N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide (ECMDB21250) (M2MDB001658)

IdentificationTaxonomyPhysical PropertiesBiological PropertiesSpectraConcentrationsLinksReferencesEnzymes (12)Transporters (1)XML
Proteins (13)
Record Information
Version2.0
Creation Date2012-07-30 14:55:06 -0600
Update Date2015-06-03 17:21:00 -0600
Secondary Accession Numbers
  • ECMDB21250
Identification
Name:N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide
DescriptionN-acetyl-D-glucosamine(anhydrous)N-acetylmuramyl-tripeptide is an intermediate in peptidoglycan synthesis and turnover. Peptidoglycan can be described as a fisherman's net that encloses bacteria. The mesh of the net is made of two segments of parallel, somewhat inextensible glycan threads, held together by two small elastic peptide crosslinks allowing the net to expand or shrink. The glycan moiety of the peptidoglycan is very uniform among all bacteria, and is made up of alternating β-1,4-linked N-acetylglucosamine and N-acetyl muramate residues, with an average chain lengthof 10 to 65 disaccharide units (depending on the organism). The peptidoglycan synthesis pathway starts in the cytoplasm, where in six steps the peptidoglycan precursor a UDP-N-acetylmuramoyl-pentapeptide is synthesized. This precursor is then attached to the memberane acceptor all-trans-undecaprenyl phosphate, generating a N-acetylmuramoyl-pentapeptide-diphosphoundecaprenol, also known as lipid I. Another transferase then adds UDP-N-acetyl-α-D-glucosamine, yielding the complete monomeric unit a lipid II, also known as lipid II. This final lipid intermediate is transferred by an as yet unknown mechanism through the membrane. The peptidoglycan monomers are then polymerized on the outside surface by glycosyltransferases, which form the linear glycan chains, and transpeptidases, which catalyze the formation of peptide crosslinks. Peptide crosslinks form between different parts of the peptides depending on the organism. For example, in Mycobacteria and in E. coli most links form between the carboxyl group of the penultimate D-alanine (residue 4) of one peptide to the amino group at the D-center of meso-diaminopimelate (residue 3) of an adjacent peptide of a second glycan chain (as in E. coli). The crosslinking reaction is catalyzed by transpeptidases and involves the cleavage of the D-alanyl-D-alanine bond of the donor peptide, providing the energy to drive the reaction. As a result, the peptides in the peptidoglycan polymers are one or two amino acids shorter than the peptides in the monomers.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms:
ValueSource
2-Amino-6-{[4-carboxy-2-({2-[(2-{[3-({4,5-dihydroxy-3-[(1-hydroxyethylidene)amino]-6-(hydroxymethyl)oxan-2-yl}oxy)-5-[(1-hydroxyethylidene)amino]-2-(hydroxymethyl)-3,4-dihydro-2H-pyran-4-yl]oxy}-1-hydroxypropylidene)amino]-1-hydroxypropylidene}amino)-1-hydroxybutylidene]amino}heptanedioateGenerator
Chemical Formula:C34H54N6O19
Weight:Average: 850.8214
Monoisotopic: 850.344373576
InChI Key:ZWZMFRJKRXDGBE-UHFFFAOYSA-N
InChI:InChI=1S/C34H54N6O19/c1-13(29(49)39-18(8-9-23(45)46)31(51)40-19(33(54)55)7-5-6-17(35)32(52)53)36-30(50)14(2)57-27-20(37-15(3)43)12-56-22(11-42)28(27)59-34-24(38-16(4)44)26(48)25(47)21(10-41)58-34/h12-14,17-19,21-22,24-28,34,41-42,47-48H,5-11,35H2,1-4H3,(H,36,50)(H,37,43)(H,38,44)(H,39,49)(H,40,51)(H,45,46)(H,52,53)(H,54,55)
CAS number:Not Available
IUPAC Name:2-amino-6-{[4-carboxy-2-({2-[(2-{[3-({4,5-dihydroxy-3-[(1-hydroxyethylidene)amino]-6-(hydroxymethyl)oxan-2-yl}oxy)-5-[(1-hydroxyethylidene)amino]-2-(hydroxymethyl)-3,4-dihydro-2H-pyran-4-yl]oxy}-1-hydroxypropylidene)amino]-1-hydroxypropylidene}amino)-1-hydroxybutylidene]amino}heptanedioic acid
