Information on EC 4.2.1.126 - N-acetylmuramic acid 6-phosphate etherase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.126
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RECOMMENDED NAME
GeneOntology No.
N-acetylmuramic acid 6-phosphate etherase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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anhydromuropeptides recycling
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
(R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming)
This enzyme, along with EC 2.7.1.170, anhydro-N-acetylmuramic acid kinase, 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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene MurQ-HI
UniProt
Manually annotated by BRENDA team
gene MurQ-HI
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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a murQ deletion mutant cannot grow on N-acetylmuramic acid as the sole source of carbon
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-chloro-3-deoxy-N-acetylglucosamine 6-phosphate
(2E)-2-(acetylamino)-2,3-dideoxy-6-O-phosphono-D-erythro-hex-2-enose + HCl
show the reaction diagram
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slow conversion, 2% activity compared to N-acetylmuramate 6-phosphate
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?
N-acetylmuramate 6-phosphate + H2O
(R)-lactate + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
N-acetylmuramate 6-phosphate + H2O
D-lactate + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
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?
N-acetylmuramate 6-phosphate + H2O
N-acetyl-D-glucosamine 6-phosphate + D-lactate
show the reaction diagram
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?
additional information
?
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N-acetylmuramate is not a substrate nor are anhydro-N-acetylmuramate or muramic acid
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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
N-acetylmuramate 6-phosphate + H2O
(R)-lactate + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-2-[[(2R,3R,4R)-5-(acetylamino)-2,3,7-trihydroxy-1-(phosphonooxy)heptan-4-yl]oxy]propanoic acid
a N-acetylmuramate 6-phosphate open chain analogue, competitive inhibition
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(2R,3S,4R)-5-(acetylamino)-2,3,4,7-tetrahydroxyheptyl phosphate
a N-acetyl-D-glucosamine 6-phosphate open chain analogue, competitive inhibition
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EDTA
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5 mM EDTA results in only weak inhibition (25% reduction in rate)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32 - 1.2
N-acetylmuramate 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 5.7
N-acetylmuramate 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0088 - 4.8
N-acetylmuramate 6-phosphate
6386
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
(2R)-2-[[(2R,3R,4R)-5-(acetylamino)-2,3,7-trihydroxy-1-(phosphonooxy)heptan-4-yl]oxy]propanoic acid
pH 8.0, 30C
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1.1
(2R,3S,4R)-5-(acetylamino)-2,3,4,7-tetrahydroxyheptyl phosphate
pH 8.0, 30C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme as apoenzyme and in complex with inhibitor (2R)-2-[[(2R,3R,4R)-5-(acetylamino)-2,3,7-trihydroxy-1-(phosphonooxy)heptan-4-yl]oxy]propanoic acid, sitting drop vapor diffusion method, mixing of 8 mg/mL protein in 200 mM NaCl, 50 mM HEPES, and 5% glycerol with 0.2 M NaCl, 0.1 M Bis-Tris-HCl, pH 5.5, and 25% w/v PEG 3350 or with 0.17 M ammonium sulfate, 25.5% w/v PEG 4000, and 15% v/v glycerol, the former gives better results, soaking of crystals in solution containing the inhibitor, 25C, X-ray diffraction structure determinnation and analysis at 2.6 A and 2.4 A resolution, respectively, molecular replacement using PDB entry 1NRI as the template
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, imidazole buffer (pH 8.0) by adding 20% glycerol and 1 mM dithiothreitol, at least several weeks, activity is retained
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4C, purified etherase is only active for a few days
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temperature, storage medium, duration, loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating HP column chromatography, gel filtration
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Ni2+-chelating Sepharose column chromatography, gel filtration
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recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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gene MurQ-HI, functional expression of N-terminally His6-tagged enzyme in Escherichia coli
MurQ-His fusion protein is expressed in Escherichia coli BL21 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D115N
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the mutant exhibits a 7fold reduction in the value of kcat
E114Q
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the mutant shows a dramatic reduction in the value of kcat (2000fold) and a modest decrease in the value of KM (4fold)
E83A
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the mutant is essentially inactive, the mutant shows a very low, but measurable, level of activity with a kcat value that wis 10000fold lower than that of the wild type enzyme
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