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

By R. K. Poole

Compliment for the Serial"This sequence has continually provided a well-balanced account if growth in microbial physiology...Invaluable for educating 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 a number of occasions of John Wilkinson, Gareth Morris and Dave Tempest, the sequence has turn into immensely profitable and influential. The editors have continuously 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 physiology.Robert Poole used to be 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 submit topical and significant studies, and to interpret body structure as greatly as some time past by means of together with all fabric that contributes to the certainty of ways microorganisms and their part elements paintings. This is still the true problem of microbial body structure.

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Fusca endoglucanases show varying degrees of synergy with T. , 1993). It is unclear which particular properties allow an endoglucanase to act synergistically with a cellobiohydrolase. , 1990; Wood and McCrae, 1978); complex formation could involve proteinprotein interactions, or targeting of enzyme pairs, perhaps by CBDs, to particular sites on the cellulose surface. , 1984). However, the finding that T. , 1994). , 1993; Wood and McCrae, 1979), implies that protein-protein interactions, if involved, are not particularly specific.

Obviously, substrate specificities within cellulase families do differ. , 1994) shows that both enzymes have a similar size, approximately 50% sequence identity, and share superimposable dp-barrel folds; the two catalytic glutamic acid residues and the surrounding sequence regions are completely conserved. However, the two enzymes have quite distinct substrate specificities: one enzyme hydrolyzes P-1,3 linkages in p-(1,3) and P-(173)-/3-(1,6)-glucans;the other is active only on the p-( 1,4)-linkages in p-(1,3)-p-( 1,4)-glucans.

1994) Viswamitra et al. (1993) Spezio et al. (1993b) Campbell et al. (1993) Divne et al. (1994) Rouvinen et al. (1990) Divne et al. (1993) Ward et al. (1993) Torronen and Rouvinen (1995) Torronen et al. (1994) aFamilies are classified according to Gilkes et al. (1991b); Subtypes (BCguin, 1990) are designated by additional numbers. The alternative family nomenclature according to Henrissat and Bairoch (1993) is as follows: A, 5; B, 6; C, 7; E, 9; F, 10; G, 11; H, 12; K, 45. bCrystal structure solved.

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