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Information on EC 6.3.2.8 - UDP-N-acetylmuramate-L-alanine ligase and Organism(s) Escherichia coli and UniProt Accession P11880
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6.3.2.8 UDP-N-acetylmuramate-L-alanine ligaseIUBMB Comments
Involved in the synthesis of a cell-wall peptide in bacteria.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
udp-n-acetylmuramate:l-alanine ligase, murc ligase, udp-n-acetylmuramate-l-alanine ligase, udp-n-acetylmuramoyl:l-alanine ligase, udp-n-acetylmuramic acid l-alanine ligase, udp-n-acetylmuramoyl-l-alanine synthetase, udp-n-acetylmuramyl:l-alanine ligase, udp-murnac:l-alanine ligase, l-alanine adding enzyme, uridine diphosphate n-acetylmuramate:l-alanine ligase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alanine-adding enzyme
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L-Ala ligase
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L-Alanine adding enzyme
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MurC
Synthetase, uridine diphospho-N-acetylmuramoylalanine
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UDP-acetylmuramoyl-L-alanine synthetase
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UDP-MurNAc:L-alanine ligase
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UDP-N-acetylmuramate-alanine ligase
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UDP-N-acetylmuramoyl-L-alanine synthetase
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UDP-N-acetylmuramoylalanine synthetase
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UDP-N-acetylmuramyl:L-alanine ligase
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Uridine 5´-diphosphate-N-acetylmuramyl-L-alanine synthetase
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Uridine diphosphate N-acetylmuramate:L-alanine ligase
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Uridine diphospho-N-acetylmuramoylalanine synthetase
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Uridine-diphosphate-N-acetylmuramate:L-alanine ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
ligase-catalyzed peptide formation proceeds through an activated acyl-phosphate linkage during the reaction process. ATP assists in this process of the peptide bond formation by donating its gamma-phosphoryl group to activate the carboxyl group of UDP-N-acetylmuramate
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ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
the binding order of the substrates can be ATP, UDP-N-acetylmuramate, and Ala
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ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
ordered sequential mechanism, with ATP binding first, N-acetylmuramate second, L-Ala third, and ADP being the last product released
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide formation
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carboxamide formation
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
Involved in the synthesis of a cell-wall peptide in bacteria.
CAS REGISTRY NUMBER
COMMENTARY
9023-52-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + dihydro-UDP-N-acetylmuramate + L-Ala
ADP + phosphate + dihydro-UDP-N-acetylmuramoyl-L-Ala
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-
-
-
?
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
ATP + UDP-N-acetyl-beta-D-muramate + L-alanine
ADP + phosphate + UDP-N-acetyl-beta-D-muramoyl-L-alanine
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-
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-
?
ATP + UDP-N-acetylglucosaminyl-enoylpyruvate + L-Ala
ADP + phosphate + UDP-N-acetylglucosaminyl-enoylpyruvoyl-L-Ala
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?
ATP + UDP-N-acetylglucosyl-enolpyruvate + L-alanine
ADP + phosphate + UDP-N-acetylglucosyl-enolpyruvoyl-L-alanine
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?
ATP + UDP-N-acetylmuramate + 2-amino-benzylpropionate
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-benzylpropionate
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?
ATP + UDP-N-acetylmuramate + 2-amino-ethylpropionate
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-ethylpropionate
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?
ATP + UDP-N-acetylmuramate + 2-amino-methylpropionate
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-methylpropionate
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?
ATP + UDP-N-acetylmuramate + 2-amino-N-butyric acid
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-N-butyric acid
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?
ATP + UDP-N-acetylmuramate + 2-amino-N-hydroxymethyl propionamide
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-N-hydroxymethylpropionamide
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?
ATP + UDP-N-acetylmuramate + 2-amino-propionamide
ADP + phosphate + UDP-N-acetylmuramoyl-2-aminopropionamide
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?
ATP + UDP-N-acetylmuramate + 2-amino-tert-butylpropionate
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-tert-butylpropionate
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?
ATP + UDP-N-acetylmuramate + benzyl L-alaninate
ADP + phosphate + benzyl UDP-N-acetylmuramoyl-L-alanine
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?
ATP + UDP-N-acetylmuramate + beta-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-beta-Ala
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?
ATP + UDP-N-acetylmuramate + beta-chloro-L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-beta-chloro-L-Ala
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?
