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Compliment for the Serial "This sequence has always provided a well-balanced account if development in microbial physiology...Invaluable for educating purposes." - AMERICAN SCIENTIST Advances in Microbial body structure was once first released in 1967, and less than the pioneering editorship of Professor Tony Rose, with the collaboration at a variety of occasions of John Wilkinson, Gareth Morris and Dave Tempest, the sequence has develop into immensely winning and influential. The editors have regularly striven to interpret microbial body structure within the broadest attainable context and feature by no means limited the contents to "traditional" perspectives of entire mobile body structure. Robert Poole was once appointed because the new editor following the premature demise of Tony Rose. below Professor Poole's editorship, Advances in Microbial body structure maintains to post topical and demanding stories, and to interpret body structure as generally as some time past via together with all fabric that contributes to the certainty of the way microorganisms and their part elements paintings. This is still the true problem of microbial body structure.

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Structural Families of Catalytic Domains The catalytic domains of nearly all cellulases and xylanases can be classified into one of a few distinct families on the basis of amino acid sequence similarities, although the degree of similarity is often low. , 1989). In general, structurally related proteins contain hydrophobic cores which retain a common fold and peripheral regions with more divergent structures (Chothia and Lesk, 1986). The success of hydrophobic cluster analysis can be attributed to its ability to detect regions corresponding to folds that are highly conserved because they are part of the catalytic core.

1988). , 1992). Removal of the CBDs from T. , 1988). Proteolytic removal of the B. succinogenes endoglucanase CBD decreases the activity of the enzyme for Avicel or regenerated cellulose two-fold, without significantly changing carboxymethylcellulase activity (McGavin and Forsberg, 1989). Similarly, grafting the T. , 1992). Two proposals have been made to explain how CBDs enhance enzyme activity on insoluble substrates: one is that they serve to increase the effective enzyme concentration on the substrate surface; the other, that they play a role in disrupting non-covalent associations, disrupting structure and thereby increasing substrate accessibility (Knowles et a l .

1992). It is now suggested that movement of the CBHI catalytic domain along the cellulose chain could weaken the interaction between adjacent molecules and render the substrate more accessible to other enzymes (Srisodsuk, 1994). e. , 1993). The CBD is clearly not essential for hydrolysis of crystalline cellulose: for example, the isolated CBHI catalytic domain can still hydrolyze highly crystalline bacterial cellulose (Srisodsuk, 1994), but further experimentation is necessary to define precise roles for these domains.

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