Traditional IUPAC Name:2-amino-6-{[4-carboxy-2-({2-[(2-{[3-({4,5-dihydroxy-3-[(1-hydroxyethylidene)amino]-6-(hydroxymethyl)oxan-2-yl}oxy)-5-[(1-hydroxyethylidene)amino]-2-(hydroxymethyl)-3,4-dihydro-2H-pyran-4-yl]oxy}-1-hydroxypropylidene)amino]-1-hydroxypropylidene}amino)-1-hydroxybutylidene]amino}heptanedioic acid
SMILES:CC(OC1C(OC2OC(CO)C(O)C(O)C2N=C(C)O)C(CO)OC=C1N=C(C)O)C(O)=NC(C)C(O)=NC(CCC(O)=O)C(O)=NC(CCCC(N)C(O)=O)C(O)=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as peptides. Peptides are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentPeptides
Alternative Parents
Substituents
  • Alpha peptide
  • Saccharolipid
  • N-acyl-alpha-hexosamine
  • N-acyl-alpha-amino acid
  • N-acyl-alpha amino acid or derivatives
  • Glycosyl compound
  • O-glycosyl compound
  • Alpha-amino acid
  • Alpha-amino acid or derivatives
  • Tricarboxylic acid or derivatives
  • Amino fatty acid
  • Hydroxy fatty acid
  • Oxane
  • Fatty acyl
  • Monosaccharide
  • Secondary alcohol
  • Amino acid
  • Amino acid or derivatives
  • Acetal
  • Carboximidic acid
  • Carboximidic acid derivative
  • Carboxylic acid
  • Dialkyl ether
  • Ether
  • Oxacycle
  • Organoheterocyclic compound
  • Organic 1,3-dipolar compound
  • Propargyl-type 1,3-dipolar organic compound
  • Amine
  • Organic oxygen compound
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Organopnictogen compound
  • Primary aliphatic amine
  • Organic oxide
  • Carbonyl group
  • Alcohol
  • Primary amine
  • Primary alcohol
  • Organonitrogen compound
  • Organooxygen compound
  • Aliphatic heteromonocyclic compound
Molecular FrameworkAliphatic heteromonocyclic compounds
External Descriptors
Physical Properties
State:Not Available
Charge:-1
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility0.2 g/LALOGPS
logP-1.6ALOGPS
logP-2.8ChemAxon
logS-3.6ALOGPS
pKa (Strongest Acidic)3.23ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count25ChemAxon
Hydrogen Donor Count13ChemAxon
Polar Surface Area418.71 ŲChemAxon
Rotatable Bond Count23ChemAxon
Refractivity194.05 m³·mol⁻¹ChemAxon
Polarizability82.91 ųChemAxon
Number of Rings2ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain) > N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide + N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide
two linked disacharide tripeptide murein units (uncrosslinked, middle of chain) >2 N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide
N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide + Water > L-alanine-D-glutamate-meso-2,6-diaminoheptanedioate + N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramic acid
N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide + Water > N-Acetyl-D-glucosamine + 1,6-Anhydrous-N-Acetylmuramyl-tripeptide
N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide + Water > D-Alanine + N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Pathways:Not Available
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0019-0205010390-85cd3c5657158613899aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0udr-0938145230-e508f2d59123ebfe6784View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-1915010000-8ee2356690ba5b763312View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-01qj-4101004970-f5bbca7c644c4263aed7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001r-2022053590-506c0fdb246d34764b03View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-000l-8397480000-91222a57edd94b56d00bView in MoNA
References
References:Not Available
Synthesis Reference:Not Available
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI IDNot Available
HMDB IDNot Available
Pubchem Compound ID45479614
Kegg IDNot Available
ChemSpider IDNot Available
Wikipedia IDNot Available
BioCyc IDCPD0-2155
EcoCyc IDCPD0-2155