ATP + UDP-N-acetylmuramate + beta-cyano-L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-beta-cyano-L-Ala
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?
ATP + UDP-N-acetylmuramate + DL-propargylglycine
ADP + phosphate + UDP-N-acetylmuramoyl-DL-propargylglycine
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?
ATP + UDP-N-acetylmuramate + DL-Ser
ADP + phosphate + UDP-N-acetylmuramoyl-DL-Ser
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?
ATP + UDP-N-acetylmuramate + ethyl L-alaninate
ADP + phosphate + ethyl UDP-N-acetylmuramoyl-L-alaninate
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?
ATP + UDP-N-acetylmuramate + Gly
ADP + phosphate + UDP-N-acetylmuramoyl-Gly
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?
ATP + UDP-N-acetylmuramate + L-alanine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
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?
ATP + UDP-N-acetylmuramate + L-Cys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Cys
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?
ATP + UDP-N-acetylmuramate + L-Ile
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ile
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?
ATP + UDP-N-acetylmuramate + L-serine
ADP + phosphate + UDP-N-acetylmuramoyl-L-serine
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?
ATP + UDP-N-acetylmuramate + L-Thr
ADP + phosphate + UDP-N-acetylmuramoyl-L-Thr
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?
ATP + UDP-N-acetylmuramate + L-Val
ADP + phosphate + UDP-N-acetylmuramoyl-L-Val
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?
ATP + UDP-N-acetylmuramate + L-vinylglycine
ADP + phosphate + UDP-N-acetylmuramoyl-L-vinylglycine
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?
ATP + UDP-N-acetylmuramate + methyl L-alaninate
ADP + phosphate + methyl UDP-N-acetylmuramoyl-L-alaninate
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?
ATP + UDP-N-acetylmuramate + N-(2-aminopropionyl)piperidine
ADP + phosphate + UDP-N-acetylmuramoyl-N-(2-aminopropionyl)piperidine
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?
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
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?
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
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determination by phosphate detection using malachite green reagent
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?
ATP + UDP-N-acetylmuramate + L-Ala
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adds the first amino acid to the sugar moiety of the peptidoglycan precursor, catalyzing one essential step in cell wall biosynthesis
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?
ATP + UDP-N-acetylmuramate + L-Ala
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formation of a acylphosphate intermediate
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?
ATP + UDP-N-acetylmuramate + L-Ala
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enzyme activity is not in excess in the cell under normal growth conditions, but the amount is adjusted to the requirements of peptidoglycan synthesis
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?
ATP + UDP-N-acetylmuramate + L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
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?
ATP + UDP-N-acetylmuramate + L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
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r
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?
ATP + UDP-N-acetylmuramate + L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
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alpha- and beta-anomer of UDP-N-acetylmuramate
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?
additional information
?
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the enzyme hydrolyzes ATP in absence of L-Ala. This L-Ala independent activity is dependent upon the concentration of both ATP and UDP-N-acetylmuramate
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?
additional information
?
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enzyme catalyzes an exchange reaction leading to the formation of 4% of the UDP-N-acetylmuramoyl-L-[14C]Ala with UDP-N-acetylmuramoyl-L-Ala, L-[14C]Ala, ADP and phosphate
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?
additional information
?
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the Mur ligases constitute a series of four ATP-dependent enzymes, MurC to Mur, that are responsible for the stepwise addition of the pentapeptide side chain onto the D-lactoyl group of the uridine diphosphate-N-acetylmuramic acid initially formed via MurA and MurB, MurC catalyzes the additon of the first amino acid L-alanine. All of the Mur ligases catalyze the formation of an amide or peptide bond through the same reaction mechanism via a tetrahedral intermediate, overview
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine
ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
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?
ATP + UDP-N-acetylmuramate + L-alanine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
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?
additional information
?
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the Mur ligases constitute a series of four ATP-dependent enzymes, MurC to Mur, that are responsible for the stepwise addition of the pentapeptide side chain onto the D-lactoyl group of the uridine diphosphate-N-acetylmuramic acid initially formed via MurA and MurB, MurC catalyzes the additon of the first amino acid L-alanine. All of the Mur ligases catalyze the formation of an amide or peptide bond through the same reaction mechanism via a tetrahedral intermediate, overview
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?
