Highlighted Text:
Show |
Hide
Full text loading...
Chapter 12 : Peptidoglycan Synthesis Inhibitors
Authors:
A. Bryskier,
C. Dini
Content Type: Reference
Publication Year:
2005
Category: Bacterial Pathogenesis
Book DOI:
10.1128/9781555815929
Chapter DOI:
10.1128/9781555815929.ch12
MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
Preview this chapter:
Peptidoglycan Synthesis Inhibitors, Page 1 of 2
< Previous page | Next page > /docserver/preview/fulltext/10.1128/9781555815929/9781555812379_Chap12-1.gif /docserver/preview/fulltext/10.1128/9781555815929/9781555812379_Chap12-2.gif
Abstract:
Bacterial peptidoglycans were first identified in the 1940s. The nucleotide precursors were isolated and characterized in 1949. Peptidoglycan biosynthesis has been investigated in many bacterial species. The glycan chains of peptidoglycan are small and repeated units composed of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc). The glmM gene was shown to be essential in Escherichia coli, but genetic data recently suggested that in Staphylococcus aureus there could be an alternative pathway for glucosamine-1-phosphate biosynthesis. The GlmU protein from E. coli is a bifunctional enzyme. Its C-terminal domain catalyzes acetylation of glucosamine-1-phosphate into GlcNAc-1-phosphate, whereas its N-terminal domain catalyzes uridylation to yield UDP-GlcNAc. Nucleoside antibiotics can be subdivided into different classes according to their chemical structures and/or their respective modes of action against MraY: the tunicamycin group, the ribosamino-uridine group, and finally the capuramycin group. Some of them possess activities against gram-positive bacteria, against Mycobacterium spp., and against Pseudomonas spp. This toxicity is explained by their high inhibitory activity upon glycoconjugate biosyntheses, such as of techoic acids, glycosaminoglycans, and glycoproteins. The major component, caprazamycin B, exhibits anti-M. tuberculosis activity and excellent activity against M. avium complex. The major chemical difference observed between liposidomycins and FR-900493 resides in the presence of an N-functionalized amino acid residue in the FR-900493 structure, instead of the diazepanone ring of liposidomycins. Lantibiotics such as mersacidin, are gene-encoded peptides that contain unusual thioether amino acids and/or 3-methyllanthionine.
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
Figures
Peptidoglycan Synthesis Inhibitors
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555815929.ch12-1,webId=/content/author/10.1128/9781555815929.ch12-1,properties={foaf_givenname=A., foaf_name=A. Bryskier, foaf_surname=Bryskier}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555815929.ch12-2,webId=/content/author/10.1128/9781555815929.ch12-2,properties={foaf_givenname=C., foaf_name=C. Dini, foaf_surname=Dini}]]
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig1
Figure 1
UDP-GlcNAc biosynthesis
10.1128/9781555815929/f0377-01_thmb.gif
10.1128/9781555815929/f0377-01.gif
Figure 1
UDP-GlcNAc biosynthesis
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig2
Figure 2
Lipopolysaccharide (LPS) or UDP-MurNac biosynthesis
10.1128/9781555815929/f0378-01_thmb.gif
10.1128/9781555815929/f0378-01.gif
Figure 2
Lipopolysaccharide (LPS) or UDP-MurNac biosynthesis
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig3
Figure 3
Pentapeptide biosynthesis
10.1128/9781555815929/f0378-02_thmb.gif
10.1128/9781555815929/f0378-02.gif
Figure 3
Pentapeptide biosynthesis
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig4
Figure 4
Mechanism of reaction catalyzed by ATP-dependent amide-forming enzymes (MurC to MurF)
10.1128/9781555815929/f0379-01_thmb.gif
10.1128/9781555815929/f0379-01.gif
Figure 4
Mechanism of reaction catalyzed by ATP-dependent amide-forming enzymes (MurC to MurF)
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig5
Figure 5
Lipid II biosynthesis
10.1128/9781555815929/f0380-01_thmb.gif
10.1128/9781555815929/f0380-01.gif
Figure 5
Lipid II biosynthesis
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig6
Figure 6
Peptide cross-linking
10.1128/9781555815929/f0381-01_thmb.gif
10.1128/9781555815929/f0381-01.gif
Figure 6
Peptide cross-linking
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig7
Figure 7
Transglycosylation
10.1128/9781555815929/f0382-01_thmb.gif
10.1128/9781555815929/f0382-01.gif
Figure 7
Transglycosylation
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig8
Figure 8
MurA inhibitors
10.1128/9781555815929/f0382-02_thmb.gif
10.1128/9781555815929/f0382-02.gif
Figure 8
MurA inhibitors
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig9
Figure 9
MurB inhibitors
10.1128/9781555815929/f0383-01_thmb.gif
10.1128/9781555815929/f0383-01.gif
Figure 9
MurB inhibitors
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig10
Figure 10
Phosphinate inhibitors of MurC
10.1128/9781555815929/f0384-01_thmb.gif
10.1128/9781555815929/f0384-01.gif
Figure 10
Phosphinate inhibitors of MurC
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig11
Figure 11
Phosphinate inhibitors of MurD
10.1128/9781555815929/f0384-02_thmb.gif
10.1128/9781555815929/f0384-02.gif
Figure 11
Phosphinate inhibitors of MurD
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig12
Figure 12
Macrocyclic derivatives
10.1128/9781555815929/f0385-01_thmb.gif
10.1128/9781555815929/f0385-01.gif
Figure 12
Macrocyclic derivatives
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig13
Figure 13
Phosphinate inhibitors of MurE
10.1128/9781555815929/f0385-02_thmb.gif
10.1128/9781555815929/f0385-02.gif
Figure 13
Phosphinate inhibitors of MurE
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig14
Figure 14
MurF inhibitors (
Gu et al., 2004
)
10.1128/9781555815929/f0385-03_thmb.gif
10.1128/9781555815929/f0385-03.gif
Figure 14
MurF inhibitors ( Gu et al., 2004 )
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig15
Figure 15
Classification of MraY inhibitors
10.1128/9781555815929/f0386-01_thmb.gif
10.1128/9781555815929/f0386-01.gif
Figure 15
Classification of MraY inhibitors
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig16
Figure 16
MraY enzymatic reaction
10.1128/9781555815929/f0386-02_thmb.gif
10.1128/9781555815929/f0386-02.gif
Figure 16
MraY enzymatic reaction
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig17
Figure 17
Nucleoside antibiotics that are non-MraY inhibitors
10.1128/9781555815929/f0386-03_thmb.gif
10.1128/9781555815929/f0386-03.gif
Figure 17
Nucleoside antibiotics that are non-MraY inhibitors
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab1
Table 1
Tunicamycins, streptovirudins, and corynetoxins
10.1128/9781555815929/f0387-01_thmb.gif
10.1128/9781555815929/f0387-01.gif
Table 1
Tunicamycins, streptovirudins, and corynetoxins
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig18
Figure 18
Ribosaminouridine is the minimal structural requirement in this class to inhibit MraY
10.1128/9781555815929/f0388-01_thmb.gif
10.1128/9781555815929/f0388-01.gif
Figure 18
Ribosaminouridine is the minimal structural requirement in this class to inhibit MraY
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab2
Table 2
Liposidomycin classification
10.1128/9781555815929/f0388-02_thmb.gif
10.1128/9781555815929/f0388-02.gif
Table 2
Liposidomycin classification
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab3
Table 3
Caprazamycin chemical structure
10.1128/9781555815929/f0389-01_thmb.gif
10.1128/9781555815929/f0389-01.gif
Table 3
Caprazamycin chemical structure
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig19
Figure 19
FR-900493 and compound 77 described in a Fujisawa patent
10.1128/9781555815929/f0389-03_thmb.gif
10.1128/9781555815929/f0389-03.gif
Figure 19
FR-900493 and compound 77 described in a Fujisawa patent
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig20
Figure 20
Muraymycins
10.1128/9781555815929/f0389-02_thmb.gif
10.1128/9781555815929/f0389-02.gif
Figure 20
Muraymycins
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig21
Figure 21
Ribosamino-uridine is the template of the riburamycin series
10.1128/9781555815929/f0390-01_thmb.gif
10.1128/9781555815929/f0390-01.gif
Figure 21
Ribosamino-uridine is the template of the riburamycin series
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig22
Figure 22
Riburamycins
10.1128/9781555815929/f0390-02_thmb.gif
10.1128/9781555815929/f0390-02.gif
Figure 22
Riburamycins
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig23
Figure 23
Uridylpeptide antibiotic template
10.1128/9781555815929/f0391-02_thmb.gif
10.1128/9781555815929/f0391-02.gif
Figure 23
Uridylpeptide antibiotic template
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab5
Table 5
