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Article: The alternative to penicillins.

Höltje, J V

2001 Volume 7, Issue 10, Page(s) 1100–1101

MeSH term(s)	Bacterial Proteins ; Carbohydrate Sequence ; Carrier Proteins/metabolism ; Cell Wall ; Hexosyltransferases ; Methicillin Resistance ; Molecular Sequence Data ; Muramoylpentapeptide Carboxypeptidase/metabolism ; Penicillin-Binding Proteins ; Penicillins/metabolism ; Penicillins/pharmacology ; Peptidoglycan/metabolism ; Peptidyl Transferases ; Staphylococcus aureus/drug effects ; Staphylococcus aureus/enzymology
Chemical Substances	Bacterial Proteins ; Carrier Proteins ; Penicillin-Binding Proteins ; Penicillins ; Peptidoglycan ; Peptidyl Transferases (EC 2.3.2.12) ; Hexosyltransferases (EC 2.4.1.-) ; Muramoylpentapeptide Carboxypeptidase (EC 3.4.17.8)
Language	English
Publishing date	2001-10
Publishing country	United States
Document type	News
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/nm1001-1100
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Zs.A 4212: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 39: Show issues

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Article: Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli.

Höltje, J V

Microbiology and molecular biology reviews : MMBR

1998 Volume 62, Issue 1, Page(s) 181–203

Abstract: To withstand the high intracellular pressure, the cell wall of most bacteria is stabilized by a unique cross-linked biopolymer called murein or peptidoglycan. It is made of glycan strands [poly-(GlcNAc-MurNAc)], which are linked by short peptides to form ...

Abstract	To withstand the high intracellular pressure, the cell wall of most bacteria is stabilized by a unique cross-linked biopolymer called murein or peptidoglycan. It is made of glycan strands [poly-(GlcNAc-MurNAc)], which are linked by short peptides to form a covalently closed net. Completely surrounding the cell, the murein represents a kind of bacterial exoskeleton known as the murein sacculus. Not only does the sacculus endow bacteria with mechanical stability, but in addition it maintains the specific shape of the cell. Enlargement and division of the murein sacculus is a prerequisite for growth of the bacterium. Two groups of enzymes, hydrolases and synthases, have to cooperate to allow the insertion of new subunits into the murein net. The action of these enzymes must be well coordinated to guarantee growth of the stress-bearing sacculus without risking bacteriolysis. Protein-protein interaction studies suggest that this is accomplished by the formation of a multienzyme complex, a murein-synthesizing machinery combining murein hydrolases and synthases. Enlargement of both the multilayered murein of gram-positive and the thin, single-layered murein of gram-negative bacteria seems to follow an inside-to-outside growth strategy. New material is hooked in a relaxed state underneath the stress-bearing sacculus before it becomes inserted upon cleavage of covalent bonds in the layer(s) under tension. A model is presented that postulates that maintenance of bacterial shape is achieved by the enzyme complex copying the preexisting murein sacculus that plays the role of a template.
MeSH term(s)	Carbohydrate Sequence ; Cell Division ; Cell Wall ; Escherichia coli/cytology ; Escherichia coli/ultrastructure ; Models, Chemical ; Molecular Sequence Data ; Peptidoglycan
Chemical Substances	Peptidoglycan
Language	English
Publishing date	1998-03
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1376131-6
ISSN	1098-5557 ; 1070-6275 ; 1092-2172
ISSN (online)	1098-5557 ; 1070-6275
ISSN	1092-2172
DOI	10.1128/MMBR.62.1.181-203.1998
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Ud II Zs.96: Show issues

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Article: A hypothetical holoenzyme involved in the replication of the murein sacculus of Escherichia coli.

Höltje, J V

Microbiology (Reading, England)

1996 Volume 142 Pt 8, Page(s) 1911–1918

MeSH term(s)	Amino Acid Sequence ; Base Sequence ; Cell Cycle ; Escherichia coli/enzymology ; Escherichia coli/growth & development ; Escherichia coli/immunology ; Models, Structural ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; Peptidoglycan/biosynthesis ; Peptidoglycan/chemistry
Chemical Substances	Multienzyme Complexes ; Peptidoglycan
Language	English
Publishing date	1996-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/13500872-142-8-1911
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Ud II Zs.140: Show issues

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Article: Bacterial lysozymes.

