Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.

Gilkes, Neil R.; Henrissat, Bernard; Kilburn, Douglas G.; Miller, Robert C.; Warren, R. A. J.

doi:10.1128/mmbr.55.2.303-315.1991

Cited by 572 publications

(333 citation statements)

References 61 publications

(110 reference statements)

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“…The CBDs belong to family I1 of CBDS,~ all of which are approximately the same size and contain conserved Trp, Asn, Gly, and Cys residues. 12 Although the CBDs of CenA and Cex can be separated from their catalytic domains by proteolysis, this is not a convenient way to prepare the relatively large quantities required for detailed characterization. The CBD of CenA (CBDcen~) can be readily obtainable in good yield by expression of the appropriate gene fragment in Escherichia coli.…”

Section: Introductionmentioning

confidence: 99%

The cellulose‐binding domain (CBD_Cex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

Ong

Gilkes

Miller

et al. 1993

Biotech & Bioengineering

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The gene fragment encoding the cellulose-binding domain (CBD) of an exoglucanase (Cex) from Cellulomonas fimi was subcloned and expressed in Escherichia coli. Transcription from the lac promoter coupled with translation from a consensus prokaryotic ribosome binding site led to the production of large quantities of CBD(Cex) (up to 25% total soluble cell protein). The polypeptide leaked into the culture supernatant (up to 50 mg . L(-1)), facilitating one-step purification by affinity chromatography on cellulose. The 11-kDa polypeptide reacted with Cex antiserum. Absence of free thiols indicated that the two Cys residues of CBD(Cex) form a disulfide bridge. It had the same N-terminal amino acid sequence as CBD(Cex) prepared from Cex by proteolysis, plus two additional N-terminal amino acid residues (Ala and Ser) encoded by the Nhel site introduced during plasmid construction. CBD(Cex) bound to a variety of beta-1, 4-glycans with different affinities and saturation levels. Adsorption to bacterial microcrystalline cellulose was dependent on the temperature, but not on the pH.

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Section: Introductionmentioning

confidence: 99%

The cellulose‐binding domain (CBD_Cex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

Ong

Gilkes

Miller

et al. 1993

Biotech & Bioengineering

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“…The degradation of cellotriose, at low concentrations (6-400 pM), by CBHII (0.1 -1.7 pM) was followed by HPLC. The time evolution of the saccharide concentrations was in a first attempt evaluated using Eqn (1). We assume that the off-rates of G,, G, and G, from the enzyme are fast compared to k,.…”

Section: Resultsmentioning

confidence: 99%

Progress-Curve Analysis Shows that Glucose Inhibits the Cellotriose Hydrolysis Catalysed by Cellobiohydrolase II from Trichoderma Reesei

Teleman¹,

Koivula²,

Reinikainen³

et al. 1995

Eur J Biochem

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NMR spectroscopy and HPLC were used to investigate the hydrolysis of cellotriose by cellobiohydrolase II from Trichoderma reesei. Substrate and product concentrations were followed as a function of time. Progress curves were calculated by forward numerical integration of the full kinetic equations and were fitted to the experimental data. Binding and rate constants were obtained from this fit, whereby no initial slope or Michaelis‐Menten approximation was used. The progress curves from a single experiment sufficed to produce agreement with the Michaelis‐Menten model (eight experiments). The absence of a kinetic isotope effect was proven. The progress‐curve analysis showed that a simple degradation model cannot describe the experimental time‐courses at substrate concentrations greater than 1 mM. A model containing competitive inhibition from cellobiose as well as non‐competitive inhibition from glucose was developed. This four‐parameter model accurately reproduces about 1000 experimental data points covering five orders of magnitude in oligosaccharide concentrations. Glucose binding to the enzyme/cellotriose complex retards, in a non‐competitive fashion, cellotriose hydrolysis by at least a factor of 30. A structural model for the non‐competitive inhibition is discussed. The NMR experiment also produced individual progress curves for the α and β anomers. The β anomer of cellotriose was degraded 2.5‐times faster than the α anomer.

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“…The genome of S. degradans encodes a wide range of polysaccharide-degrading enzymes, with approximately two thirds of the 180 candidate carbohydrate-active enzymes predicted to target plant polysaccharides [9]. As observed in other enzyme cocktails targeting the plant cell wall, many of these enzymes are appended to various CBMs and from family CBM2 in particular [26]. Sequence comparison, alone, cannot identify whether the Sde_1182 CBM2 binds cellulose or xylan.…”

Section: Discussionmentioning

confidence: 99%

Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown

Vincent¹,

Molin²,

Weiner³

et al. 2010

FEBS Letters

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a b s t r a c tSaccharophagus degradans belongs to a recently discovered group of marine bacteria equipped with an arsenal of sugar cleaving enzymes coupled to carbohydrate-binding domains to degrade various insoluble complex polysaccharides. The modular Sde-1182 protein consists of a family 2 carbohydrate binding module linked to a X158 domain of unknown function. The 1.9 Å and 1.55 Å resolution crystal structures of the isolated X158 domain bound to the two related polyisoprenoid molecules, ubiquinone and octaprenyl pyrophosphate, unveil a b-barrel architecture reminiscent of the YceI-like superfamily that resembles the architecture of the lipocalin fold. This unprecedented association coupling oxidoreduction and carbohydrate recognition events may have implications for effective nutrient uptake in the marine environment.

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Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.

Cited by 572 publications

References 61 publications

The cellulose‐binding domain (CBD_Cex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

The cellulose‐binding domain (CBD_Cex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

Progress-Curve Analysis Shows that Glucose Inhibits the Cellotriose Hydrolysis Catalysed by Cellobiohydrolase II from Trichoderma Reesei

Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown

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Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.

Cited by 572 publications

References 61 publications

The cellulose‐binding domain (CBDCex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

The cellulose‐binding domain (CBDCex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

Progress-Curve Analysis Shows that Glucose Inhibits the Cellotriose Hydrolysis Catalysed by Cellobiohydrolase II from Trichoderma Reesei

Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown

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Product

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The cellulose‐binding domain (CBD_Cex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide

The cellulose‐binding domain (CBD_Cex) of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide