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Chapter 5 : Biosynthesis and Function of Membrane Lipids

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Abstract:

This chapter focuses on the aspects of lipid metabolism that differ from those of the better-studied gram-negative bacteria. The primary focus is on because of the availability of its genome sequence and its advantages in genetic analysis, but data from related species has been incorporated when appropriate. The chapter describes lipid biosynthetic pathways. Malonyl-coenzyme A (CoA) is utilized for fatty acid biosynthesis only after its conversion to malonyl-acyl carrier protein (ACP) by malonyl-CoA transacylase, the product of the fabD gene. Two general mechanisms have been described for the biosynthesis of long-chain, monounsaturated fatty acids in living cells. One of them (found only in bacteria) is independent of oxygen and consists of a branch point in the fatty acid synthesis pathway at the level of a C-10 intermediate. In this mechanism, a β-hydroxydecanoyl dehydrase converts (stereospecifically) the C-10 hydroxy intermediate to two isomers, the -2,3 and the -3,4 unsaturated C-10 intermediates, the first of which gives rise to normal saturated products while the second gives monounsaturated fatty acids. As the growth temperature is lowered, the proportion of low-melting-point fatty acids in the membrane lipids increases. The finding that the substrates for the ∆5-desaturase are membrane lipids provides the cell with a rapid mechanism for decreasing the fluidity of preexisting membranes upon temperature decrease. A focused attack using the information of the genome sequence should yield new clues to understanding membrane biogenesis and membrane differentiation in prokaryotes.

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5

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Type II Fatty Acid Synthase
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Figures

Image of FIGURE 1
FIGURE 1

Organization of genes involved in fatty acid biosynthesis in and other low-G+C gram-positive bacteria. The deduced amino acid sequence of genes involved in fatty acid synthesis, which are organized in clusters, were compared with the Microbial Genomes BLAST Databases at the National Center for Biotechnology Information ( ). Only genes with a deduced amino acid sequence 30% identical or higher with ortholog were included. The names of various bacteria are abbreviated as indicated in Table 2 .

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Image of FIGURE 2
FIGURE 2

Partial reactions catalyzed by acetyl-CoA carboxylase. First, biotin carboxylase (BC) catalyzes the carboxy-lation of biotin covalently coupled to biotin carboxyl carrier protein (BCCP). The second step is the transfer of the CO moiety to acetyl-CoA by carboxyltransferase (CT)

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Image of FIGURE 3
FIGURE 3

Initiation of fatty acid biosynthesis. Malonyl-CoA, the product of the acetyl-CoA carboxylase (ACC) reaction, is converted to malonyl-ACP by malonyl-CoA transacylase (MTA). The following step is catalyzed by two homologs of β-ketoacyl-ACP synthase III (KAS III), FabH1 and FabH2, which are able to utilize straight- and branched-chain acyl-CoA primers as substrates.

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Image of FIGURE 4
FIGURE 4

Elongation cycle of fatty acid biosynthesis. The elongation of the growing acyl chains is accomplished by the action of four enzymes: β-ketoacyl-ACP synthase II (KAS II), which is the target of the antibiotic cerulenin; β-ketoacyl-ACP reductase (KAR); β-hydroxyacyl-ACP dehydrase (HAD); and enoyl reductase (ER).

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Image of FIGURE 5
FIGURE 5

Proposed pathway of branched-chain keto acid incorporation into fatty acids. Branched-chain amino acids are converted to branched-chain 2-keto acid by a branched-chain amino acid transaminase (BCAT). Acyl-CoA intermediaries are then synthesized by a branched-chain α-ketoacid dehydrogenase complex (BCKAD). Isovaleryl-CoA, 2-methylbutyryl-CoA, and isobutyryl-CoA are substrates of the fatty acid synthase (FAS) yielding iso-branched C and C, anteiso-branched C and C, and iso-branched C and C fatty acids, respectively. αKg, α-ketoglutarate; glu, glutamate.

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Image of FIGURE 6
FIGURE 6

Proposed pathway of phosphatide acid biosynthesis. Glycerol-3-phosphate is synthesized by the product of the A gene, glycerol-3-phosphate dehydrogenase (G3PD). Glycerol-3-phosphate acyltransferase (G3PAT) catalyzes the first acylation step, and the second acyl group is introduced by l-acylglycerol-3-phosphate acyltransferase (AG3PAT) to yield phosphatidic acid.

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Image of FIGURE 7
FIGURE 7

Complex lipid biosynthesis. The first step is the activation of phosphatide acid to CDP-diacylglycerol by CDP-diacylglycerol synthetase (CDAGS). Biosynthesis of PE is achieved by the sequential catalysis of PS synthase (PSS), followed by PS decarboxylase (PSD). PG is formed by the condensation of CDP-diacylglycerol with G3P, catalyzed by PGP synthase (PGPS), followed by removal of the phosphate by PGP phosphatase (PGPP). CL is formed by the condensation of two molecules of PG catalyzed by the CL synthase (CLS). Diacylglyceride is synthesized by dephosphorylation of phosphatidic acid by phosphatidic acid phosphatase (PAP). The diacylglyceride is then glucosylated by one or two transfers of glucose from UDP-glucose in a sequential reaction catalyzed by UDP-glucosyltransferase (UGT).

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
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Tables

Generic image for table
TABLE 1

Fatty acid composition of total membrane lipid extracts from

JH642 strain was grown at 37°C or 20°C in minimal medium supplemented with casamino acids and glucose as a carbon source. The total lipids were extracted and transesterified to yield fatty acid methylesters. Then the fatty acid methylesters were subjected to gas chromatography-mass spectrometry analysis.

nd, not detected.

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5
Generic image for table
TABLE 2

genes coding for proteins involved in lipid synthesis

Gene names are indicated as currently used. Previous names still in use in Subtilist are shown in parentheses.

Functions assigned to the genes are shown.

The names of bacteria are abbreviated as follows: Ban, ; Bst, ; Bsu, ; Cac, ; Cdi, ; Sau, ; Smu, ; Spn, ; Spy, .

Citation: de Mendoza D, Schujman G, Aguilar P. 2002. Biosynthesis and Function of Membrane Lipids, p 43-55. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch5

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