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Information on EC 1.13.11.73 - methylphosphonate synthase
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
1.13.11.73
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RECOMMENDED NAME
GeneOntology No.
methylphosphonate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-
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-
-
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2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-
catalytic mechanism
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2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-
initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species, catalytic mechanism, detailed overview
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (methylphosphonate forming)
Isolated from the marine archaeon Nitrosopumilus maritimus.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
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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
evolution
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2-hydroxyethylphosphonate dioxygenase (HEPD, EC 1.13.11.72) and methylphosphonate synthase (MPnS) are non-heme iron oxygenases that both catalyze the carbon-carbon bond cleavage of 2-hydroxyethylphosphonate but generate different products. Both HEPD and MPnS generate a methylphosphonate radical. Substrate labeling experiments lead to a mechanistic hypothesis in which the fate of a common intermediate determines product identity, overview. Primary sequences and homology modeling suggest that the architectures of the active sites of HEPD and MPnS are similar
evolution
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one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD, EC 1.13.11.72) and methylphosphonate synthase (MPnS) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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-
-
-
?
(S)-2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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-
-
-
?
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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enzyme catalyzes the asymmetric oxidation of hydroxyethylphosphonate, with all four electrons being derived from the C-2 carbon
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-
?
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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stereospecific hydrogen transfer of the pro-R hydrogen at C2 of the substrate to the methyl group of methylphosphonate. Neither hydrogen transfer is rate limiting under saturating substrate conditions
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-
?
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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the pro-(R) hydrogen at C2 of 2-hydroxyethylphosphonate is quantitatively incorporated by enzyme MPnS into methylphosphonate. AN irreversible step involving O2
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ir
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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-
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-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxyethylphosphonate + O2
methylphosphonate + HCO3-
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-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Fe2+
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a mononuclear non-heme iron-dependent enzyme. MPnS contains iron-binding residues at only the two histidines, raising the specter that either MPnS is a 2-His only enzyme or that the third ligand is not well conserved in the alignment
Fe2+
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a non-heme iron oxygenase, Fe2+ is required for catalysis
Iron
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Fe(II)-dependent oxygenase that cleaves the unactivated C-C bond of 2-hydroxyethylphosphonate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0071
(R)-2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
0.0065
(S)-2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
0.0045
2-hydroxyethylphosphonate
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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
LITERATURE
IMAGE
0.17
(R)-2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
0.17
(S)-2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
0.18
2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
(R)-2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
26
(S)-2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
40
2-hydroxyethylphosphonate
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temperature not specified in the publication, pH not specified in the publication
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Nitrosopumilus maritimus (strain SCM1);
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutant E176H, X-ray diffraction structure determination and analysis at 1.75 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the mutant enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.13.11.73)
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