Mureidomycin, pacidamycin, and napsamycin chemical structures
10.1128/9781555815929/f0391-01_thmb.gif
10.1128/9781555815929/f0391-01.gif
Table 5
Mureidomycin, pacidamycin, and napsamycin chemical structures
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig24
Figure 24
Dihydropacidamycin D isomers are reduction products of pacidamycin D
10.1128/9781555815929/f0392-01_thmb.gif
10.1128/9781555815929/f0392-01.gif
Figure 24
Dihydropacidamycin D isomers are reduction products of pacidamycin D
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig25
Figure 25
Capuramycin template
10.1128/9781555815929/f0392-02_thmb.gif
10.1128/9781555815929/f0392-02.gif
Figure 25
Capuramycin template
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig26
Figure 26
Amphomycin
10.1128/9781555815929/f0393-03_thmb.gif
10.1128/9781555815929/f0393-03.gif
Figure 26
Amphomycin
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig27
Figure 27
HMR 1043 (friulimicin)
10.1128/9781555815929/f0394-01_thmb.gif
10.1128/9781555815929/f0394-01.gif
Figure 27
HMR 1043 (friulimicin)
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig28
Figure 28
MurG enzymatic reaction
10.1128/9781555815929/f0394-02_thmb.gif
10.1128/9781555815929/f0394-02.gif
Figure 28
MurG enzymatic reaction
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig29
Figure 29
Ramoplanin
10.1128/9781555815929/f0395-01_thmb.gif
10.1128/9781555815929/f0395-01.gif
Figure 29
Ramoplanin
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig30
Figure 30
Mode of action of bacitracin
10.1128/9781555815929/f0395-02_thmb.gif
10.1128/9781555815929/f0395-02.gif
Figure 30
Mode of action of bacitracin
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig31
Figure 31
Moenomycin A
10.1128/9781555815929/f0396-01_thmb.gif
10.1128/9781555815929/f0396-01.gif
Figure 31
Moenomycin A
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12fig32
Figure 32
Chlorobiphenyl vancomycin
10.1128/9781555815929/f0397-01_thmb.gif
10.1128/9781555815929/f0397-01.gif
Figure 32
Chlorobiphenyl vancomycin
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
References
/content/book/10.1128/9781555815929.ch12
1.
Abo-Ghalia M,, Flegel M,, Blanot D,, Van Heijenoort J, 1988, Synthesis of inhibitors of the meso-diaminopimelate-adding enzyme from Escherichia coli, Int J Pept Protein Res, 32, 208– 222.
2.
Anderson MS,, Eveland SS,, Onishi HR,, Pompliano DL, 1996, Kinetic mechanism of the Escherichia coli UDPMurNAc-tripeptide d-alanyl- d-alanine-adding enzyme, use of a glutathione S-transferase fusion, Biochemistry, 35, 16264– 16269.
3.
Arthur M,, Reynolds P,, Courvalin P, 1996, Glycopeptide resistance in enterococci, Trends Microbiol, 4, 401– 407.
4.
Auger G,, van Heijenoort J, et al, 1995, J Prakt Chem, 337, 351.
5.
Bearne SL, 1996, Active site-directed inactivation of Escherichia coli glucosamine-6-phosphate synthase, determination of the fructose 6-phosphate binding constant using a carbohydrate-based inactivator, J Biol Chem, 271, 3052– 3057.
6.
Bearne SL,, Blouin C, 2000, Inhibition of Escherichia coli glucosamine-6-phosphate synthase by reactive intermediate analogues, the role of the 2-amino function in catalysis, J Biol Chem, 275, 135– 140.
7.
Bemer P,, Juvin M-E,, Bryskier A,, Drugeon H, 2003, In vitro activities of a new lipopeptide, HMR 1043, against susceptible and resistant gram-positive isolates, Antimicrob Agents Chemother, 47, 3025– 3029.
8.
Benson TE,, Harris MS,, Choi GH,, Cialdella JI,, Herberg JT,, Martin JP Jr,, Baldwin ET, 2001, A structural variation for MurB, X-ray crystal structure of Staphylococcus aureus UDP-Nacetylenolpyruvylglucosamine reductase (MurB), Biochemistry, 40, 2340– 2350.
9.
Bertrand JA,, Auger G,, Fanchon E,, Martin L,, Blanot D,, van Heijenoort J,, Dideberg O, 1997, Crystal structure of UDP-Nacetylmuramoyl- l-alanine d-glutamate ligase from Escherichia coli, EMBO J, 16, 3416– 3125.
10.
Bertrand JA,, Auger G,, Martin L,, Fanchon E,, Blanot D,, Le Beller D, van Heijenoort J,, Dideberg O, 1999, Determination of the MurD mechanism through crystallographic analysis of enzyme complexes, J Mol Biol, 289, 579– 590.
11.
Bertrand JA,, Fanchon E,, Martin L,, Chantalat L,, Auger G,, Blanot D,, van Heijenoort J,, Dideberg O, 2000, Open structures of MurD, domain movements and structural similarities with folylpolyglutamate synthetase, J Mol Biol, 301, 1257– 1266.
