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EC Tree
IUBMB Comments Involved in the synthesis of a cell-wall peptide in bacteria. This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase) adds 2,6-diaminopimelate instead.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
udp-n-acetylmuramoyl-l-alanyl-d-glutamate:l-lysine ligase, udp-n-acetylmuramoyl-l-alanyl-d-glutamyl-l-lysine synthetase, udp-n-acetylmuramoyl-l-alanyl-d-glutamate:meso-2,6-diaminopimelate ligase, udp-n-acetylmuramoyl-l-alanyl-d-glutamate l-lysine ligase,
more
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Synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-lysine ligase
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: L-lysine ligase
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine ligase
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase
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uridine 5'-diphospho-N-acetylmuramoyl L-alanyl-D-glutamate:lysine ligase
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Uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine synthetase
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MurE
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ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
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carboxamide formation
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carboxylic acid amide formation
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine gamma-ligase (ADP-forming)
Involved in the synthesis of a cell-wall peptide in bacteria. This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase) adds 2,6-diaminopimelate instead.
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
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one step in the biosynthesis of bacterial cell walls
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
additional information
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
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ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
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ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
the enzyme of the Gram-positive bacterium discriminates between L-lysine and D,L-diaminopimelic acid, the predominant amino acid that replaces L-lysine in Gram-negative peptidoglycan. Despite the absolute specificity for L-lysine, Staphylococcus aureus MurE binds this substrate relatively poorly. In vivo analysis and metabolomic data reveal that this is compensated for by high cytoplasmic L-lysine concentrations
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ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
despite the absolute specificity for L-lysine, Staphylococcus aureus MurE binds this substrate relatively poorly. In vivo analysis and metabolomic data reveal that this is compensated for by high cytoplasmic L-lysine concentrations, substrate discrimination mechanism, overview. Glu460 is crucial for interaction with the epsilon-amino group of the L-lysine substrate
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additional information
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enzyme is specific for L-lysine and does not accept meso-diaminopimelic acid as substrate. The inverse and strict substrate specificities of the two MurE orthologues are responsible for the presence of exclusively mesodiaminopimelic acid and L-lysine at the third position of the peptide in the peptidoglycans of Escherichia coli and Staphylococcus aureus, respectively
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additional information
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the third amino acid added to the peptide stem of peptidoglycan is usually either meso-diaminopimelic acid (in most Gram-negative bacteria), EC 6.3.2.13, or L-lysine (in most Gram-positive bacteria), EC 6.3.2.7
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additional information
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the third amino acid added to the peptide stem of peptidoglycan is usually either meso-diaminopimelic acid (in most Gram-negative bacteria), EC 6.3.2.13, or L-lysine (in most Gram-positive bacteria), EC 6.3.2.7, although in some cases other amino acids are found at this position
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ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
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one step in the biosynthesis of bacterial cell walls
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ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
additional information
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ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
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ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
the enzyme of the Gram-positive bacterium discriminates between L-lysine and D,L-diaminopimelic acid, the predominant amino acid that replaces L-lysine in Gram-negative peptidoglycan. Despite the absolute specificity for L-lysine, Staphylococcus aureus MurE binds this substrate relatively poorly. In vivo analysis and metabolomic data reveal that this is compensated for by high cytoplasmic L-lysine concentrations
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additional information
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the third amino acid added to the peptide stem of peptidoglycan is usually either meso-diaminopimelic acid (in most Gram-negative bacteria), EC 6.3.2.13, or L-lysine (in most Gram-positive bacteria), EC 6.3.2.7
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additional information