Höltje, J V

EXS

1996 Volume 75, Page(s) 65–74

Abstract: Lysozymes are found in many bacteria that are surrounded by a murein-(peptidoglycan) containing cell wall. Their physiological function for the bacteria is still a matter of debate. On the one hand they can autolyse the cell, on the other hand they may ... ...

Abstract	Lysozymes are found in many bacteria that are surrounded by a murein-(peptidoglycan) containing cell wall. Their physiological function for the bacteria is still a matter of debate. On the one hand they can autolyse the cell, on the other hand they may have an essential role during enlargement and division of the cell wall by the controlled splitting of bonds in the murein sacculus. Both beta-1.4-N,6-O-diacetylmuramidase and beta-1.4-N-acetylmuramidases have been described in bacteria. In some cases a modular design of the enzyme has been demonstrated with a catalytic domain and a substrate (murein)-binding and recognition domain consisting of repeated motifs.
MeSH term(s)	Bacteria/enzymology ; Bacteriolysis ; Carbohydrate Sequence ; Escherichia coli/chemistry ; Molecular Sequence Data ; Muramic Acids/chemistry ; Muramic Acids/metabolism ; Muramidase/chemistry ; Muramidase/metabolism ; Peptidoglycan/chemistry ; Peptidoglycan/metabolism ; Polysaccharides, Bacterial/chemistry ; Polysaccharides, Bacterial/metabolism ; Substrate Specificity
Chemical Substances	Muramic Acids ; Peptidoglycan ; Polysaccharides, Bacterial ; Muramidase (EC 3.2.1.17)
Language	English
Publishing date	1996
Publishing country	Switzerland
Document type	Journal Article ; Review
ISSN	1023-294X
ISSN	1023-294X
DOI	10.1007/978-3-0348-9225-4_4
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Article: Lysozyme substrates.

Höltje, J V

EXS

1996 Volume 75, Page(s) 105–110

Abstract: The natural substrate of lysozyme is the rigid layer of bacterial cell walls, the murein (peptidoglycan), which is a gigantic polymer of (GlcNAc-MurNAc)n polysaccharide strands crosslinked through short peptide bridges at the lactyl groups of the muramic ...

Abstract	The natural substrate of lysozyme is the rigid layer of bacterial cell walls, the murein (peptidoglycan), which is a gigantic polymer of (GlcNAc-MurNAc)n polysaccharide strands crosslinked through short peptide bridges at the lactyl groups of the muramic acid residues. Thus, lysozyme lyses bacteria by degrading their protective exoskeleton, the murein sacculus. The high molecular weight murein is thereby hydrolysed to low molecular weight muropeptides, a process that can be followed quantitatively by different methods. However, due to the insolubility of the murein sacculus, the enzyme kinetics are rather complex. Therefore, a variety of different low molecular weight substrates have been prepared, both murein degradation products and synthetic compounds. These substrates allow a better characterization of the binding and catalytic mechanism of lysozyme. In addition, they are used in various photometric, isotopic and immunological lysozyme assays.
MeSH term(s)	Carbohydrate Sequence ; Cell Wall/chemistry ; Kinetics ; Molecular Sequence Data ; Muramic Acids/chemistry ; Muramic Acids/metabolism ; Muramidase/metabolism ; Nephelometry and Turbidimetry ; Oligosaccharides/chemistry ; Oligosaccharides/metabolism ; Peptidoglycan/metabolism ; Polysaccharides, Bacterial/metabolism ; Substrate Specificity
Chemical Substances	Muramic Acids ; Oligosaccharides ; Peptidoglycan ; Polysaccharides, Bacterial ; Muramidase (EC 3.2.1.17)
Language	English
Publishing date	1996
Publishing country	Switzerland
Document type	Journal Article ; Review
ISSN	1023-294X
ISSN	1023-294X
DOI	10.1007/978-3-0348-9225-4_7
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Article: Lytic transglycosylases.

Höltje, J V

EXS

1996 Volume 75, Page(s) 425–429

Abstract: Although cleaving the same glycosidic bond between MurNAc and GlcNAc in murein, lytic transglycosylases differ from lysozymes by catalyzing an intramolecular transglycosylation of the glycosyl-bond onto the C6 hydroxyl group of the muramic acid residue ... ...