12.
Billot-Klein D,, Gutmann L,, Sable S,, Guittet E,, van Heijenoort J, 1994, Modification of peptidoglycan precursors is a common feature of the low-level vancomycin-resistant VANB-type Enterococcus D366 and of the naturally glycopeptide-resistant species Lactobacillus casei, Pediococcus pentosaceus, Leuconostoc mesenteroides, and Enterococcus gallinarum, J Bacteriol, 176, 2398– 2405.
13.
Biton J,, Braham K, et al, 2002, Synthesis and in vitro evaluation of riburamycin (Ru75411), activity against MraY, antibacterial profile, and mechanism of action (MOA) on whole cells, 42nd Intersci Conf Antimicrob Agents Chemother.
14.
Boojamra CG,, Lemoine RC, et al, 2001, Stereochemical elucidation and total synthesis of dihydropacidamycin D, a semisynthetic pacidamycin, J Am Chem Soc, 123, 870– 874.
15.
Brandish PE,, Burnham MK, et al, 1996, Slow binding inhibition of phospho-N-acetylmuramyl-pentapeptide-translocase (Escherichia coli) by mureidomycin A, J Biol Chem, 271, 760.
16.
Brandish PE,, Kimura K, et al, 1996, Modes of action of tunicamycin, liposidomycin B, and mureidomycin A, inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli, Antimicrob Agents Chemother, 40, 1640– 1644.
17.
Brown ED,, Marquardt JL,, Lee JP,, Walsh CT,, Anderson KS, 1994, Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ, Biochemistry, 33, 10638– 10645.
18.
Brown ED,, Vivas EI,, Walsh CT,, Kolter R, 1995, MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli, J Bacteriol, 177, 4194– 4197.
19.
Bugg TD,, Wright GD,, Dutka-Malen S, Arthur M, Courvalin P,, Walsh CT, 1991, Molecular basis for vancomycin resistance in Enterococcus faecium BM4147, biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA, Biochemistry, 30, 10408– 10415.
20.
Chatterjee S,, Chatterjee DK, et al, 1992, Mersacidin, a new antibiotic from Bacillus, in vitro and in vivo antibacterial activity, J Antibiotics, 45, 839– 845.
21.
Chatterjee S,, Nadkarni SR, et al, 1994, Napsamycins, new Pseudomonas active antibiotics of the mureidomycin family from Streptomyces sp HIL Y-82, 11372, J Antibiot, 47, 595– 598.
22.
Chen L,, Walker D, et al, 2003, Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate, Proc Natl Acad Sci USA, 100, 5658– 5663.
23.
Chen RH,, Buko AM, et al, 1989, Pacidamycins, a novel series of antibiotics with anti-Pseudomonas aeruginosa activity. II. Isolation and structural elucidation, J Antibiot, 42, 512– 20.
24.
Crouvoisier M,, Mengin-Lecreulx D, et al, 1999, UDP-N-acetylglucosamine, N-acetylmuramoyl-(pentapeptide) pyrophosphoryl undecaprenol N-acetylglucosamine transferase from Escherichia coli, overproduction, solubilization, and purification, FEBS Lett, 449, 289– 292.
25.
Cudic P,, Kranz JK, et al, 2002, Complexation of peptidoglycan intermediates by the lipoglycodepsipeptide antibiotic ramoplanin, minimal structural requirements for intermolecular complexation and fibril formation, Proc Natl Acad Sci USA, 99, 7384– 7389.
26.
Dini C,, Collette P, et al, 2000, Synthesis of the nucleoside moiety of liposidomycins, elucidation of the pharmacophore of this family of MraY inhibitors, Bioorg Med Chem Lett, 10, 1839– 1843.
27.
Dini C,, Drochon N, et al, 2001a, Synthesis of analogues of the O-beta-d-ribofuranosyl nucleoside moiety of liposidomycins. Part 1. Contribution of the amino group and the uracil moiety upon the inhibition of MraY, Bioorg Med Chem Lett, 11, 529– 531.
28.
Dini C,, Drochon N, et al, 2001b, Synthesis of analogues of the O-beta-d-ribofuranosyl nucleoside moiety of liposidomycins. Part 2. Role of the hydroxyl groups upon the inhibition of MraY, Bioorg Med Chem Lett, 11, 533– 536.
29.
Dini C,, Didier-Laurent S, et al, 2002, Synthesis of sub-micromolar inhibitors of MraY by exploring the region originally occupied by the diazepanone ring in the liposidomycin structure, Bioorg Med Chem Lett, 12, 1209– 1213.