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the third amino acid added to the peptide stem of peptidoglycan is usually either meso-diaminopimelic acid (in most Gram-negative bacteria), EC 6.3.2.13, or L-lysine (in most Gram-positive bacteria), EC 6.3.2.7, although in some cases other amino acids are found at this position
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ATP
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Cl-
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activation by different anions in decreasing order: HPO42-, Cl-, SO42- , potassium salts give higher activity than the corresponding sodium salts
HPO42-
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activation by different anions in decreasing order: HPO42-, Cl-, SO42- , potassium salts give higher activity than the corresponding sodium salts
Mn2+
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Mn2+ or Mg2+ required, optimal concentration: 2 mM
phosphate
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the presence of phosphate changes the enzyme conformation to a catalytically more active form
SO42-
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activation by different anions in decreasing order: HPO42-, Cl-, SO42- , potassium salts give higher activity than the corresponding sodium salts
Mg2+
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required
Mg2+
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optimal concentration: 10 mM
Mg2+
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Mg2+ or Mn2+ required
Mg2+
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optimal concentration: 30 mM
Mg2+
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required, optimal concentration 15 mM
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(2R)-2-amino-6-([[(3R)-3-carboxy-3-([N-[6-(phosphonooxy)hexanoyl]-L-alanyl]amino)propyl](hydroxy)phosphoryl]methyl)heptanedioic acid
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(2R)-2-amino-6-([[(3R)-3-carboxy-3-[[N-(6-[[[[[[(2R,5S)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methoxy](hydroxy)phosphoryl]oxy](hydroxy)phosphoryl]oxy]hexanoyl)-L-alanyl]amino]propyl](hydroxy)phosphoryl]methyl)heptanedioic acid
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(6S,9R,14S)-benzyl 9-benzyloxycarbonyl-14-(4-benzyloxycarbonylaminobutyl)-2,2,6-trimethyl-4,7-dioxo-3-oxa-5,8,13-triazapentadecan-15-oate
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(R)-2-[bis(tert-butoxycarbonyl)amino]-5-oxopentanoate
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(R)-benzyl 2-[(tert-butoxycarbonyl)amino]-5-[methoxy(methyl)amino]-5-oxopentanoate
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(R)-benzyl 2-[bis(tert-butoxycarbonyl)amino]-5-[methoxy(methyl)amino]-5-oxopentanoate
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(S)-1-(2-tert-butoxycarbonylaminopropanoyl)piperidine-4-carboxylic acid
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(S)-6-amino-2-((R)-4-amino-4-carboxybutylamino)hexanoic acid
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(S)-6-amino-2-(piperidine-4-carboxamido)hexanoic acid
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(S)-6-amino-2-([[1-((S)-2-aminopropanoyl)piperidin-4-yl]methyl]amino)hexanoic acid
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(S)-6-amino-2-[(piperidin-4-ylmethyl)amino]hexanoic acid
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(S)-6-amino-2-[1-((S)-2-aminopropanoyl)piperidine-4-carboxamido]hexanoic acid 2,2,2-trifluoroacetate
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(S)-6-amino-2-[1-(carboxymethyl)piperidine-4-carboxamido]hexanoic acid
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(S)-6-amino-2-[[(R)-4-((S)-2-aminopropanamido)-4-carboxybutyl]amino]hexanoic acid
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(S)-benzyl 1-(2-tert-butoxycarbonylaminopropanoyl)piperidine-4-carboxylate
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(S)-benzyl 2-([(R)-5-(benzyloxy)-4-[bis(tert-butoxycarbonyl)amino]-5-oxopentyl]amino)-6-benzyloxycarbonylaminohexanoate
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(S)-benzyl 6-benzyloxycarbonylamino-2-[([1-[(S)-2-(tert-butoxycarbonylamino)propanoyl]piperidin-4-yl]methyl)amino]hexanoate
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(S)-benzyl 6-benzyloxycarbonylamino-2-[1-((S)-2-tertbutoxycarbonylaminopropanoyl)piperidine-4-carboxamido]hexanoate
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(S)-benzyl 6-benzyloxycarbonylamino-2-[1-(2-tertbutoxy-2-oxoethyl)piperidine-4-carboxamido]hexanoate
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(S)-N-(2-amino-4,5,6,7-tetrahydrobenzo[d]thiazol-6-yl)piperidine-4-carboxamide
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(S)-tert-butyl 4-[(1-benzyloxy-6-benzyloxycarbonylamino-1-oxohexan-2-yl)carbamoyl]piperidine-1-carboxylate
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(S)-tert-butyl 4-[[(1-benzyloxy-6-benzyloxycarbonylamino-1-oxohexan-2-yl)amino]methyl]piperidine-1-carboxylate
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1-(2-tert-butoxy-2-oxoethyl)piperidine-4-carboxylic acid
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2-([hydroxy[1-([N-[(4-nitrobenzyl)sulfonyl]-D-alanyl]amino)ethyl]phosphoryl]methyl)pentanedioic acid
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1 mM, 13% residual activity
2-[[(1-[[(2E)-3-(1,3-benzodioxol-5-yl)prop-2-enoyl]amino]ethyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
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1 mM, 52% residual activity
2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
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1 mM, 35% residual activity
2-[[hydroxy(1-[[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]amino]ethyl)phosphoryl]methyl]pentanedioic acid
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1 mM, 21% residual activity
2-[[hydroxy(1-[[(2E)-3-phenylprop-2-enoyl]amino]ethyl)phosphoryl]methyl]pentanedioic acid