Enzymes

Protein Details
1. N-acetylmuramoyl-L-alanine amidase AmiB
General function:
Involved in N-acetylmuramoyl-L-alanine amidase activity
Specific function:
Cell-wall hydrolase probably involved in cell-wall hydrolysis, septation or recycling
Gene Name:
amiB
Uniprot ID:
P26365
Molecular weight:
47985
Reactions
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Protein Details
2. Probable N-acetylmuramoyl-L-alanine amidase AmiA
General function:
Involved in N-acetylmuramoyl-L-alanine amidase activity
Specific function:
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Gene Name:
amiA
Uniprot ID:
P36548
Molecular weight:
31412
Reactions
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Protein Details
3. N-acetylmuramoyl-L-alanine amidase AmiC
General function:
Involved in N-acetylmuramoyl-L-alanine amidase activity
Specific function:
Cell-wall hydrolase probably involved in cell-wall hydrolysis, septation or recycling
Gene Name:
amiC
Uniprot ID:
P63883
Molecular weight:
45634
Reactions
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Protein Details
4. Beta-hexosaminidase
General function:
Involved in beta-N-acetylhexosaminidase activity
Specific function:
Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides
Gene Name:
nagZ
Uniprot ID:
P75949
Molecular weight:
37594
Reactions
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Protein Details
5. Murein tetrapeptide carboxypeptidase
General function:
Defense mechanisms
Specific function:
Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso- Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc- anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross- linked muropeptides. The tripeptides produced by the lcdA reaction can then be reused as peptidoglycan building blocks; lcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase
Gene Name:
ldcA
Uniprot ID:
P76008
Molecular weight:
33567
Reactions
GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + H(2)O = GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + D-alanine.
Protein Details
6. Soluble lytic murein transglycosylase
General function:
Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific function:
Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N- acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division
Gene Name:
slt
Uniprot ID:
P0AGC3
Molecular weight:
73353
Reactions
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Protein Details
7. Endo-type membrane-bound lytic murein transglycosylase A
General function:
Involved in lytic endotransglycosylase activity
Specific function:
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain. Prefers cross-linked murein in vivo
Gene Name:
emtA
Uniprot ID:
P0C960
Molecular weight:
22226
Reactions
Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Protein Details
8. Membrane-bound lytic murein transglycosylase C
General function:
Involved in hydrolase activity, acting on glycosyl bonds
Specific function:
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division
Gene Name:
mltC
Uniprot ID:
P0C066
Molecular weight:
40112
Reactions
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Protein Details
9. Membrane-bound lytic murein transglycosylase F
General function:
Involved in carbon-oxygen lyase activity, acting on polysaccharides
Specific function:
Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella
Gene Name:
mltF
Uniprot ID:
P0AGC5
Molecular weight:
58302
Reactions
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Protein Details
10. Membrane-bound lytic murein transglycosylase B
General function:
Cell wall/membrane/envelope biogenesis
Specific function:
Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N- acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division
Gene Name:
mltB
Uniprot ID:
P41052
Molecular weight:
40256
Reactions
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Protein Details
11. 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
General function:
Involved in N-acetylmuramoyl-L-alanine amidase activity
Specific function:
Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha- amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety
Gene Name:
ampD
Uniprot ID:
P13016
Molecular weight:
20536
Reactions
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Protein Details
12. Membrane-bound lytic murein transglycosylase A
General function:
Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific function:
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi
Gene Name:
mltA
Uniprot ID:
P0A935
Molecular weight:
40410
Reactions
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.

Transporters

Protein Details
1. Protein AmpG
General function:
Involved in transmembrane transport
Specific function:
Probably acts as a permease in the beta-lactamase induction system and in peptidoglycan recycling
Gene Name:
ampG
Uniprot ID:
P0AE16
Molecular weight:
53245