30.
Du W,, Brown JR,, Sylvester DR,, Huang J,, Chalker AF,, So CY,, Holmes DJ,, Payne DJ,, Wallis NG, 2000, Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria, J Bacteriol, 182, 4146– 4152.
31.
Duncan K,, van Heijenoort J,, Walsh CT, 1990, Purification and characterization of the d-alanyl- d-alanine-adding enzyme from Escherichia coli, Biochemistry, 29, 2379– 2386.
32.
Eckardt K,, Wetzstein H, et al, 1980, Streptovirudin and tunicamycin, two inhibitors of glycolipid synthesis, differentiation by use of gel chromatography, HPLC and hydrolysis, J Antibiot (Tokyo), 33, 908– 910.
33.
Edgar JA,, Frahn JL, et al, 1982, Corynetoxins, causative agents of annual ryegrass toxicity; their identification as tunicamycin group antibiotics, J Chem Soc, 4, 222– 224.
34.
El-Abadla N,, Lampilas M, et al, 1999, Moenomycin A, the role of the methyl group in the moenuronamide unit and a general discussion of structure-activity relationships, Tetrahedron, 55, 699– 722.
35.
Emanuele JJ Jr,, Jin H,, Jacobson BL,, Chang CY,, Einspahr HM,, Villafranca JJ, 1996, Kinetic and crystallographic studies of Escherichia coli UDP-N-acetylmuramate, l-alanine ligase, Protein Sci, 5, 2566– 2574.
36.
Fernandes PB,, Swanson RN, et al, 1989, Pacidamycins, a novel series of antibiotics with anti-Pseudomonas aeruginosa activity. III. Microbiologic profile, J Antibiot, 42, 521– 526.
37.
Ge M,, Chen Z,, Onishi HR,, Kohler J,, Silver LL,, Kerns R,, Fukuzawa S,, Thompson C,, Kahne D, 1999, Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding d-Ala- d-Ala, Science, 284, 442– 443.
38.
Gegnas LD,, Waddell ST,, Chabin RM,, Reddy S,, Wong KK, 1998, Inhibitors of the bacterial cell wall biosynthesis enzyme MurD, Bioorg Med Chem Lett, 8, 1643– 1648.
39.
Gehring AM,, Lees WJ,, Mindiola DJ,, Walsh CT,, Brown ED, 1996, Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli, Biochemistry, 35, 579– 585.
40.
Glanzmann P,, Gustafson J,, Komatsuzawa H,, Ohta K,, BergerBachi B, 1999, glmM operon and methicillin-resistant glmM suppressor mutants in Staphylococcus aureus, Antimicrob Agents Chemother, 43, 240– 245.
41.
Gobec S,, Urleb U,, Auger G,, Blanot D, 2001, Synthesis and biochemical evaluation of some novel N-acyl phosphono- and phosphinoalanine derivatives as potential inhibitors of the d-glutamic acid-adding enzyme, Pharmazie, 56, 295– 257.
42.
Goldman RC,, Baizman ER, et al, 2000, Differential antibacterial activity of moenomycin analogues on gram-positive bacteria, Bioorg Med Chem Lett, 10, 2251– 2254.
43.
Goldman RC,, Gange D, 2000, Inhibition of transglycosylation involved in bacterial peptidoglycan synthesis, Curr Med Chem, 7, 801– 820.
44.
Gordon E,, Flouret B,, Chantalat L,, van Heijenoort J, MenginLecreulx D,, Dideberg O, 2001, Crystal structure of UDP-N-acetylmuramoyl- l-alanyl- d-glutamate, meso-diaminopimelate ligase from Escherichia coli, J Biol Chem, 276, 10999– 11006.
45.
Gu YG,, Florjancic AS, et al, 2004, Structure-activity realationship of novel potent MurF inhibitors, Bioorg Med Chem Lett, 14, 267– 270.
46.
Gubler M,, Appoldt Y,, Keck W, 1996, Overexpression, purification, and characterization of UDP-N-acetylmuramyl, l-alanine ligase from Escherichia coli, J Bacteriol, 178, 906– 910.
47.
Hammes W,, Schleifer KH,, Kandler O, 1973, Mode of action of glycine on the biosynthesis of peptidoglycan, J Bacteriol, 116, 1029– 1053.
48.
Horton JR,, Bostock JM, et al, 2003, Macrocyclic inhibitors of the bacterial cell wall biosynthesis enzyme MurD, Bioorg Med Chem Lett, 13, 1557– 1560.
49.
Hotoda H,, Daigo M, et al, 2003, Synthesis and antimycobacterial activity of capuramycin analogues. Part 2. Acylated derivatives of capuramycin-related compounds, Bioorg Med Chem Lett, 13, 2833– 2836.