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1 mM, 50% residual activity
2-[[hydroxy(1-[[(3-nitrobenzyl)sulfonyl]amino]ethyl)phosphoryl]methyl]pentanedioic acid
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1 mM, 52% residual activity
2-[[hydroxy(1-[[(3-nitrophenyl)sulfonyl]amino]ethyl)phosphoryl]methyl]pentanedioic acid
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1 mM, 39% residual activity
2-[[hydroxy(1-[[(4-nitrobenzyl)sulfonyl]amino]ethyl)phosphoryl]methyl]pentanedioic acid
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1 mM, 44% residual activity
2-[[hydroxy(2-methyl-1-[[(3-nitrobenzyl)sulfonyl]-amino]butyl)phosphoryl]methyl]pentanedioic acid
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1 mM, 71% residual activity
2-[[hydroxy(2-methyl-1-[[(4-nitrobenzyl)sulfonyl]-amino]butyl)phosphoryl]methyl] pentanedioic acid
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1 mM, 54% residual activity
2-[[hydroxy(2-methyl-1-[[(4-nitrobenzyl)sulfonyl]amino]propyl)phosphoryl]methyl] pentanedioic acid
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1 mM, 29% residual activity
2-[[[1-[(1,3-benzodioxol-5-ylacetyl)amino]ethyl](hydroxy)phosphoryl]methyl]pentanedioic acid
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1 mM, 12% residual activity; 1 mM, 42% residual activity; 1 mM, 60% residual activity
3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]propanoic acid
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1 mM, 50% residual activity
3-[hydroxy[1-([N-[(4-nitrobenzyl)sulfonyl]-D-alanyl]amino)ethyl]phosphoryl]propanoic acid
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1 mM, 46% residual activity
3-[[1-[(1,3-benzodioxol-5-ylacetyl)amino]ethyl](hydroxy)phosphoryl]propanoic acid
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1 mM, 35% residual activity
4-benzyloxycarbonylpiperidin-1-ium 4-methylbenzenesulfonate
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benzyl 1-(2-tert-butoxy-2-oxoethyl)piperidine-4-carboxylate
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N-[(S)-2-amino-4,5,6,7-tetrahydrobenzo[d]thiazol-6-yl]-1-[(S)-2-aminopropanoyl]piperidine-4-carboxamide
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tert-butyl 4-formylpiperidine-1-carboxylate
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tert-butyl 4-[(2-amino-4,5,6,7-tetrahydrobenzo[d]thiazol-6-yl)carbamoyl]piperidine-1-carboxylate
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tert-butyl 4-[methoxy(methyl)carbamoyl]piperidine-1-carboxylate
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tert-butyl [(S)-1-[4-((S)-2-amino-4,5,6,7-tetrahydrobenzo[d]thiazol-6-ylcarbamoyl)piperidin-1-yl]-1-oxopropan-2-yl]carbamate
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UDP-N-acetylmuramoyl-L-Ala-D-Glu
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above 10 mM
additional information
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design and synthesise a small focused library of peptidomimetics as potential inhibitors of MurE from Staphylococcus aureus, overview
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isopropyl-beta-D-thiogalactosylpyranoside
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concentration 1mM
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0.087 - 0.59
UDP-N-acetylmuramoyl-L-Ala-D-Glu
0.125
ATP
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23°C
0.52
ATP
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in presence of 2 mM K2HPO4
0.55
ATP
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in presence of 30 mM K2HPO4
0.0205
L-Lys
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23°C
0.55
L-Lys
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pH 8.6, 37°C
0.55
L-lysine
pH 8.6, 37°C, recombinant wild-type enzyme
2.8
L-lysine
pH 8.6, 37°C, recombinant mutant D406A
3.1
L-lysine
pH 8.6, 37°C, recombinant mutant P408A
20
L-lysine
above, pH 8.6, 37°C, recombinant mutant A409R
20
L-lysine
above, pH.6, 37°C, recombinant mutant E460A
0.37
Lys
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in presence of 30 mM K2HPO4
0.42
Lys
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in presence of 2 mM K2HPO4
0.44
Lys
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in presence of 60 mM KCl
0.49
Lys
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in presence of 60 mM KCl
0.087
UDP-N-acetylmuramoyl-L-Ala-D-Glu
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pH 8.6, 37°C
0.122
UDP-N-acetylmuramoyl-L-Ala-D-Glu
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23°C
0.53
UDP-N-acetylmuramoyl-L-Ala-D-Glu
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in presence of 30 mM K2HPO4
0.57
UDP-N-acetylmuramoyl-L-Ala-D-Glu
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in presence of 2 mM K2HPO4
0.59
UDP-N-acetylmuramoyl-L-Ala-D-Glu
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in presence of 60 mM KCl
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9
UDP-N-acetylmuramoyl-L-Ala-D-Glu
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23°C
0.001
L-lysine
pH 8.6, 37°C, recombinant mutant D406A
0.283
L-lysine
pH 8.6, 37°C, recombinant mutant P408A
4.833
L-lysine
pH 8.6, 37°C, recombinant wild-type enzyme
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0.001
L-lysine
pH 8.6, 37°C, recombinant mutant D406A
0.003
L-lysine
above, pH 8.6, 37°C, recombinant mutant A409R
0.029
L-lysine
above, pH.6, 37°C, recombinant mutant E460A
0.091
L-lysine
pH 8.6, 37°C, recombinant mutant P408A
8.787
L-lysine
pH 8.6, 37°C, recombinant wild-type enzyme
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0.7
(2R)-2-amino-6-([[(3R)-3-carboxy-3-([N-[6-(phosphonooxy)hexanoyl]-L-alanyl]amino)propyl](hydroxy)phosphoryl]methyl)heptanedioic acid
Staphylococcus aureus
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pH and temperature not specified in the publication
0.0011