ATP + UDP-N-acetylmuramate + L-Ala
?
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adds the first amino acid to the sugar moiety of the peptidoglycan precursor, catalyzing one essential step in cell wall biosynthesis
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?
ATP + UDP-N-acetylmuramate + L-Ala
?
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formation of a acylphosphate intermediate
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?
ATP + UDP-N-acetylmuramate + L-Ala
?
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enzyme activity is not in excess in the cell under normal growth conditions, but the amount is adjusted to the requirements of peptidoglycan synthesis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mn2+
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optimal concentration: 5 mM, reaching 50% of the activity measured in the presence of 20 mM MgCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-[4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]piperidin-2-yl)methanol
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(1R,2S)-1-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2,3-dihydro-1H-inden-2-ol
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(2R)-2-((4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino)-3-cyclohexylpropan-1-ol
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a pyrazolopyrimidine, is a potent inhibitor of the enzyme and is active against an efflux pump mutant of Escherichia coli, but cellular activity against Escherichia coli is not observed. MIC values for (2R)-2-((4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino)-3-cyclohexylpropan-1-ol are 0.2 mM for wild-type Escherichia coli and 0.0125 for Escherichia coli tolC mutant
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(2-methoxypyridin-4-yl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(3-chloropyridin-4-yl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(3-fluorophenyl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(3-methyl-1,2-oxazol-5-yl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(4-methoxyphenyl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(pyridin-2-yl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(pyridin-3-yl)ethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-cyclohexylethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethan-1-ol
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl (2-aminoethyl)carbamate
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl (2-hydroxyethyl)carbamate
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl (2R)-2-(aminomethyl)morpholine-4-carboxylate
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl hydroxycarbamate
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl [(1,5-dihydroxy-4-oxo-1,4-dihydropyridin-2-yl)methyl]carbamate
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl [2-(3-oxopyrazolidin-1-yl)ethyl]carbamate
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(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl [[(4S)-3-methyl-2-oxoimidazolidin-4-yl]methyl]carbamate
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(2R)-2-([4-[(5-tert-butyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-cyclohexylethan-1-ol
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(2R)-2-cyclohexyl-2-[(4-[[5-(propan-2-yl)-1H-pyrazol-3-yl]amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino]ethan-1-ol
-
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(2S)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-cyclohexylethan-1-ol
-
-
(2S)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethan-1-ol
-
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(2S)-2-cyclohexyl-2-([4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)ethan-1-ol
-
-
(2S)-2-cyclohexyl-2-[(4-[[5-(propan-2-yl)-1H-pyrazol-3-yl]amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino]ethan-1-ol
-
-
(5Z)-5-([2-[(4-chlorobenzyl)sulfanyl]-5-nitrophenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-([4-[(E)-2-phenylethenyl]phenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
2-((4-[(2S)-butan-2-ylamino]-6-(ethylamino)-1,3,5-triazin-2-yl)sulfanyl)-N-(2-chlorophenyl)acetamide
0.5 mM, 26% inhibition
2-(4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl} phenoxy) acetic acid
-
complete inhibition at 0.5 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 2-nitrobenzenesulfonate
-
55% inhibition at 0.05 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 3-nitrobenzenesulfonate
-
65% inhibition at 0.05 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 4-nitrobenzenesulfonate
-
75% inhibition at 0.10 mM
2-([2-(naphthalen-2-ylsulfonyl)hydrazono]methyl)phenyl 2-(benzo[d][1,3]dioxol-5-yl)acetate
-
57% inhibition at 0.10 mM
2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(oxan-4-yl)ethan-1-ol
-
-
2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-3-methylbutan-1-ol
-
-
2-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
41% inhibition at 0.10 mM
2-phenyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
-
18% inhibition at 0.25 mM
2-[4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono} methyl)phenoxy]acetic acid
-
complete inhibition at 0.5 mM
4-([(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl)-6-(naphthalen-2-ylmethyl)-1,3,5-triazin-2-amine
0.5 mM, 30% inhibition
4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono} methyl)benzoic acid
-
94% inhibition at 0.5 mM
4-cyano-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
91% inhibition at 0.05 mM
4-methyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
-
26% inhibition at 0.5 mM
4-methyl-N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]-1,3-thiazole-5-carbohydrazide
-
complete inhibition at 0.5 mM
4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl}benzoic acid
-
complete inhibition at 0.5 mM
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
-
IC50 2.3 microM
6-([(1,1-dioxidotetrahydrothiophen-3-yl)sulfanyl]methyl)-N-(2-phenylethyl)-1,3,5-triazine-2,4-diamine