50.
Hotoda H,, Miyuki F, et al, 2003, Synthesis and antimycobacterial activity of capuramycin analogues. Part 1. Substitution of the azepan-2-one moiety of capuramycin, Bioorg Med Chem Lett, 13, 2829– 2832.
51.
Igarashi M,, Nakagawa S, et al, 2002, 42nd Intersci Conf Antimicrob Agents Chemother, abstract F-2031, p 232.
52.
Inukai M,, Isono F, et al, 1989, Mureidomycins A-D, novel peptidyl nucleoside antibiotics with spheroplast forming activity. I. Taxonomy, fermentation, isolation and physicochemical properties, J Antibiot, 42, 662– 666.
53.
Inukai M,, Isono F, et al, 1993, Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins, Antimicrob Agents Chemother, 37, 980– 983.
54.
Ishiguro EE, 1982, Inhibition of uridine 5’-diphosphate-N-acetylmuramyl- l-alanine synthetase by beta-chloro- l-alanine in Escherichia coli, Can J Microbiol, 28, 654– 659.
55.
Isono K,, Uramoto M, et al, 1985, Liposidomycins, novel nucleo-side antibiotics which inhibit bacterial peptidoglycan synthesis, J Antibiot, 38, 1617– 1621.
56.
Isono F,, Katayama T, et al, 1989, Mureidomycins A-D, novel peptidylnucleoside antibiotics with spheroplast forming activity. III. Biological properties, J Antibiot, 42, 674– 679.
57.
Isupov MN,, Obmolova G,, Butterworth S,, Badet-Denisot MA, Badet B, Polikarpov I, Littlechild JA,, Teplyakov A, 1996, Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases, evidence from the 18 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase, Structure, 4, 801– 810.
58.
Jolly L,, Ferrari P,, Blanot D,, Van Heijenoort J, Fassy F,, MenginLecreulx D, 1999, Reaction mechanism of phosphoglucosamine mutase from Escherichia coli, Eur J Biochem, 262, 202– 210.
59.
Kahan FM,, Kahan JS,, Cassidy PJ,, Kropp H, 1974, The mechanism of action of fosfomycin (phosphonomycin), Ann NY Acad Sci, 235, 364– 386.
60.
Karwowski JP,, Jackson M,, Theriault RJ,, Chen RH,, Barlow GJ,, Maus ML, 1989, Pacidamycins, a novel series of antibiotics with anti-Pseudomonas aeruginosa activity. I. Taxonomy of the producing organism and fermentation, J Antibiot 42, 506– 511.
61.
Kimura K,, Ikeda Y, et al, 1998, Selective inhibition of the bacterial peptidoglycan biosynthesis by the new types of liposidomycins, J Antibiot, 51, 1099– 1104.
62.
Kimura K,, Bugg TDH, 2003, Recent advances in antimicrobial nucleoside antibiotics targetting cell wall biosynthesis, Nat Prod Rep, 20, 252– 273.
63.
Kostrewa D,, D’Arcy A,, Takacs B,, Kamber M, 2001, Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 233 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 196 A resolution, J Mol Biol, 305, 279– 289.
64.
Le Roux P,, Auger G, et al, 1992, Synthesis of new peptide inhibitors of the meso-diaminopimelate-adding enzyme, Eur J Med Chem, 27, 899– 907.
65.
Lee VJ,, Hecker SJ, 1999, Antibiotic resistance versus small molecules, the chemical evolution, Med Res Rev, 19, 521– 542.
66.
Leriche C,, Badet-Denisot MA,, Badet B, 1997, Affinity labeling of Escherichia coli glucosamine-6-phosphate synthase with a fructose 6-phosphate analog—evidence for proximity between the N-terminal cysteine and the fructose-6-phosphate-binding site, Eur J Biochem, 245, 418– 422.
67.
Liger D,, Blanot D,, van Heijenoort J, 1991, Effect of various ala-nine analogues on the l-alanine-adding enzyme from Escherichia coli, FEMS Microbiol Lett, 64, 111– 115.
68.
Liger D,, Masson A,, Blanot D,, van Heijenoort J,, Parquet C, 1995, Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate, l-alanine ligase from Escherichia coli, Eur J Biochem, 230, 80– 87.
69.
Liger D,, Masson A,, Blanot D,, van Heijenoort J,, Parquet C, 1996, Study of the overproduced uridine-diphosphate-N-acetylmuramate, l-alanine ligase from Escherichia colim Microb Drug Resist, 2, 25– 27.
70.
