

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.91 additional information xylan and xylooligosaccharides (XOS) play a key role in inhibition of cellobiohydrolases of glycoside hydrolase family 7. Analysis of the binding mode at the entrance of the substrate-binding tunnel of the enzyme, in which each xylose residue is shifted about 2.4 A towards the catalytic center compared with binding of cello-oligosaccharides. Partial occupancy of two consecutive xylose residues at subsites -2 and -1 suggests an alternative binding mode for XOS in the vicinity of the catalytic center. The -1 xylosyl unit exhibits an open aldehyde conformation in one of the structures and a ring-closed pyranoside in another complex. Complementary inhibition studies with 4-nitrophenyl lactoside as substrate indicate mixed inhibition rather than pure competitive inhibition. Inhibitor binding structure analysis with wild-type and mutant Cel7A enzymes, detailed overview. No inhibition by xylose Trichoderma reesei
3.2.1.91 xylan from birchwood Trichoderma reesei
3.2.1.91 xylobiose mixed-type inhibition Trichoderma reesei
3.2.1.91 xylopentaose mixed-type inhibition Trichoderma reesei
3.2.1.91 xylotriose mixed-type inhibition Trichoderma reesei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.91 additional information
-
 additional information Michaelis-Menten kinetics Trichoderma reesei
3.2.1.91 1.6
-
 4-nitrophenyl lactoside pH 5.0, 37°C, recombinant wild-type enzyme Trichoderma reesei

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.91 extracellular
-
 Trichoderma reesei
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.91 Trichoderma reesei G0RVK1 i.e. Hypocrea jecorina
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.91 additional information the major enzyme, cellobiohydrolase Cel7A, constitutes nearly half of the total protein in the secretome Trichoderma reesei
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.91 4-nitrophenyl lactoside + H2O
-
 Trichoderma reesei 4-nitrophenol + lactose
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.91 37
-
 assay at Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.91 5
-
 assay at Trichoderma reesei

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.91 additional information
-
 additional information Michaelis-Menten kinetics indicating mixed-type inhibition Trichoderma reesei
3.2.1.91 9.7
-
 xylobiose pH 5.0, 37°C, inhibition of recombinant wild-type enzyme Trichoderma reesei
3.2.1.91 14
-
 xylopentaose pH 5.0, 37°C, inhibition of recombinant wild-type enzyme Trichoderma reesei
3.2.1.91 29
-
 xylotriose pH 5.0, 37°C, inhibition of recombinant wild-type enzyme Trichoderma reesei

General Information

EC Number General Information Comment Organism
3.2.1.91 evolution the enzyme belongs to the glycoside hydrolase family 7, GH7 Trichoderma reesei