(2R)-2-amino-6-([[(3R)-3-carboxy-3-[[N-(6-[[[[[[(2R,5S)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methoxy](hydroxy)phosphoryl]oxy](hydroxy)phosphoryl]oxy]hexanoyl)-L-alanyl]amino]propyl](hydroxy)phosphoryl]methyl)heptanedioic acid
Staphylococcus aureus
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pH and temperature not specified in the publication
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23.4
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cells induced with isopropyl-beta-D-thiogalactosylpyranoside
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8.6
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assay at
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8 - 8.5
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activity decreases sharply below pH 8.0, optimal activity at pH 8.5
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37
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assay at
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15 - 40
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15°C: about 30% of maximal activity, 40°C: about 45% of maximal activity
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6.02
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calculation from amino acid sequence
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9602
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brenda
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brenda
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brenda
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brenda
9602
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brenda
enzyme is synthesized during vegetative growth
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brenda
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brenda
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SwissProt
brenda
gene murE
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brenda
temperature sensitive mutant
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brenda
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brenda
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the activity of L-lysine ligase, which is required only for the synthesis of vegetative peptidoglycan, decays after the end of of vegetative growth, except for a small but reproducible increase in activity just prior to the onset of refractility
brenda
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brenda
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metabolism
the enzyme is involved in peptidoglycan biosynthesis and cell wall assembly
additional information
ATP-binding site structure and homology, overview. Asn407 makes a series of structurally important hydrogen bond interactions within the context of the architecture of the active site region
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purified recombinant His-tagged enzyme in complex with UDP-MurNAc-Ala-Glu-Lys or with UDP-MurNAc-Ala-Glu-Lys and ADP, from 0.1 M Na-HEPES/MOPS, pH 7.5, 0.09 M nitrate phosphate sulfate mix, 30% w/v PEG550MME/PEG20K, method evaluation, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, molecular replacement
crystals are obtained by the hanging-drop vapour-diffusion method at 291 K from solutions containing 25%(w/v) polyethylene glycol 2000 monomethylether, 0.2 M potassium thiocyanate, 0.1 M MES pH 6.5 in the presence of uridine 5'-diphospho-N-acetylmuramoyl alanyl glutamate (UDP-MurNAc-l-Ala-d-Glu) with and without 5'-adenylyl imidophosphate (AMP-PNP), a non-hydrolysable analogue of ATP. Crystals grown in the presence of two ligands belong to space group P1, with unit-cell parameters a = 68.4 A, b = 71.4 A, c = 74.8 A, alpha = 73.4, beta = 80.5, gamma = 72.3 A. Crystals grown in the presence of UDP-MurNAc-l-Ala-d-Glu alone belong to space group P2(1), with unit-cell parameters a = 71.1 A, b = 129.4 A, c = 74.6 A, beta = 106.3°
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A409R
site-directed mutagenesis, the lytic phenotype observed upon overexpression of the wild-type murESa gene is replicated with the mutant
D406A
site-directed mutagenesis, the mutant shows very low or no activity in vivo
E460A
site-directed mutagenesis, the mutant shows very low or no activity in vivo
N407A
site-directed mutagenesis, inactive mutant
N407R
site-directed mutagenesis, the growth curve of N407R mutant is similar to that of wild-type murESa
P408A
site-directed mutagenesis, the lytic phenotype observed upon overexpression of the wild-type murESa gene is replicated with the mutant
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7.5
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rapid loss of activity at or below, even at 0°C
1270
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-20°C, stable for over 3 months when stored in the lyophilized form
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3):pLysS by nickel affinity chromatography, gel filtration, and ion exchange chromatography
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cloned into the high-expression plasmid pET21b and overexpressed in Escherichia coli BL21 (DE3) Star
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expressed as a glutathione-S-transferase/His12 fusion in Escherichia coli
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expressed in Escherichia coli. Overexpression induced with isopropyl-beta-D-thiogalactosylpyranoside results in abnormal morphological changes and subsequent cell lysis
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expression in Escherichia coli
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gene murE, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3):pLysS from plasmid pET2160:murESa, coexpression with chaperone from pREP4groESL
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Linnett, P.E.; Tipper, D.J.