Abstract	Although cleaving the same glycosidic bond between MurNAc and GlcNAc in murein, lytic transglycosylases differ from lysozymes by catalyzing an intramolecular transglycosylation of the glycosyl-bond onto the C6 hydroxyl group of the muramic acid residue yielding 1.6-anhydromuramic acid-carrying products. The three dimensional structure of the soluble lytic transglycosylase Slt70 of E. coli revealed a doughnut-like shape that would allow the protein to encircle the polysaccharide strands of the murein. Despite the absence of significant sequence homology, the catalytic center shows structural similarity to lysozymes, although the catalytic aspartate is missing. All lytic transglycosylases which have been characterized up until now turned out to be processive exo-glycosylases.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Carbohydrate Sequence ; Escherichia coli/enzymology ; Escherichia coli Proteins ; Genes, Bacterial ; Glycoside Hydrolases ; Glycosylation ; Glycosyltransferases/chemistry ; Glycosyltransferases/genetics ; Glycosyltransferases/metabolism ; Models, Molecular ; Molecular Sequence Data ; Muramic Acids/metabolism ; Peptidoglycan/metabolism ; Protein Structure, Tertiary
Chemical Substances	Bacterial Proteins ; Escherichia coli Proteins ; Muramic Acids ; Peptidoglycan ; N-acetylmuramic acid (246FXU111L) ; 1,6-anhydromuramic acid (82080-93-1) ; Glycosyltransferases (EC 2.4.-) ; Glycoside Hydrolases (EC 3.2.1.-) ; slt protein, E coli (EC 3.2.1.-)
Language	English
Publishing date	1996
Publishing country	Switzerland
Document type	Journal Article ; Review
ISSN	1023-294X
ISSN	1023-294X
DOI	10.1007/978-3-0348-9225-4_21
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Article: Molecular interplay of murein synthases and murein hydrolases in Escherichia coli.

Höltje, J V

Microbial drug resistance (Larchmont, N.Y.)

1996 Volume 2, Issue 1, Page(s) 99–103

Abstract: Affinity chromatography using different lytic transglycosylases as a specific ligand revealed an interaction of both murein hydrolases and murein synthases. This interaction is taken as evidence for the assemblage into a multienzyme complex that could ... ...

Abstract	Affinity chromatography using different lytic transglycosylases as a specific ligand revealed an interaction of both murein hydrolases and murein synthases. This interaction is taken as evidence for the assemblage into a multienzyme complex that could function as a murein replicase precisely copying the given three-dimensional structure of the murein sacculus. The sacculus of the mother cell would function as a template, which is identically replicated by copying the lengths of the existing glycan strands and the pattern of crosslinkages. A hypothetical enzyme complex specifically involved in cell division and a complex specifically involved in cell elongation are presented. It is postulated that PBPs 1a and/or 1b are present in both complexes, whereas the presence of PBP2 or PBP3 defines the specificity of the murein-synthesizing machinery as being involved in either cell elongation or septation. Moreover, the proposed "holoenzyme" suprastructure could explain why the specific inhibition of PBPs 1a/1b results in bacteriolysis and why inhibition of PBP2 and PBP3 causes the well-known morphological alterations, spherical growth, and filamentation, respectively.
MeSH term(s)	Escherichia coli/enzymology ; Escherichia coli/ultrastructure ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; Penicillins/pharmacology ; Peptide Synthases/metabolism ; Peptidoglycan/biosynthesis ; Peptidoglycan/metabolism
Chemical Substances	Penicillins ; Peptidoglycan ; N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28) ; Peptide Synthases (EC 6.3.2.-) ; murein synthetase (EC 6.3.2.-)
Language	English
Publishing date	1996
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1290490-9
ISSN	1931-8448 ; 1076-6294
ISSN (online)	1931-8448
ISSN	1076-6294
DOI	10.1089/mdr.1996.2.99
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Zs.A 4435: Show issues

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Article: From growth to autolysis: the murein hydrolases in Escherichia coli.

Höltje, J V

Archives of microbiology

1995 Volume 164, Issue 4, Page(s) 243–254

Abstract: Murein hydrolases cleave bonds in the bacterial exoskeleton, the murein (peptidoglycan) sacculus, a covalently closed bag-shaped polymer made of glycan strands that are crosslinked by peptides. During growth and division of a bacterial cell, these ... ...

