Cellulase families and their genes

Knowles, Jonathan; Lehtovaara, Päivi; Teeri, Tuula T.

doi:10.1016/0167-7799(87)90102-8

Cited by 280 publications

(134 citation statements)

References 26 publications

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“…The region is susceptible to proteolytic cleavage by papain, and its presence prompts the question whether this stretch of amino acids may form a linker-region between the domains, similar to the glycosylated inter-domain spacer regions found in fungal cellulases [26,27]. In the case of cellulases, the spacer is ~30 residues long and separates the catalytic domain of the enzyme from its cellulose-binding domain to allow optimal operation of both domains on crystalline cellulose [26].…”

Section: Resultsmentioning

confidence: 99%

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

et al. 1995

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The eDNA of cellobiose dehydrogenase (CDH) fromPhanerochaete chrysosporium has been cloned and sequenced.The 5' end was obtained by PCR amplification. The cDNA contains 2310 translated bases excluding the poly(A) tail. The deduced mature protein contains 770 amino acid residues and is preceded by a 18 residue long signal peptide. The regions of the amino acid sequence corresponding to the heme and FAD domains of CDH were identified as well as the nucleotide-binding motif, the disulfide pairing and a methionine residue chelating the heme iron. No homologous sequences were found for the heme domain, however, the FAD domain appears to be distantly related to the GMC nxidoreductase family.

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Section: Resultsmentioning

confidence: 99%

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

et al. 1995

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“…It has been hypothesized that cellulose-specific CBMs may play a key role in disrupting the ordered hydrogen-bonding network in crystalline cellulose, making the surface chains accessible to the appended cellulase (Knowles et al, 1987;Teeri, 1997). There is biochemical, biophysical, and microscopic data (Din et al, 1994;Wang et al, 2008) indicating that CBMs mediate changes to the surface structure of cellulose.…”

Section: How Do Cbms Potentiate Catalysis?mentioning

confidence: 99%

The Biochemistry and Structural Biology of Plant Cell Wall Deconstruction

2010

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“…Many of these enzymes have a multiple domain architecture comprising one or several non-catalytic domains attached to a catalytic domain (Knowles et al, 1987;Gilkes et al, 1991). The location and boundaries of the various domains can often be readily deduced from amino acid sequence comparisons .…”

mentioning

confidence: 99%

Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases

Schou

Rasmussen

Kaltoft

et al. 1993

European Journal of Biochemistry

101

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The catalytic activity of nine enzymes (endoglucanases 1-111, V, VI and cellobiohydrolases I and I1 from Humicola insolens; endoglucanases A and C from Bacillus lautus), representative of cellulase families A-C, H, J and K, has been investigated using a series of reduced cellooligosaccharides (cellotriitol to cellohexaitol) as substrates. For each enzyme, the specificity of cleavage was determined by analytical HPLC while the kinetic constants were obtained from a kinetic assay involving a cellobiose dehydrogenase purified from H . insotens as a coupled enzyme using 2,6-dichloroindophenol as the electron acceptor. These data were used to estimate the number of subsites in the enzymes. The stereochemical course of hydrolysis by seven enzymes, representing the six different families, was assessed using 'H-NMR. The enzymes belonging to families which had already been investigated (A-C), showed results in agreement with previous studies. The three other families (H, J and K), for which no mechanistic data was previously available, gave results which indicated that enzymes in group H had retaining-type activity and enzymes in groups J and K had inverting-type activity. The retaining endoglucanases I and I11 displayed a high glycosyltransferase activity under the conditions used during the NMR experiments resulting in precipitates of higher oligomers.

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Cellulase families and their genes

Cited by 280 publications

References 26 publications

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

The Biochemistry and Structural Biology of Plant Cell Wall Deconstruction

Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases

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