Marquardt JL,, Siegele DA,, Kolter R,, Walsh CT, 1992, Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase, J Bacteriol, 174, 5748– 5752.
71.
McDonald LA,, Barbieri LR,, Carter GT,, Lenoy E,, Lotvin J,, Petersen PJ,, Siegel MM,, Singh G,, Williamson RT, 2002, Structures of the muraymycins, novel peptidoglycan biosynthesis inhibitors, J Am Chem Soc, 124, 10260– 10261.
72.
Mengin-Lecreulx D,, van Heijenoort J, 1994, Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli, characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-Nacetylglucosamine synthesis, J Bacteriol, 176, 5788– 5795.
73.
Mengin-Lecreulx D,, van Heijenoort J,, Park JT, 1996, Identification of the mpl gene encoding UDP-N-acetylmuramate, l-alanyl-gamma- d-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan, J Bacteriol, 178, 5347– 5352.
74.
Mengin-Lecreulx D,, Falla T,, Blanot D,, van Heijenoort J,, Adams DJ,, Chopra I, 1999, Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- l-alanyl- d-glutamate, l-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth, J Bacteriol, 181, 5909– 5914.
75.
Michaud C,, Blanot D,, Flouret B,, Van Heijenoort J, 1987, Partial purification and specificity studies of the d-glutamate-adding and d-alanyl- d-alanine-adding enzymes from Escherichia coli K12, Eur J Biochem, 166, 631– 637.
76.
Michaud C,, Parquet C,, Flouret B,, Blanot D,, van Heijenoort J, 1990, Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli, Biochem J, 269, 277– 278.
77.
Miller DJ,, Hammond SM,, Anderluzzi D,, Bugg TDH, 1998, Aminoalkylphosphinate inhibitors of d-Ala- d-Ala adding enzyme, J Chem Soc Perkin Trans, 1, 131– 142.
78.
Mizuno Y,, Yaegashi M,, Ito E, 1973, Purification and properties of uridine diphosphate N-acetylmuramate, l-alanine ligase, J Biochem (Tokyo), 74, 525– 538.
79.
Neuhaus FC,, Struve WG, 1965, Enzymatic synthesis of analogs of the cell-wall precursor - I - kinetics and specificity of uridine diphospho-N-acetylmuramyl- l-alanyl- d-glutamyl- l-lysine, d-alanyl-Dalanine ligase (adenosine diphosphate) from Streptococcus faecalis R, Biochemistry, 10, 120– 131.
80.
Ochi K,, Ezaki M, et al, 1989, Antibiotic FR-900493 manufacture with Bacillus EP-333177, Fujisawa Pharmaceutical Co, Ltd, Japan.
81.
Pompeo F,, Bourne Y,, van Heijenoort J, Fassy F,, Mengin-Lecreulx D, 2001, Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth, J Biol Chem, 276, 3833– 3839.
82.
Pratviel-Sosa F,, Acher F,, Trigalo F,, Blanot D,, Azerad R,, van Heijenoort J, 1994, Effect of various analogues of d-glutamic acid on the d-glutamate-adding enzyme from Escherichia coli, FEMS Microbiol Lett, 115, 223– 228.
83.
Reynolds PE,, Snaith HA,, Maguire AJ,, Dutka-Malen S,, Courvalin P, 1994, Analysis of peptidoglycan precursors in vancomycin-resistant Enterococcus gallinarum BM4174, Biochem J, 301, 5– 8.
84.
Ritzeler O,, Hennig L, et al, 1997, Synthesis of a trisaccharide analogue of moenomycin A-12, implications of new moenomycin structure-activity relationships, Tetrahedron, 53, 1675– 1694.
85.
Schleifer KH,, Hammes WP,, Kandler O, 1976, Effect of endogenous and exogenous factors on the primary structures of bacterial peptidoglycan, Adv Microb Physiol, 13, 245– 292.
86.
Schonbrunn E,, Eschenburg S,, Krekel F,, Luger K,, Amrhein N, 2000, Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA, Biochemistry, 39, 2164– 2173.
87.
Schwartz R,, Datema R, 1980, Inhibitors of protein glycosylation, Trends Biochem Sci, 65– 67.
88.
Skarzynski T,, Mistry A,, Wonacott A,, Hutchinson SE,, Kelly VA,, Duncan K, 1996, Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin, Structure, 4, 1465– 1474.
89.
Somner EA,, Reynolds PE, 1990, Inhibition of peptidoglycan biosynthesis by ramoplanin, Antimicrob Agents Chemother, 34, 423– 429.
90.
Takatsuki A,, Tamura G, 1971, Tunicamycin, a new antibiotic. III. Reversal of the antiviral activity of tunicamycin by aminosugars and their derivatives, J Antibiot (Tokyo), 24, 232– 238.
