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Chapter 18 : Biosynthesis of the Aspartate Family of Amino Acids

Author: Henry Paulus1
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Affiliations: 1: Department of Metabolic Regulation, Boston Biomédical Research Institute, Boston, Massachusetts 02114, and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115
Content Type: Monograph
Publication Year: 1993

Category: Bacterial Pathogenesis; Microbial Genetics and Molecular Biology

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Abstract:

Diaminopimelate, lysine, methionine, and threonine derive most of their carbon atoms from L-aspartate, and these amino acids are therefore often referred to as the aspartate family. Their biosynthesis is effected by a complex pathway involving common intermediates from which multiple branches lead to the end products. The so-called aspartate pathway has several features that distinguish it from other pathways of amino acid biosynthesis and lend its study particular interest in the contexts of bacterial physiology and biochemical evolution. A number of different mechanisms for the control of the aspartate pathway that has evolved in the eubacteria and even within the genus Bacillus is discussed in this chapter. The primary focus of this chapter is on and closely related species. The aspartate pathway splits after the synthesis of aspartate semialdehyde, one branch leading to biosynthesis of diaminopimelate and lysine and the other leading to biosynthesis of threonine and methionine. The branch point enzyme homoserine dehydrogenase is the counterpart of dihydrodipicolinate synthase in controlling the utilization of aspartate semialdehyde for the biosynthesis of threonine and methionine by catalyzing the NADPH-dependent reduction of L-aspartate semialdehyde to L-homoserine. The major route for the biosynthesis of aspartate from glycolytic intermediates involves the carboxylation of pyruvate to oxaloacetate and subsequent transamination.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18

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Biosynthesis of the Aspartate Family of Amino Acids
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Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
/content/10.1128/9781555818388.chap18.fig18-1
Figure 1

Overview of the pathway for biosynthesis of the aspartate family of amino acids. S-adenosyl-methionine.

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Figure 1

Overview of the pathway for biosynthesis of the aspartate family of amino acids. S-adenosyl-methionine.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 5

The branch of the aspartate pathway leading to biosynthesis of diaminopimelate and lysine. The reaction catalyzed by diaminopimelate dehydrogenase, indicated by the dotted arrows, occurs in a few species and in coryneform bacteria but not in Ac-SCoA, acetyl-CoA; CoASH, coenzyme A; Ac, acetyl.

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Figure 5

The branch of the aspartate pathway leading to biosynthesis of diaminopimelate and lysine. The reaction catalyzed by diaminopimelate dehydrogenase, indicated by the dotted arrows, occurs in a few species and in coryneform bacteria but not in Ac-SCoA, acetyl-CoA; CoASH, coenzyme A; Ac, acetyl.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 6

The branch of the aspartate pathway leading to biosynthesis of threonine and methionine. The reaction catalyzed by O-acetylhomoserine sulfhydrylase, indicated by dotted arrows, occurs in coryneform bacteria. CoASH, coenzyme A; Ac-SCoA, acetyl-CoA; Ac, aceryl; THF, tetrahydrofolate.

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Figure 6

The branch of the aspartate pathway leading to biosynthesis of threonine and methionine. The reaction catalyzed by O-acetylhomoserine sulfhydrylase, indicated by dotted arrows, occurs in coryneform bacteria. CoASH, coenzyme A; Ac-SCoA, acetyl-CoA; Ac, aceryl; THF, tetrahydrofolate.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 2

Common reactions in the biosynthesis of diaminopimelate, lysine, threonine, and methionine.

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Figure 2

Common reactions in the biosynthesis of diaminopimelate, lysine, threonine, and methionine.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 3

Postulated folding domains of aspartokinases. (A) Proposed biglobular structure of the subunit of aspartokinase II (left) and arrangements of the and subunits in the native enzyme (right). (B) Proposed triglobular structure of a subunit of aspartokinase-homoserine dehydrogenase I (left) and arrangements of subunits in the native tetrameric enzyme (right) (modified from reference ). AK, aspartokinase domain; HSD, homoserine dehydrogenase domain; I, interdomain.

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Figure 3

Postulated folding domains of aspartokinases. (A) Proposed biglobular structure of the subunit of aspartokinase II (left) and arrangements of the and subunits in the native enzyme (right). (B) Proposed triglobular structure of a subunit of aspartokinase-homoserine dehydrogenase I (left) and arrangements of subunits in the native tetrameric enzyme (right) (modified from reference ). AK, aspartokinase domain; HSD, homoserine dehydrogenase domain; I, interdomain.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 4

Sequence homology of aspartokinase II and the aspartokinases. A and B are the sites at which trypsin cleaves aspartokinase II and aspartokinase-homoserine dehydrogenase I, respectively. AK, aspartokinase; HSD, homoserine dehydrogenase.

