Information on EC 1.13.11.73 - methylphosphonate synthase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.13.11.73
-
RECOMMENDED NAME
GeneOntology No.
methylphosphonate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
non-pathway related
-
-
Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (methylphosphonate forming)
Isolated from the marine archaeon Nitrosopumilus maritimus.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
-
apo MPnS homology modeling using the crystal structure of Cd2+-substituted HEPD, EC 1.13.11.72, in complex with substrate 2-hydroxyethylphosphonate, PDB ID 3GBF
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
show the reaction diagram
-
-
-
-
?
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
show the reaction diagram
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
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0071
(R)-2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
0.0065
(S)-2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
0.0045
2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
additional information
additional information
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steady-state Michaelis-Menten kinetics of mutant E176H
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
(R)-2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
0.17
(S)-2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
0.18
2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24
(R)-2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
26
(S)-2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
40
2-hydroxyethylphosphonate
-
temperature not specified in the publication, pH not specified in the publication
PDB
SCOP
CATH
UNIPROT
ORGANISM
Nitrosopumilus maritimus (strain SCM1);
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutant E176H, X-ray diffraction structure determination and analysis at 1.75 A resolution
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant mutant enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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recombinant expression of the mutant enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E176H
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site-directed mutagenesis, the HEPD, EC 1.13.11.72, mutant is bifunctional exhibiting the activity of both 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS). The product distribution of the mutant is sensitive to a substrate isotope effect, consistent with an isotope-sensitive branching mechanism involving a common intermediate. The introduced histidine does not coordinate the active site metal, unlike the iron-binding glutamate it replaces. More HEPD activity is observed when the reaction is carried out with (R)-2-[2-2H1]-hydroxyethylphosphonate