0.25 mM, 32% inhibition
6-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N,N'-diphenyl-1,3,5-triazine-2,4-diamine
0.5 mM, 36% inhibition
benzylidene rhodanines
-
possess MurC inhibitory activity in the low micromolar range
-
feglymycin
-
isolated from Streptomyces sp. DSM 11171, 13-mer peptide, noncompetitive inhibition, the inhibition is fully reversible after dilution
methyl4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono}methyl)benzoate
-
95% inhibition at 0.5 mM
methyl4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl} benzoate
-
complete inhibition at 0.5 mM
N'-((2-[(2-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
30% inhibition at 0.10 mM
N'-((2-[(3-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
36% inhibition at 0.05 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)(2-fluorophenyl)methanesulfonohydrazide
-
59% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)(phenyl)methanesulfonohydrazide
-
complete inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
36% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-nitrobenzenesulfonohydrazide
-
95% inhibition at 0.01 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-3-nitrobenzenesulfonohydrazide
-
-
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)[4-(trifluoromethyl)phenyl]methanesulfonohydrazide
-
-
N'-((3-[(3-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
58% inhibition at 0.05 mM
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
42% inhibition at 0.25 mM
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
64% inhibition at 0.10 mM
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
74% inhibition at 0.25 mM
N'-[(E)-(2-hydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 0.25 mM
N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]-1H-indazole-3-carbohydrazide
-
78% inhibition at 0.10 mM
N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]benzohydrazide
-
70% inhibition at 0.25 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
36% inhibition at 0.5 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide
-
95% inhibition at 0.5 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]benzohydrazide
-
complete inhibition at 0.5 mM
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 0.5 mM
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide
-
complete inhibition at 0.5 mM
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]benzohydrazide
-
97% inhibition at 0.5 mM
N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide
-
43% inhibition at 0.25 mM
N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene] benzohydrazide
-
92% inhibition at 0.5 mM
N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
67% inhibition at 0.25 mM
N'-[(E)-(4-cyanophenyl)methylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 0.25 mM
N'-[(E)-(4-cyanophenyl)methylidene]benzohydrazide
-
complete inhibition at 0.25 mM
N'-[(E)-(4-nitrophenyl)methylidene]-1H-indazole-3-carbohydrazide
-
91% inhibition at 0.5 mM
N'-[(E)-1H-indol-3-ylmethylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 010 mM
N'-{(E)-[4-(dimethylamino)phenyl]methylidene}-1H-indazole-3-carbohydrazide
-
95% inhibition at 0.25 mM
N'-{(E)-[4-(dimethylamino)phenyl]methylidene}-4-methyl-1,3-thiazole-5-carbohydrazide
-
97% inhibition at 0.25 mM
N'-{(E)-[4-(dimethylamino)phenyl]methylidene}benzohydrazide
-
complete inhibition at 0.25 mM
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-3,5-dinitrobenzamide
-
51% inhibition at 0.10 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-3,5-dinitrobenzamide
-
72% inhibition at 0.10 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
-
71% inhibition at 0.05 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
97% inhibition at 0.10 mM
N-[(E)-(2,4-dihydroxyphenyl)methylidene]benzohydrazide
-
complete inhibition at 0.5 mM
potassium phosphate
-
no effect up to 20 mM, significant decrease of activity at higher concentrations
UDP-2-(acetylamino)-4-O-[[(2-carboxypropyl)(hydroxy)phosphoryl]methyl]-2-deoxy-alpha-D-glucopyranose
-
-
additional information
-
synthesis and evaluation of a series of transition-state analog inhibitors
-
additional information
-
design and synthesis of N-benzylidenesulfonohydrazide inhibitors of MurC as antibacterial agents
-
additional information
-
inhibitor design and synthesis, mass spectrometric analysis, ligand molecular docking calculations, inhibitory potency, MIC values lay above 0.128 mg/ml, overview
-
additional information
-
a class of pyrazolopyrimidines with subnanomolar potency against both Escherichia coli and Pseudomonas aeruginosa MurC enzymes is constructed, which demonstrate a concomitant bactericidal activity against efflux-deficient strains. The compounds selectively inhibit peptidoglycan biosynthesis. In the presence of permeability enhancers such as colistin, pyrazolopyrimidines exhibit low micromolar MIC against the wild-type bacteria, thereby, indicating permeability and efflux as major challenges for this chemical series. Inhibitors evaluation and binding mode of pyrazolopyrimidines, docking study, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-value of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045 - 0.0063
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
0.0045
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
-
against ATP
0.0063
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
-
against UDP-N-acetylmuramate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000002
(1R,2S)-1-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2,3-dihydro-1H-inden-2-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000012
(2R)-2-((4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino)-3-cyclohexylpropan-1-ol
Escherichia coli
-
pH 8.0, 25°C, recombinant enzyme
0.000015
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(2-methoxypyridin-4-yl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000057
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(3-chloropyridin-4-yl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000004