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Image of Figure 4
Figure 4

Sequence homology of aspartokinase II and the aspartokinases. A and B are the sites at which trypsin cleaves aspartokinase II and aspartokinase-homoserine dehydrogenase I, respectively. AK, aspartokinase; HSD, homoserine dehydrogenase.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 7

Physical map of the chromosome near the locus at 144°. The diagram shows positions of various restriction endonuclease cleavage sites and locations of deduced coding regions. Dotted arrows indicate polarities of transcription.

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Image of Figure 7
Figure 7

Physical map of the chromosome near the locus at 144°. The diagram shows positions of various restriction endonuclease cleavage sites and locations of deduced coding regions. Dotted arrows indicate polarities of transcription.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 8

Possible secondary structures of RNA transcribed from the intercistronic region of ( ). Stabilization free energies were estimated by using the parameters of Freier et al. ( ). RBS, ribosome-binding site; Fmet, formylmethionyl.

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Image of Figure 8
Figure 8

Possible secondary structures of RNA transcribed from the intercistronic region of ( ). Stabilization free energies were estimated by using the parameters of Freier et al. ( ). RBS, ribosome-binding site; Fmet, formylmethionyl.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 9

Diagram of the operon and adjacent regions (modified from reference ). The diagram shows positions of various restriction endonuclease cleavage sites and locations of deduced coding regions. Arrows indicate the polarities of transcription. P, promoter; SD, ribosome-binding site; T, transcription terminator; ORF, open reading frame.

10.1128/9781555818388/fig18-9_thmb.gif
10.1128/9781555818388/fig18-9.gif
Image of Figure 9
Figure 9

Diagram of the operon and adjacent regions (modified from reference ). The diagram shows positions of various restriction endonuclease cleavage sites and locations of deduced coding regions. Arrows indicate the polarities of transcription. P, promoter; SD, ribosome-binding site; T, transcription terminator; ORF, open reading frame.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 10

Nucleotide sequence of the untranslated leader region of the operon ( ). The sequence from 168 is shown in its entirety. Sequences from strains VB217, FB59, and KA120 ( ) and from A34, ATR1, ATR4, AT9, AT10, TSH9, TSH25, TSH112, and TSHL2 ( ) are shown only where they differ from that of strain 168. The sequence is annotated to show elements of potential regulatory significance, with inverted repeats indicated by arrows and ribosome-binding sites (R.B.S.) indicated by asterisks. Nucleotide residues are numbered from the transcription start site.

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Figure 10

Nucleotide sequence of the untranslated leader region of the operon ( ). The sequence from 168 is shown in its entirety. Sequences from strains VB217, FB59, and KA120 ( ) and from A34, ATR1, ATR4, AT9, AT10, TSH9, TSH25, TSH112, and TSHL2 ( ) are shown only where they differ from that of strain 168. The sequence is annotated to show elements of potential regulatory significance, with inverted repeats indicated by arrows and ribosome-binding sites (R.B.S.) indicated by asterisks. Nucleotide residues are numbered from the transcription start site.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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Figure 11

Biosynthesis of l-aspartate. Ac-SCoA, acetyl-CoA.

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Image of Figure 11
Figure 11

Biosynthesis of l-aspartate. Ac-SCoA, acetyl-CoA.

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
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References

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Tables

Biosynthesis of the Aspartate Family of Amino Acids
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Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
/content/10.1128/9781555818388.chap18.tab18-1
Table 1

Aspartokinase isozymes of

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10.1128/9781555818388/tab18-1.gif
Generic image for table
Table 1

Aspartokinase isozymes of

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
/content/10.1128/9781555818388.chap18.tab18-2
Table 2

Enzymes of the diaminopimelate-lysine pathway

10.1128/9781555818388/tab18-2_thmb.gif
10.1128/9781555818388/tab18-2.gif
Generic image for table
Table 2

Enzymes of the diaminopimelate-lysine pathway

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18
/content/10.1128/9781555818388.chap18.tab18-3
Table 3

Enzymes of the threonine-methionme pathway

10.1128/9781555818388/tab18-3_thmb.gif
10.1128/9781555818388/tab18-3.gif
Generic image for table
Table 3

Enzymes of the threonine-methionme pathway

Citation: Paulus H. 1993. Biosynthesis of the Aspartate Family of Amino Acids, p 237-267. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch18

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