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Advances in Microbial Physiology, Vol. 37 by R. K. Poole PDF

By R. K. Poole

ISBN-10: 0120277379

ISBN-13: 9780120277377

Compliment for the Serial"This sequence has regularly awarded a well-balanced account if development in microbial physiology...Invaluable for instructing purposes."- AMERICAN SCIENTISTAdvances in Microbial body structure was once first released in 1967, and lower than the pioneering editorship of Professor Tony Rose, with the collaboration at quite a few occasions of John Wilkinson, Gareth Morris and Dave Tempest, the sequence has turn into immensely profitable and influential. The editors have consistently striven to interpret microbial body structure within the broadest attainable context and feature by no means limited the contents to "traditional" perspectives of complete mobilephone physiology.Robert Poole used to be appointed because the new editor following the premature demise of Tony Rose. less than Professor Poole's editorship, Advances in Microbial body structure keeps to post topical and demanding stories, and to interpret body structure as greatly as some time past through together with all fabric that contributes to the certainty of the way microorganisms and their part components paintings. This remains to be the true problem of microbial body structure.

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Additional resources for Advances in Microbial Physiology, Vol. 37

Example text

Most of the early work on enzymatic cellulose hydrolysis involved 42 P. TOMME €7 AL. cellulases isolated from the supernatants of fungal cultures because the various components could be prepared with apparent ease. e. their combined activity on cellulose was greater than the sum of their individual activities. This effect is commonly observed with crystalline substrates but not soluble derivatives such as carboxymethylcellulose. Synergy is discussed here at some length because it is the focus of many studies on cellulase interactions in non-complexed systems; whether or not the same general principles also apply to complexed systems is not yet known.

1994). The approach relies upon the ability of an azide molecule to replace the acid-base catalyst when it is mutated to an alanine or glycine residue and should be applicable to any cloned cellulase or xylanase in which putative catalytic residues can be identified by sequence comparison. 4. Three-dimensional Structures of Cellulase and Xylanase Catalytic Domains X-ray crystallographic analysis of about 20 cellulases and xylanases has been reported or is in progress (Table 2). Although few three-dimensional structures have been solved, the number is steadily increasing.

I TsaXynA I 1 E2 I CBDlV I CBD 111 Fn3 I Fn3 IF n 3 ICBD El 111 1 7 CfiXynD I 16 ' I IBH Et 7 0Catalytic 7 I F I 7 domain (letters refer to cellulase family) Cellulose-binding domain (numbers refer to CBD family) Fn3 module Duplicated segment Nodulation B-like module C-terminal S-layer-like ILinkers module 171 repeat unknown function Is Is I s ] 22 P. TOMME ET AL. Table 2 Catalogue of cellulases and xylanases for which X-ray crystallographic analysis has been reported or is in progress. Family" H - G G G A3 F A4 A3 El F C K F F F B G C B C H G G Organism Aspergillus aculeatus Aspergillus oryzae Bacillus pumilus Bacillus circulans Bacillus sp.

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Advances in Microbial Physiology, Vol. 37 by R. K. Poole


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