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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
IUBMB Comments The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
The expected taxonomic range for this enzyme is: Pseudomonas putida
Synonyms
murU, N-acetylmuramate alpha-1-phosphate uridylyltransferase, pp_0406,
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N-acetylmuramate alpha-1-phosphate uridylyltransferase
murU
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gene name
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N-acetylmuramate alpha-1-phosphate uridylyltransferase
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N-acetylmuramate alpha-1-phosphate uridylyltransferase
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pp_0406
gene name
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UDP + N-acetyl-alpha-D-muramate 1-phosphate = UDP-N-acetyl-alpha-D-muramate + phosphate
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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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UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
additional information
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UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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additional information
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no substrates: ATP, CTP, TTP, or GTP
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no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate
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no substrates: ATP, CTP, TTP, or GTP
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additional information
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no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate
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Mg2+
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two Mg2+ ions are likely part of the active site. Mg2+ is not required for substrate binding per se
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EDTA
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1 mM, complete loss of activity
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UniProt
brenda
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UniProt
brenda
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physiological function
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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
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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
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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; 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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MURU_CAUVC
Caulobacter vibrioides (strain ATCC 19089 / CB15)
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25590
Swiss-Prot
MURU_NEIMB
Neisseria meningitidis serogroup B (strain MC58)
231
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24537
Swiss-Prot
MURU_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
224
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24149
Swiss-Prot
MURU_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
223
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23814
Swiss-Prot
A0A4U8Z068_METTU
241
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26617
TrEMBL
A0A0H3CFI8_CAUVN
Caulobacter vibrioides (strain NA1000 / CB15N)
242
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25590
TrEMBL
A0A4U9GA19_9RHIZ
261
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28491
TrEMBL
A0A508X3U2_9RHIZ
243
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26406
TrEMBL
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Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
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25000 - 27000
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gel filtration
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monomer
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1 * 24879, calculated for recombinant His-tagged protein
monomer
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1 * 24879, calculated for recombinant His-tagged protein
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crystal structures of MurU in native and ligand-bound states at 1.8 A resolution
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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
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2.7.7.99 N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
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