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(3-fluorophenyl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.00006
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(3-methyl-1,2-oxazol-5-yl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000021
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(4-methoxyphenyl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.00004
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(pyridin-2-yl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000005
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000004
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl (2-aminoethyl)carbamate
Escherichia coli
-
pH and temperature not specified in the publication
0.000003
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl (2-hydroxyethyl)carbamate
Escherichia coli
-
pH and temperature not specified in the publication
0.000005
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl (2R)-2-(aminomethyl)morpholine-4-carboxylate
Escherichia coli
-
pH and temperature not specified in the publication
0.000052
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl hydroxycarbamate
Escherichia coli
-
pH and temperature not specified in the publication
0.000001
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl [(1,5-dihydroxy-4-oxo-1,4-dihydropyridin-2-yl)methyl]carbamate
Escherichia coli
-
pH and temperature not specified in the publication
0.00006
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl [2-(3-oxopyrazolidin-1-yl)ethyl]carbamate
Escherichia coli
-
pH and temperature not specified in the publication
0.000003
(2R)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethyl [[(4S)-3-methyl-2-oxoimidazolidin-4-yl]methyl]carbamate
Escherichia coli
-
pH and temperature not specified in the publication
0.000011
(2S)-2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-phenylethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.027
(5Z)-5-([2-[(4-chlorobenzyl)sulfanyl]-5-nitrophenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
Escherichia coli
-
pH 8.0, 37°C
0.018
(5Z)-5-([4-[(E)-2-phenylethenyl]phenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
Escherichia coli
-
pH 8.0, 37°C
0.000101
2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-2-(oxan-4-yl)ethan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.000188
2-([4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl]amino)-3-methylbutan-1-ol
Escherichia coli
-
pH and temperature not specified in the publication
0.032
2-phenyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
Escherichia coli
-
pH 8.0, 37°C
0.03
3-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
Escherichia coli
-
pH 8.0, 37°C
0.0023
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
Escherichia coli
-
Compound A, IC50 2.3 microM
0.027
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
Escherichia coli
-
pH 8.0, 37°C
0.031
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-naphthamide
Escherichia coli
-
pH 8.0, 37°C
0.051
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-nitrobenzamide
Escherichia coli
-
pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 10
-
7.5: about 70% of maximal activity, 10.0: about 95% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
UDP-N-acetylmuramic acid L-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death. The mutant strain shows accumulation of the MurC substrate and a decrease in the level of product upon treatment with (2R)-2-((4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino)-3-cyclohexylpropan-1-ol, indicating inhibition of MurC enzyme in these cells. Overexpression of wild-type MurC in the Escherichia coli tolC mutant leads to an increase in the compound A MIC by over 16fold, establishing a correlation between MurC inhibition and cellular activity
metabolism
-
the enzyme is essentially involved in the bacterial peptidoglycan biosynthesis pathway. MurC, the first of four Mur ligases, ligates L-alanine to UDP-N-acetylmuramic acid, initiating the synthesis of pentapeptide precursor
physiological function
-
the enzyme is essential for peptidoglycan biosynthesis. Peptidoglycan is an essential cell wall component of both gram-positive and gram-negative bacteria that protects the cytoplasmic membrane from osmotic stress
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54486
54486
-
1 * 54486, calculation from nucleotide sequence, electrospray ionization mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations
54486
-
2 * 54486, calculation from nucleotide sequence, electrospray mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 54486, calculation from nucleotide sequence, electrospray mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations
monomer
-
1 * 54486, calculation from nucleotide sequence, electrospray ionization mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase determined to 2.6 A resolution. The structure is solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212. Crystals of both native and SeMet-substituted EcMurC belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 73.9 A, b = 93.6 A, c = 176.8 A. The SeMet crystals give the best quality diffraction data
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C426A
-
Km increased 3fold for ATP and 10fold for UDP-MurNAc and L-alanine, with respect to the wild-type
H199A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
K130A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
N293A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
N296A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
R327A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM potassium phosphate, pH 7.2, 1 mM EDTA, 2.5 mM 2-mercaptoethanol, 15% glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant MurC from Escherichia coli strain JM83 by anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene murC, overexpression of wild-type MurC in the Escherichia coli tolC mutant
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mengin-Lecreulx, D.; Flouret, B.; Van Heijenoort, J.
Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
J. Bacteriol.
151
1109-1117
1982
Escherichia coli
Ishiguro, E.E.
Inhibition of uridine 5-diphosphate-N-acetylmuramyl-L-alanine synthetase by beta-chloro-L-alanine in Escherichia coli
Can. J. Microbiol.
28
654-659
1982
Escherichia coli
Falk, P.J.; Ervin, K.M.; Volk, K.S.; Ho, H.T.
Biochemical evidence of the formation of a covalent acyl-phosphate linkage between UDP-N-acetylmuramate and ATP in the Escherichia coli UDP-N-acetylmuramate:L-alanine ligase-catalyzed reaction
Biochemistry
35
1417-1422
1996
Escherichia coli
Jin, H.; Emanuele, J.J.; Fairman, R.; Robertson, J.G.; Hail, M.E.; Ho, H.T.; Falk, P.J.; Villafranca, J.J.
Structural studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase
Biochemistry
35
1423-1431
1996
Escherichia coli
Liger, D.; Blanot, D.; van Heijenoort, J.
Effect of various alanine analogues on the L-alanine-adding enzyme from Escherichia coli
FEMS Microbiol. Lett.
80
111-116
1991
Escherichia coli, Escherichia coli K12HfrH
Liger, D.; Masson, A.; Blanot, D.; van Heijenoort, J.; Parquet, C.
Study of the overproduced uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli
Microb. Drug Resist.
2
25-27
1996
Escherichia coli
Liger, S.; Masson, A.; Blanot, D.; van Heijenoort, J.; Parquet, C.
Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli
Eur. J. Biochem.
230
80-87
1995
Escherichia coli
Gubler, M.; Appold, Y.; Keck, W.
Overexpression, purification and characterization of UDP-N-acetylmuramyl:L-alanine ligase from Escherichia coli
J. Bacteriol.
178
906-910
1996
Escherichia coli
Emanuele, J.J.; Jin, H.; Jacobson, B.L.; Chang, C.Y.; Einspahr, H.M.; Villafranca, J.J.
Kinetic and crystallographic studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase
Protein Sci.
5
2566-2574
1996
Escherichia coli
Emanuele, J.J.; Jin, H.; Yanchunas, J.; Villafranca, J.J.
Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase
Biochemistry
36
7264-7271
1997
Escherichia coli
Bouhss, A.; Mengin-Lecreulx, D.; Blanot, D.; van Heijenoort, J.; Parquet, C.
Invariant amino acids in the Mur peptide synthetases of bacterial peptidoglycan synthesis and their modification by site-directed mutagenesis in the UDP-MurNAc;L-alanine ligase from Escherichia coli
Biochemistry
36
11556-11563
1997
Escherichia coli
Deva, T.; Pryor, K.D.; Leiting, B.; Baker, E.N.; Smith, C.A.
Purification, crystallization and preliminary x-ray analysis of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)
Acta Crystallogr. Sect. D
D59
1510-1513
2003
Escherichia coli (P11880), Escherichia coli
Reck, F.; Marmor, S.; Fisher, S.; Wuonola, M.A.
Inhibitors of the bacterial cell wall biosynthesis enzyme MurC
Bioorg. Med. Chem. Lett.
11
1451-1454
2001
Escherichia coli
Nosal, F.; Masson, A.; Legrand, R.; Blanot, D.; Schoot, B.; van Heijenoort, J.; Parquet, C.