91.
Takeuchi T,, Igarashi M, et al, 1999, Antibiotic caprazamycins and process for producing the same, WO 2001012643-A1, Zaidan Hojin Biseibutsu Kagaku Kenkyu Kai, Japan.
92.
Takeuchi T,, Igarashi M, et al, 2001, Caprazamycin manufacture with Streptomyces for control of acid-fast bacteria, JP 2003012687, Meiji Seika Kaisha, Ltd, Japan.
93.
Tanner ME,, Vaganay S,, van Heijenoort J,, Blanot D, 1996, Phosphinate inhibitors of the d-glutamic acid-adding enzyme of peptidoglycan biosynthesis, J Org Chem, 61, 1756– 1760.
94.
Teplyakov A,, Obmolova G,, Badet-Denisot MA, Badet B,, Polikarpov I, 1998, Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase, evidence from a 16 A crystal structure of the isomerase domain, Structure, 6, 1047– 1055.
95.
Vogel P,, Petterson DS, et al, 1981, Isolation of a group of glycolipid toxins from seedheads of annual ryegrass (Lolium rigidum Gaud) infected by Corynebacterium rathayi, Aust J Exp Biol Med Sci, 59, 455– 467.
96.
Walker B,, Brown MF,, Lynas JF,, Martin SL,, McDowell A,, Badet B,, Hill AJ, 2000, Inhibition of Escherichia coli glucosamine synthetase by novel electrophilic analogues of glutamine—comparison with 6-diazo-5-oxo-norleucine, Bioorg Med Chem Lett, 10, 2795– 2798.
97.
Wu HC,, Wu TC, 1971, Isolation and characterization of a glucosamine-requiring mutant of Escherichia coli K-12 defective in glucosamine-6-phosphate synthetase, J Bacteriol, 105, 455– 466.
98.
Yamaguchi H,, Sato S, et al, 1986, Capuramycin, a new nucleoside antibiotic: taxonomy, fermentation, isolation and characterization, J Antibiotics, 39, 1047– 1053.
99.
Yan Y,, Munshi S,, Li Y,, Pryor KA,, Marsilio F,, Leiting B, 1999, Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide d-alanyl- d-alanine-adding enzyme (MurF), Acta Crystallogr D Biol Crystallogr, 55 (Pt 12), 2033– 2034.
100.
Yan Y,, Munshi S,, Leiting B,, Anderson MS,, Chrzas J,, Chen Z, 2000, Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl- d-alanine-adding enzyme (MurF) at 23 A resolution, J Mol Biol, 304, 435– 445.
101.
Yoshida Y,, Yamanaka H, et al, 1993, Preparation of uronic acid (FR-900493) derivatives as antibacterial agents, JP05078385, Fujisawa, Pharma.
102.
Zeng B,, Wong KK,, Pompliano DL,, Reddy S,, Tanner ME, 1998, A phosphinate inhibitor of the meso-diaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis, J Org Chem, 63, 10081– 10085.
Tables
Peptidoglycan Synthesis Inhibitors
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555815929.ch12-1,webId=/content/author/10.1128/9781555815929.ch12-1,properties={foaf_givenname=A., foaf_name=A. Bryskier, foaf_surname=Bryskier}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555815929.ch12-2,webId=/content/author/10.1128/9781555815929.ch12-2,properties={foaf_givenname=C., foaf_name=C. Dini, foaf_surname=Dini}]]
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab4
Table 4
Riburamycin activity against gram-positive bacteria, including multiresistant strains
Table 4
Riburamycin activity against gram-positive bacteria, including multiresistant strains
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab6
Table 6
Inhibitory activity of capuramycin and closely related compounds against MraY
Table 6
Inhibitory activity of capuramycin and closely related compounds against MraY
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab7
Table 7
Evaluation of capuramycin and related compounds against MraY and M. smegmatis
Table 7
Evaluation of capuramycin and related compounds against MraY and M. smegmatis
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab8
Table 8
Evaluation of capuramycin and related compounds against M. avium, M. intracellulare, and M. kansasii and comparison with rifampin and isoniazid
Table 8
Evaluation of capuramycin and related compounds against M. avium, M. intracellulare, and M. kansasii and comparison with rifampin and isoniazid
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12
/content/10.1128/9781555815929.ch12.ch12tab9
Table 9
In vitro activity of HMR 1043
Table 9
In vitro activity of HMR 1043
Citation:
Bryskier A, Dini C.
2005.
Peptidoglycan Synthesis Inhibitors,
p 377-400.
In
Bryskier, M.D. A (ed),
Antimicrobial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555815929.ch12