A.H. Rose, D.W. Tempest (Ed.)'s Advances in Microbial Physiology, Vol. 36 PDF

By A.H. Rose, D.W. Tempest (Ed.)

ISBN-10: 0120277360

ISBN-13: 9780120277360

From the experiences of prior Volumes "This sequence has always awarded a well-balanced account of development in microbial physiology...Invaluable for educating purposes." -AMERICAN SCIENTIST

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Substrate Specificities of the Dipeptide Permease Studies similar to those used to characterize the Opp (Section VI. B2) have shown the Dpp to have analogous structural specificities, and to transport substrates with comparable kinetics. However, in one respect the specificity of the Dpp appears stricter than the Opp, in that loss or derivatization (amidation, esterification) of the C-terminal a-carboxyl on a dipeptide dramatically decreases its uptake capacity (Payne and Gilvarg, 1968a; Payne, 1973; Hirshfield and Price, 1975).

W. SMITH considered important for the function of binding proteins and is discussed by Quiocho (1990). Evidence for conformational changes has been obtained experimentally for many binding proteins, using a variety of techniques (Furlong, 1987). The most commonly used method is fluorescence-emission spectroscopy, as discussed previously. , 1992). The p l value of the protein from E. , 1986). 55 respectively; each of these species yields the same single band on a sodium dodecylsulphatepolyacrylamide gel and has an identical N-terminal sequence.

As a general observation, DppA expression seems somewhat variable amongst different strains of E. coli and S . typhimurium but the reasons for this are obscure. Expression of dpp has been studied in E. coli by monitoring DppA levels under different growth conditions, and in S. typhimurium using dpp-lacZ fusions. In the latter case, production of P-galactosidase (and thus, by presumption, dpp expression) was unaffected by growth in media containing glycerol or glucose, addition of casamino acids or peptides, the level of nitrogenous nutrients or anaerobic growth.

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Advances in Microbial Physiology, Vol. 36 by A.H. Rose, D.W. Tempest (Ed.)


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