Site-directed mutagenesis and chemical modification of the two cysteine residues of the UDP-N-acetylmuramoyl:L-alanine ligase of Escherichia coli
FEBS Lett.
426
309-313
1998
Escherichia coli
Bouhss, A.; Dementin, S.; van Heijenoort, J.; Parquet, C.; Blanot, D.
Formation of adenosine 5'-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli
FEBS Lett.
453
15-19
1999
Escherichia coli, Escherichia coli JM83(pAM1005)
Bouhss, A.; Dementin, S.; Van Heijenoort, J.; Parquet, C.; Blanot, D.
MurC and MurD synthetases of peptidoglycan biosynthesis: borohydride trapping of acyl-phosphate intermediates
Methods Enzymol.
354
189-196
2002
Escherichia coli, Escherichia coli JM83(pAM1005)
Ehmann, D.E.; Demeritt, J.E.; Hull, K.G.; Fisher, S.L.
Biochemical characterization of an inhibitor of Escherichia coli UDP-N-acetylmuramyl-L-alanine ligase
BIOCHIM. BIOPHYS. ACTA
1698
167-174
2004
Escherichia coli
Deng, G.; Gu, R.F.; Marmor, S.; Fisher, S.L.; Jahic, H.; Sanyal, G.
Development of an LC-MS based enzyme activity assay for MurC: application to evaluation of inhibitors and kinetic analysis
J. Pharm. Biomed. Anal.
35
817-828
2004
Escherichia coli
Deva, T.; Baker, E.N.; Squire, C.J.; Smith, C.A.
Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)
Acta Crystallogr. Sect. D
62
1466-1474
2006
Escherichia coli (P17952), Escherichia coli
Sink, R.; Kovac, A.; Tomasi?, T.; Rupnik, V.; Boniface, A.; Bostock, J.; Chopra, I.; Blanot, D.; Masic, L.P.; Gobec, S.; Zega, A.
Synthesis and biological evaluation of N-acylhydrazones as inhibitors of MurC and MurD ligases
ChemMedChem
3
1362-1370
2008
Escherichia coli
Frlan, R.; Kovac, A.; Blanot, D.; Gobec, S.; Pecar, S.; Obreza, A.
Design and synthesis of novel N-benzylidenesulfonohydrazide inhibitors of MurC and MurD as potential antibacterial agents
Molecules
13
11-30
2008
Escherichia coli
Tomasic, T.; Kovac, A.; Klebe, G.; Blanot, D.; Gobec, S.; Kikelj, D.; Masic, L.P.
Virtual screening for potential inhibitors of bacterial MurC and MurD ligases
J. Mol. Model.
18
1063-1072
2012
Escherichia coli (P17952)
Rausch, S.; Haenchen, A.; Denisiuk, A.; Loehken, M.; Schneider, T.; Suessmuth, R.
Feglymycin is an inhibitor of the enzymes MurA and MurC of the peptidoglycan biosynthesis pathway
ChemBioChem
12
1171-1173
2011
Escherichia coli, Staphylococcus aureus
Hameed P, S.; Manjrekar, P.; Chinnapattu, M.; Humnabadkar, V.; Shanbhag, G.; Kedari, C.; Mudugal, N.V.; Ambady, A.; de Jonge, B.L.; Sadler, C.; Paul, B.; Sriram, S.; Kaur, P.; Guptha, S.; Raichurkar, A.; Fleming, P.; Eyermann, C.J.; McKinney, D.C.; Sambandamurthy, V.K.; Panda, M.; Ravishankar, S.
Pyrazolopyrimidines establish MurC as a vulnerable target in Pseudomonas aeruginosa and Escherichia coli
ACS Chem. Biol.
9
2274-2282
2014
Escherichia coli, Pseudomonas aeruginosa, Pseudomonas aeruginosa Pae546
Humnabadkar, V.; Prabhakar, K.R.; Narayan, A.; Sharma, S.; Guptha, S.; Manjrekar, P.; Chinnapattu, M.; Ramachandran, V.; Hameed, S.P.; Ravishankar, S.; Chatterji, M.
UDP-N-acetylmuramic acid L-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death
Antimicrob. Agents Chemother.
58
6165-6171
2014
Escherichia coli, Pseudomonas aeruginosa
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