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Information on EC 2.7.7.99 - N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
for references in articles please use BRENDA:EC2.7.7.99
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.99 N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
IUBMB Comments
The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
murU, N-acetylmuramate alpha-1-phosphate uridylyltransferase, NAM alpha-1 phosphate uridylyl transferase, pp_0406, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
murU
N-acetylmuramate alpha-1-phosphate uridylyltransferase
NAM alpha-1 phosphate uridylyl transferase
pp_0406
murU
-
-
-
-
N-acetylmuramate alpha-1-phosphate uridylyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP + N-acetyl-alpha-D-muramate 1-phosphate = UDP-N-acetyl-alpha-D-muramate + phosphate
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
peptidoglycan recycling II
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SYSTEMATIC NAME
IUBMB Comments
UDP:N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
Substrates: -
Products: -
Products: -
?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: ATP, CTP, TTP, or GTP
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: ATP, CTP, TTP, or GTP
Products: -
Products: -
?
additional information
?
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Substrates: no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
UDP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + phosphate
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
two Mg2+ ions are likely part of the active site. Mg2+ is not required for substrate binding per se
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme is involved in peptidoglycan cell wall biosynthesis
metabolism
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
metabolism
-
the enzyme is involved in peptidoglycan cell wall biosynthesis
-
metabolism
-
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
-
metabolism
-
the enzyme is involved in peptidoglycan cell wall biosynthesis
-
metabolism
-
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
-
metabolism
-
the enzyme is involved in peptidoglycan cell wall biosynthesis
-
metabolism
-
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
-
physiological function
enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity
physiological function
the metabolic pathway of anomeric cell wall amino sugar kinase AmgK and uridylyl transferase MurU converts N-acetylmuramic acid to uridine diphosphate-N-acetylmuramic acid. It is responsible for the high intrinsic resistance of Pseudomonas aeruginosa to fosfomycin due to bypassing the fosfomycin-sensitive de novo synthesis of UDP-N-acetylmuramic acid
physiological function
-
enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity
-
physiological function
-
the metabolic pathway of anomeric cell wall amino sugar kinase AmgK and uridylyl transferase MurU converts N-acetylmuramic acid to uridine diphosphate-N-acetylmuramic acid. It is responsible for the high intrinsic resistance of Pseudomonas aeruginosa to fosfomycin due to bypassing the fosfomycin-sensitive de novo synthesis of UDP-N-acetylmuramic acid
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MURU_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
223
0
23814
Swiss-Prot
-
MURU_CAUVC
Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)
242
0
25590
Swiss-Prot
-
MURU_NEIMB
Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
231
0
24537
Swiss-Prot
-
MURU_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
224
0
24149
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of MurU in native and ligand-bound states at 1.8 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
additional information
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
additional information
-
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
-
additional information
-
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
-
additional information
-
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
-
additional information
-
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
-
additional information
-
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
-
additional information
-
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged MurU from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, tag cleavage by PreScission protease, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene murU, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Renner-Schneck, M.; Hinderberger, I.; Gisin, J.; Exner, T.; Mayer, C.; Stehle, T.
Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens
J. Biol. Chem.
290
10804-10813
2015
Pseudomonas putida (Q88QT2), Pseudomonas putida DSM 6125 (Q88QT2)
brenda
Borisova, M.; Gisin, J.; Mayer, C.
Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates intrinsic resistance to fosfomycin
Microb. Drug Resist.
20
231-237
2014
Pseudomonas putida (Q88QT2), Pseudomonas putida DSM 6125 (Q88QT2)
brenda
Gisin, J.; Schneider, A.; Naegele, B.; Borisova, M.; Mayer, C.
A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis
Nat. Chem. Biol.
9
491-493
2013
Pseudomonas putida (Q88QT2), Pseudomonas putida DSM 6125 (Q88QT2)
brenda
DeMeester, K.E.; Liang, H.; Jensen, M.R.; Jones, Z.S.; D'Ambrosio, E.A.; Scinto, S.L.; Zhou, J.; Grimes, C.L.
Synthesis of functionalized N-acetyl muramic acids to probe bacterial cell wall recycling and biosynthesis
J. Am. Chem. Soc.
140
9458-9465
2018
Pseudomonas putida (Q88QT2), Pseudomonas putida ATCC 47054 (Q88QT2), Pseudomonas putida DSM 6125 (Q88QT2), Pseudomonas putida NCIMB 11950 (Q88QT2)
brenda
Ukaegbu, O.I.; DeMeester, K.E.; Liang, H.; Brown, A.R.; Jones, Z.S.; Grimes, C.L.
Utility of bacterial peptidoglycan recycling enzymes in the chemoenzymatic synthesis of valuable UDP sugar substrates
Methods Enzymol.
638
1-26
2020
Pseudomonas putida (Q88QT2), Pseudomonas putida ATCC 47054 (Q88QT2), Pseudomonas putida DSM 6125 (Q88QT2), Pseudomonas putida NCIMB 11950 (Q88QT2)
brenda
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