By Author Unknown
Compliment for the Serial "This sequence has regularly awarded a well-balanced account if development in microbial physiology...Invaluable for instructing purposes." - AMERICAN SCIENTIST Advances in Microbial body structure used to be first released in 1967, and less than the pioneering editorship of Professor Tony Rose, with the collaboration at a variety of instances of John Wilkinson, Gareth Morris and Dave Tempest, the sequence has turn into immensely winning and influential. The editors have constantly striven to interpret microbial body structure within the broadest attainable context and feature by no means limited the contents to "traditional" perspectives of complete mobile body structure. Robert Poole was once appointed because the new editor following the premature loss of life of Tony Rose. less than Professor Poole's editorship, Advances in Microbial body structure keeps to put up topical and critical reports, and to interpret body structure as extensively as some time past by means of together with all fabric that contributes to the certainty of the way microorganisms and their part components paintings. This is still the true problem of microbial body structure.
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Extra resources for Adv in Microbial Physiology
1991c) and one of these is known to be functional (H. Ennis, personal communication). There are no fungal representatives. , 1993). , Clostridiurn spp. and Caldocellurn saccharolyticurn. They contain 130-170 amino acid residues; many are located internally. , 1992). So far, all representatives are from enzymes with catalytic domains belonging to family E. Family V I is a new family of CBDs found predominantly in xylanases. , 1994). 2. Functional Characterization of Cellulose-binding Domains Only some of the CBDs listed in Table 3 have been characterized biochemically.
A and E) are consistent with the existence of subtypes; however, at least CELLULOSE HYDROLYSIS BY BACTERIA AND FUNGI 23 three families contain enzymes with clearly different substrate specificities. Family D contains both p-174-glucanases and p-l,3(4)-glucanases; family H contains members with p-l74-rnannanase and p-174-glucanase activity; family A contains p-174-glucanases, p-1,3-glucanases, P-174-mannanases, cellodextrinases and at least one p-174-xylanase (Table 1). Other families show more subtle differences in substrate specificity: for example, Cex from C.
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.
Adv in Microbial Physiology by Author Unknown