Abstract	Murein hydrolases cleave bonds in the bacterial exoskeleton, the murein (peptidoglycan) sacculus, a covalently closed bag-shaped polymer made of glycan strands that are crosslinked by peptides. During growth and division of a bacterial cell, these enzymes are involved in the controlled metabolism of the murein sacculus. Murein hydrolases are believed to function as pacemaker enzymes for the enlargement of the murein sacculus since opening of bonds in the murein net is needed to allow the insertion of new subunits into the sacculus. Furthermore, they are responsible for splitting the septum during cell division. The murein turnover products that are released during growth are further degraded by these (1 --> 6)-anhydromuramic acid derivatives by an intramolecular transglycosylation reaction.
MeSH term(s)	Bacteriolysis/physiology ; Carbohydrate Sequence ; Escherichia coli/enzymology ; Escherichia coli/growth & development ; Molecular Sequence Data ; N-Acetylmuramoyl-L-alanine Amidase/metabolism
Chemical Substances	N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28)
Language	English
Publishing date	1995-10
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	124824-8
ISSN	1432-072X ; 0302-8933
ISSN (online)	1432-072X
ISSN	0302-8933
DOI	10.1007/bf02529958
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Zs.A 805: Show issues

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Article: Morphogenesis of Escherichia coli.

Vollmer, W / Höltje, J V

Current opinion in microbiology

2001 Volume 4, Issue 6, Page(s) 625–633

Abstract: Morphogenesis of the rod-shaped Escherichia coli is determined by controlled growth of an exoskeleton made of murein (peptidoglycan). Recent insights in the growth strategy of the stress-bearing murein sacculus has contributed to our understanding of how ...

Abstract	Morphogenesis of the rod-shaped Escherichia coli is determined by controlled growth of an exoskeleton made of murein (peptidoglycan). Recent insights in the growth strategy of the stress-bearing murein sacculus has contributed to our understanding of how the required concerted action of murein polymerizing and hydrolyzing enzymes is achieved. The proteins involved are coordinated by the formation of multienzyme complexes. In this review, we summarize the recent results on murein structure and metabolism. On the basis of these findings, we present a model that explains maintenance of the specific rod shape of E. coli.
MeSH term(s)	Cell Division ; Escherichia coli/cytology ; Escherichia coli/enzymology ; Escherichia coli/growth & development ; Morphogenesis ; Peptidoglycan/metabolism
Chemical Substances	Peptidoglycan
Language	English
Publishing date	2001-11-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1418474-6
ISSN	1879-0364 ; 1369-5274
ISSN (online)	1879-0364
ISSN	1369-5274
DOI	10.1016/s1369-5274(01)00261-2
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Zs.A 5514: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 51: Show issues

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Article: Enzymology of elongation and constriction of the murein sacculus of Escherichia coli.

Höltje, J V / Heidrich, C

Biochimie

2001 Volume 83, Issue 1, Page(s) 103–108

Abstract: Multiple deletions in murein hydrolases revealed that predominantly amidases are responsible for cleavage of the septum during cell division. Endopeptidases and lytic transglycosylases seem also be involved. In the absence of these enzymes E. coli grows ... ...

Abstract	Multiple deletions in murein hydrolases revealed that predominantly amidases are responsible for cleavage of the septum during cell division. Endopeptidases and lytic transglycosylases seem also be involved. In the absence of these enzymes E. coli grows normally but forms chains of adhering cells. Surprisingly, mutants lacking up to eight different murein hydrolases still grow with almost unaffected growth rate. Therefore it is speculated that general enlargement of the murein sacculus may differ from cell division by using transferases rather than the two sets of hydrolytic and synthetic enzymes as seems to be the case for the constriction process. A model is presented that describes growth of the murein of both Gram-positive and -negative bacteria by the activity of murein transferases. It is speculated that enzymes exist that catalyze a transpeptidation of the pre-existing murein onto murein precursors or nascent murein by using the chemical energy present in peptide cross-bridges. Such enzymes would at the same time cleave bonds in the murein net and insert new material into the growing sacculus.
MeSH term(s)	Cell Wall/metabolism ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli/physiology ; Escherichia coli/ultrastructure ; Gram-Positive Bacteria/enzymology ; Gram-Positive Bacteria/metabolism ; Models, Biological ; Multienzyme Complexes/metabolism ; N-Acetylmuramoyl-L-alanine Amidase/genetics ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; Peptide Synthases/metabolism ; Peptidoglycan/genetics ; Peptidoglycan/metabolism ; Transferases/metabolism
Chemical Substances	Multienzyme Complexes ; Peptidoglycan ; Transferases (EC 2.-) ; N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28) ; Peptide Synthases (EC 6.3.2.-) ; murein synthetase (EC 6.3.2.-)
Language	English
Publishing date	2001-01
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	120345-9
ISSN	0300-9084
ISSN	0300-9084
DOI	10.1016/s0300-9084(00)01226-8
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