Cell wall polymers of Bacillus sphaericus: activities of enzymes involved in peptidoglycan precursor synthesis during sporulation
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342-354
1974
Lysinibacillus sphaericus
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Tipper, D.J.; Linnett, P.E.
Distribution of peptidoglycan synthetase activities between sporangia and forespores in sporulating cells of Bacillus sphaericus
J. Bacteriol.
126
213-221
1976
Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
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Anwar, R.A.; Vlaovic, M.
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase from Bacillus sphaericus: activation by potassium phosphate
Biochem. Cell Biol.
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1986
Lysinibacillus sphaericus
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Chatterjee, A.N.; Young, F.E.
Regulation of the bacterial cell wall: isolation and characterization of peptidoglycan mutants of Staphylococcus aureus
J. Bacteriol.
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220-230
1972
Staphylococcus aureus
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Good, C.M.; Tipper, D.J.
Conditional mutants of Staphylococcus aureus defective in cell wall precursor synthesis
J. Bacteriol.
111
231-241
1972
Staphylococcus aureus
brenda
Ito, E.; Strominger, J.L.
Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine
J. Biol. Chem.
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2689-2695
1962
Staphylococcus aureus
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brenda
Mengin-Lecreulx, D.; Falla, T.; Blanot, D.; van Heijenoort, J.; Adams, D.J.; Chopra, I.
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
1999
Staphylococcus aureus
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Blewett, A.M.; Lloyd, A.J.; Echalier, A.; Fulop, V.; Dowson, C.G.; Bugg, T.D.; Roper, D.I.
Expression, purification, crystallization and preliminary characterization of uridine 5'-diphospho-N-acetylmuramoyl L-alanyl-D-glutamate:lysine ligase (MurE) from Streptococcus pneumoniae 110K/70
Acta Crystallogr. Sect. D
60
359-361
2004
Streptococcus pneumoniae
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Triolo, T.A.; Chabin, R.M.; Pompliano, D.L.
Cloning, expression and characterization of the Streptococcus pyogenes murE gene encoding a UDP-MurNAc-L-alanyl-D-glutamate: L-lysine ligase
Enzyme Microb. Technol.
35
300-308
2004
Streptococcus pyogenes
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Strancar, K.; Boniface, A.; Blanot, D.; Gobec, S.
Phosphinate inhibitors of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: L-lysine ligase (MurE)
Arch. Pharm.
340
127-134
2007
Staphylococcus aureus
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Patin, D.; Boniface, A.; Kovac, A.; Herv, M.; Dementin, S.; Barreteau, H.; Mengin-Lecreulx, D.; Blanot, D.
Purification and biochemical characterization of Mur ligases from Staphylococcus aureus
Biochimie
92
1793-1800
2010
Staphylococcus aureus
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Zivec, M.; Turk, S.; Blanot, D.; Gobec, S.
Design and synthesis of new peptidomimetics as potential inhibitors of MurE
Acta Chim. Slov.
58
95-109
2011
Staphylococcus aureus
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Ruane, K.M.; Lloyd, A.J.; Fueloep, V.; Dowson, C.G.; Barreteau, H.; Boniface, A.; Dementin, S.; Blanot, D.; Mengin-Lecreulx, D.; Gobec, S.; Dessen, A.; Roper, D.I.
Specificity determinants for lysine incorporation in Staphylococcus aureus peptidoglycan as revealed by the structure of a MurE enzyme ternary complex
J. Biol. Chem.
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33439-33448
2013
Staphylococcus aureus (Q2FZP6)
brenda
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