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Chapter 23 : Metabolism of

Authors: Paul R. Wheeler1, Colin Ratledge2
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Affiliations: 1: Department of Clinical Sciences, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom; 2: Department of Applied Biology, University of Hull, Hull HU6 7RX, United Kingdom
Content Type: Monograph
Publication Year: 1994

Category: Fungi and Fungal Pathogenesis; Clinical Microbiology

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Abstract:

Researchers in mycobacterial biochemistry have almost exclusively concentrated their efforts on those aspects of metabolism that appear to be unique to members of the genus and have, in the absence of information to the contrary, assumed that other aspects of metabolism will be more or less the same as those of other, more amenable bacteria. In this chapter, the authors have chosen to follow the same elective pathway, concentrating on those aspects of metabolism that appear to be at least in some way unique to the mycobacteria and are, moreover, of relevance to the growth of as a pathogen within the tissues and fluids of its host. The peptidoglycan in mycobacteria is of a type common in many bacteria but with two slight differences. First, there are interpeptide linkages between two diaminopimelate residues as well as the usual D-alanyl-diaminopimelate linkages. Second, the usual N-acetylmuramic acid is replaced with N-glycolyl-muramic acid in and in other mycobacteria. An approach that might be appropriate would be to make probes for DNA based on appropriate genes identified in muramic acid metabolism from other microbes, as these genes would be expected to have some sequence similarity in all bacteria. There are many interesting and important implications for the new field of mycobacterial genetics: the complex organization of these microbes demands multiple genes for fatty acid biosynthesis and seemingly innumerable glycosyltransferase genes.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Metabolism of Mycobacterium tuberculosis
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Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
/content/10.1128/9781555818357.chap23.fig23-1
Figure 1

Metabolism of host carbon sources by intracellular mycobacteria (adapted from ). In addition, mycobacteria may also assimilate purines and pyrimidines and use these for nucleic acid biosynthesis. TCA, tricarboxylic acid.

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Figure 1

Metabolism of host carbon sources by intracellular mycobacteria (adapted from ). In addition, mycobacteria may also assimilate purines and pyrimidines and use these for nucleic acid biosynthesis. TCA, tricarboxylic acid.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Figure 2

Iron assimilation in microorganisms.

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Figure 2

Iron assimilation in microorganisms.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Figure 3

Structure of mycobactin, the intracellular siderophore of mycobacteria. For structures of other mycobactins, see and . Substituents: R1, alkyl chain up to C, often with double bond at Δ2 position, though occasionally, as with , this can be CH; R, —H or —CH; R —H or —CH; R, usually —CH or —CH, though occasionally, as with a long alkyl chain up to C; R, —H or —CH. For R is—CH, R = R = R = —H, and R is —CH.

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Figure 3

Structure of mycobactin, the intracellular siderophore of mycobacteria. For structures of other mycobactins, see and . Substituents: R1, alkyl chain up to C, often with double bond at Δ2 position, though occasionally, as with , this can be CH; R, —H or —CH; R —H or —CH; R, usually —CH or —CH, though occasionally, as with a long alkyl chain up to C; R, —H or —CH. For R is—CH, R = R = R = —H, and R is —CH.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Figure 4

Mechanism of iron uptake in mycobacteria as mediated by the exochelins and mycobactins.

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Figure 4

Mechanism of iron uptake in mycobacteria as mediated by the exochelins and mycobactins.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Figure 5

Possible biosynthetic pathways for phosphatidylinositolmannosides (PIM). PIM is strictly an intermediate and does not accumulate.

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Figure 5

Possible biosynthetic pathways for phosphatidylinositolmannosides (PIM). PIM is strictly an intermediate and does not accumulate.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Figure 6

Early dedicated stages of mycolate biosynthesis. , Speculated—reaction sought but not shown; , see Wheeler et al., 1993b; , methylation reaction shown but not for 24:1 -5.

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Image of Figure 6
Figure 6

Early dedicated stages of mycolate biosynthesis. , Speculated—reaction sought but not shown; , see Wheeler et al., 1993b; , methylation reaction shown but not for 24:1 -5.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Figure 7

Biosynthesis of methylmannose polysaccharide, x = 3 to 12.

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Image of Figure 7
Figure 7

Biosynthesis of methylmannose polysaccharide, x = 3 to 12.

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
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Tables

Metabolism of Mycobacterium tuberculosis
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Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
/content/10.1128/9781555818357.chap23.tab23-1
Table 1

Substrates that may be available to mycobacteria growing in the host

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Table 1

Substrates that may be available to mycobacteria growing in the host

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
/content/10.1128/9781555818357.chap23.tab23-2
Table 2

Growth and rates of synthesis of nucleic acids

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Generic image for table
Table 2

Growth and rates of synthesis of nucleic acids

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
/content/10.1128/9781555818357.chap23.tab23-3
Table 3

Heat shock proteins in and

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Generic image for table
Table 3

Heat shock proteins in and

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
/content/10.1128/9781555818357.chap23.tab23-4
Table 4

Occurrence of IREPs and HIPs as analyzed by SDS-PAGE in mycobacteria grown in vitro and in vivo

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Generic image for table
Table 4

Occurrence of IREPs and HIPs as analyzed by SDS-PAGE in mycobacteria grown in vitro and in vivo

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23
/content/10.1128/9781555818357.chap23.tab23-5
Table 5

Mannosyltransferases detected in mycobacteria

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10.1128/9781555818357/tab23-5.gif
Generic image for table
Table 5

Mannosyltransferases detected in mycobacteria

Citation: Wheeler P, Ratledge C. 1994. Metabolism of , p 353-385. In Bloom B (ed), Tuberculosis. ASM Press, Washington, DC. doi: 10.1128/9781555818357.ch23

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