Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose

Carrard, Géraldine; Koivula, Anu; Söderlund, Hans; Béguin, Pierre

doi:10.1073/pnas.160216697

Cited by 237 publications

(189 citation statements)

References 40 publications

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“…As shown in Figure 6B, the model predicts that lowering K dis EG1 by up to eightfold increases the overall hydrolysis rate by 11.3% for Avicel, 7.9% for filter paper, and 3.4% for bacterial cellulose. The prediction of higher hydrolysis rates accompanying higher affinity CBMs is consistent with experimental results showing that higher hydrolysis rates are obtained for the C. thermocellum endoglucanase CelD when it is linked to the C. thermocellum CipA CBM as compared to the CBMs from the T. reesei CBH1 and 2 and C. fimi Cex (Carrard et al, 2000). It may be noted that the predicted benefits of increasing K dis EG1 are larger at longer reaction times (data not shown).…”

Section: Cellulase Activity Improvementsupporting

confidence: 86%

“…In light of the availability of CBMs with a great range of dissociation constants (Klyosov, 1988), as well as several examples of CBM substitution in the literature (Carrard et al, 2000;Coutinho et al, 1993;Karita et al, 1996;Poole et al, 1991;Srisodsuk et al, 1997), we examined the impact of larger changes in K dis EG1 than considered in Figure 6A. As shown in Figure 6B, the model predicts that lowering K dis EG1 by up to eightfold increases the overall hydrolysis rate by 11.3% for Avicel, 7.9% for filter paper, and 3.4% for bacterial cellulose.…”

Section: Cellulase Activity Improvementmentioning

confidence: 99%

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A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang

Lynd

2006

Biotechnol. Bioeng.

201

157

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A new functionally based kinetic model for enzymatic hydrolysis of pure cellulose by the Trichoderma cellulase system is presented. The model represents the actions of cellobiohydrolases I, cellobiohydrolase II, and endoglucanase I; and incorporates two measurable and physically interpretable substrate parameters: the degree of polymerization (DP) and the fraction of b-glucosidic bonds accessible to cellulase, F a (Zhang and Lynd, 2004). Initial enzyme-limited reaction rates simulated by the model are consistent with several important behaviors reported in the literature, including the effects of substrate characteristics on exoglucanase and endoglucanase activities; the degree of endo/exoglucanase synergy; the endoglucanase partition coefficient on hydrolysis rates; and enzyme loading on relative reaction rates for different substrates. This is the first cellulase kinetic model involving a single set of kinetic parameters that is successfully applied to a variety of cellulosic substrates, and the first that describes more than one behavior associated with enzymatic hydrolysis. The model has potential utility for data accommodation and design of industrial processes, structuring, testing, and extending understanding of cellulase enzyme systems when experimental date are available, and providing guidance for functional design of cellulase systems at a molecular scale. Opportunities to further refine cellulase kinetic models are discussed, including parameters that would benefit from further study.

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Section: Cellulase Activity Improvementsupporting

confidence: 86%

Section: Cellulase Activity Improvementmentioning

confidence: 99%

A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang

Lynd

2006

Biotechnol. Bioeng.

201

157

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“…The family 9 CBM from xylanase 10A of Thermotoga maritima has a distinct specificity for only the reducing ends of polysaccharides, suggesting the intriguing notion of targeting to damaged regions of plant cell walls [32,33]. An elegant study by Carrard et al [34] showed that family 1 and family 3 CBMs that were appended to the same catalytic module displayed different capacities to degrade crystalline cellulose, implying that these non-catalytic modules can recognize distinct regions of this otherwise chemically invariant polysaccharide. This work was complemented further by studies demonstrating that examples of CBMs from families 17 and 28 recognize different regions of noncrystalline cellulose, influencing the ability of the enzyme to hydrolyse the polysaccharide [23].…”

Section: Cbm Binding and Polysaccharide Hydrolysismentioning

confidence: 99%

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Boraston

Bolam

Gilbert

et al. 2004

Biochemical Journal

1,733

1,694

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The enzymic degradation of insoluble polysaccharides is one of the most important reactions on earth. Despite this, glycoside hydrolases attack such polysaccharides relatively inefficiently as their target glycosidic bonds are often inaccessible to the active site of the appropriate enzymes. In order to overcome these problems, many of the glycoside hydrolases that utilize insoluble substrates are modular, comprising catalytic modules appended to one or more non-catalytic CBMs (carbohydrate-binding modules). CBMs promote the association of the enzyme with the substrate. In view of the central role that CBMs play in the enzymic hydrolysis of plant structural and storage polysaccharides, the ligand specificity displayed by these protein modules and the mechanism by which they recognize their target carbohydrates have received considerable attention since their discovery almost 20 years ago. In the last few years, CBM research has harnessed structural, functional and bioinformatic approaches to elucidate the molecular determinants that drive CBM-carbohydrate recognition. The present review summarizes the impact structural biology has had on our understanding of the mechanisms by which CBMs bind to their target ligands.

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“…This CBP exhibited a relatively high affinity for cellulose and was found to be essential for the degradation of crystalline cellulose (Goldstein et al, 1993). It is thought that CBD determines the efficiency of degradation of insoluble cellulose by concentrating cellulase catalytic domains on the surface of the insoluble cellulose substrate (Tomme et al, 1998;Carrard et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…cnrs-mrs.fr/˜pedro/CAZY/cbm.html). CBDs also differ in their binding affinity and substrate specificity (Carrard et al, 2000;McCartney et al, 2006). In plant-parasitic nematodes, the first CBP gene to be identified was Mi CBP-1 from the root-knot nematode Meloidogyne incognita (Ding et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Cellulose Binding Protein from the Parasitic Nematode Heterodera schachtii Interacts with Arabidopsis Pectin Methylesterase: Cooperative Cell Wall Modification during Parasitism

et al. 2008

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Plant-parasitic cyst nematodes secrete a complex of cell wall-digesting enzymes, which aid in root penetration and migration. The soybean cyst nematode Heterodera glycines also produces a cellulose binding protein (Hg CBP) secretory protein. To determine the function of CBP, an orthologous cDNA clone (Hs CBP) was isolated from the sugar beet cyst nematode Heterodera schachtii, which is able to infect Arabidopsis thaliana. CBP is expressed only in the early phases of feeding cell formation and not during the migratory phase. Transgenic Arabidopsis expressing Hs CBP developed longer roots and exhibited enhanced susceptibility to H. schachtii. A yeast two-hybrid screen identified Arabidopsis pectin methylesterase protein 3 (PME3) as strongly and specifically interacting with Hs CBP. Transgenic plants overexpressing PME3 also produced longer roots and exhibited increased susceptibility to H. schachtii, while a pme3 knockout mutant showed opposite phenotypes. Moreover, CBP overexpression increases PME3 activity in planta. Localization studies support the mode of action of PME3 as a cell wall-modifying enzyme. Expression of CBP in the pme3 knockout mutant revealed that PME3 is required but not the sole mechanism for CBP overexpression phenotype. These data indicate that CBP directly interacts with PME3 thereby activating and potentially targeting this enzyme to aid cyst nematode parasitism.

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Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose

Cited by 237 publications

References 40 publications

A functionally based model for hydrolysis of cellulose by fungal cellulase

A functionally based model for hydrolysis of cellulose by fungal cellulase

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Cellulose Binding Protein from the Parasitic Nematode Heterodera schachtii Interacts with Arabidopsis Pectin Methylesterase: Cooperative Cell Wall Modification during Parasitism

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