Advances in Microbial Physiology, Vol. 24 by A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.) PDF

By A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.)

ISBN-10: 0120277247

ISBN-13: 9780120277247

This quantity in a research-level sequence covers various elements of microbial body structure and biochemistry together with inositol metabolisms in yeasts, bacterial adhesion, natural acids, the bacterial flagellum and the mechanical behaviour of bacterial telephone partitions. it's meant to be of use to microbiologists, biochemists and biotechnologists. different comparable works during this sequence are volumes 29, 30 and 31.

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14). The other product, ammonia, is used as a source of intracellular nitrogen. As already mentioned, primary amines cannot serve as a carbon and energy source for yeasts. It could be argued that this might be due to the fact that the aldehyde reaction product cannot be utilized as an (intracellular) carbon source. Although this may hold, for example, for the utilization of propylamine or butylamine, it cannot explain the inability of yeasts to utilize, for +- rx M. VEENHUIS, J. P. VAN DIJKEN AND W.

The above examples clearly illustrate that peroxisomes may have an important function in the nitrogen metabolism of yeasts. Enhanced levels of specific oxidases and proliferation of peroxisomes during utilization of D-amino acids (D-amino acid oxidase) and uric acid (urate oxidase) have also been observed (K. B. Zwart, unpublished observations) supporting the hypothesis that peroxisomes may carry several specific oxidases involved in nitrogen metabolism. It is to be expected that in the near future the number of examples in which peroxisomes develop in fungi as a consequence of the need to utilize an unusual nitrogen source will be extended to utilization of diamines and polyamines which are generally metabolized via an oxidative attack by oxidases that produce hydrogen peroxide (Blaschko, 1963; Zeller, 1963).

Polymorpha was grown under methanol-limitation in chemostat culture, the ratio of alcohol oxidase and catalase varied considerably with the growth rate (van Dijken, 1976). Yet, under these conditions, the peroxisomes were completely crystalline, irrespective of the growth rate of these cells. , 1976,1979a)it is difficult to envisage that these organellescan be composed of the two enzymes in a fixed 1:l ratio. The distribution of alcohol oxidase and catalase activities in completely crystalline peroxisomes present in chemostat-grown cells of H.

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Advances in Microbial Physiology, Vol. 24 by A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.)

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