Information on EC 2.7.1.170 - anhydro-N-acetylmuramic acid kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.170
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RECOMMENDED NAME
GeneOntology No.
anhydro-N-acetylmuramic acid kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anhydromuropeptides recycling
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SYSTEMATIC NAME
IUBMB Comments
ATP:1,6-anhydro-N-acetyl-beta-muramate 6-phosphotransferase
This enzyme, along with EC 4.2.1.126, N-acetylmuramic acid 6-phosphate etherase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the alpha- and beta-anomers.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene anmK
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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1,6-anhydro-N-acetylmuramic acid is produced during peptidoglucan degeneration by transglycosylases, e.g. AmpD or NagZ. The AnmK reaction product N-acetylmuramate 6-phosphate returns into peptidoglycan recycling
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
show the reaction diagram
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetylmuramate 6-phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetylmuramate 6-phosphate
show the reaction diagram
additional information
?
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AnmK is an unusual sugar kinase that both cleaves and phosphorylates its 1,6-anhMurNAc substrate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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enzyme AnmK adopts an open conformation in solution in the absence of ligand and that it remains in this open state after binding nonhydrolyzable ATP analogue adenosine 5'-(beta,gamma-methylene)triphosphate (AMPPCP)
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 1
1,6-anhydro-N-acetyl-beta-muramate
1
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7000
1,6-anhydro-N-acetyl-beta-muramate
Escherichia coli
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pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
ADP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39500
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calculated from amino acid sequence
40000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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the enzyme structure exhibits two major domains separated by a deep hinge region with the nucleotide and sugar binding near the hinge. The protein forms a dimer, with extensive interactions between the two monomers
homodimer
x-ray crystallography
additional information
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open and closed ligand-bound enzyme structure, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
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analysis of several crystal structures
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AnmK in complex with 1,6-anhydro-N-acetylmuramic acid and ADP, hanging drop vapor diffusion method, using 25% (w/v) polyethylene glycol 4000, 0.2 M (NH4)2SO4, and 0.1 M tri-sodium citrate (pH 5.6)
purified recombinant enzyme bound to a nonhydrolyzable ATP analogue (AMPPCP) and 1,6-anhydroMurNAc, hanging drop vapor diffusion method, for enzyme AnmK bound to AMPPCP, 6.5 mg/ml protein in 600 mM NaCl, 2 mM AMPPCP, 4 mM MgCl2, 0.5 mM TCEP, and 20 mM Tris, pH 8.0, is mixed with an equal volume of mother liquor containing 26% PEG 4000, 0.2 M MgCl2, 0.1 M Tris, pH 9.0, for enzyme AnmK bound to AMPPCP and the anhMurNAc sugar, AnmK s first co-crystallized with AMPPCP by mixing equal volumes of mother liquor containing 24% PEG 4000, 0.2 M MgCl2, 0.1 M Tris, pH 8.2, with the enzyme at 6.5 mg/ml in 600 mM NaCl, 2 mM AMPPCP, 4 mM MgCl2, 0.5 mM TCEP, 20 mM Tris, pH 8.0, a single crystal of the AnmK-AMPPCP complex is then transferred to a drop of reservoir buffer supplemented with 8 mM anhMurNAc, 2 mM AMPPCP, and 4 mM MgCl2 and soaked for 1 h, at room temperature, X-ray diffraction structure determination and analysis at 1.67-1.84 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephacel column chromatography, hydroxylapatite column chromatography, and Mono Q column chromatography
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Ni-NTA-agarose column chromatography and gel filtration
recombinant enzyme from Escherichia coli strain BL21(DE3) GOLD by metal affinity chromatography, gel filtration, and ultrafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) Gold cells
gene anmK, phylogenetic analysis and tree
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gene anmK, recombinant expression in Escherichia coli
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gene anmK, recombinant expression in Escherichia coli strain BL21(DE3) GOLD
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phylogenetic analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D182A
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site-directed mutagenesis, inactive catalytic site mutant
D182N
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site-directed mutagenesis, inactive catalytic site mutant
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