Information on EC 1.13.11.72 - 2-hydroxyethylphosphonate dioxygenase

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The expected taxonomic range for this enzyme is: Streptomyces viridochromogenes

EC NUMBER
COMMENTARY hide
1.13.11.72
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RECOMMENDED NAME
GeneOntology No.
2-hydroxyethylphosphonate dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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phosalacine biosynthesis
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phosphinothricin tripeptide biosynthesis
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Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming)
Requires non-heme-Fe(II). Isolated from some bacteria including Streptomyces hygroscopicus and Streptomyces viridochromogenes. The pro-R hydrogen at C-2 of the ethyl group is retained by the formate ion. Any stereochemistry at C-1 of the ethyl group is lost. One atom from dioxygen is present in each product. Involved in phosphinothricin biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-hydroxypropylphosphonate + O2
2-oxopropylphosphonate + hydroxymethylphosphonate + acetate
show the reaction diagram
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substrate partitions between conversion to 2-oxopropylphosphonate and hydroxymethylphosphonate
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?
(R)-2-hydroxyethylphosphonate + O2
hydroxymethylphosphonate + formate
show the reaction diagram
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product is almost racemic
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?
(S)-2-hydroxyethylphosphonate + O2
hydroxymethylphosphonate + formate
show the reaction diagram
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product is almost racemic
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?
1-hydroxy-2,2,2-trifluoroethylphosphonate + O2
trifluoroacetylphosphonate
show the reaction diagram
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-
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?
1-hydroxyethylphosphonate + O2
acetylphosphate
show the reaction diagram
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?
2-hydroxyethylphosphonate + O2
hydroxymethylphosphonate + formate
show the reaction diagram
hydroxymethylphosphonate + O2
phosphate + formate
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no cofactors required
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0098 - 0.8
2-hydroxyethylphosphonate
0.033 - 0.1
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 0.81
2-hydroxyethylphosphonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13 - 36
2-hydroxyethylphosphonate
3950
0.1 - 11
O2
9
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.8 A resolution. The overall structure consists of imperfect tandem repeats of a bi-domain architecture. Each of the repeats is composed of an all-alpha-helical domain linked to a beta-barrel fold characteristic of the cupin superfamily. A Cd(II) ion is situated at the base of the active site and is coordinated by residues His 129, Glu 176 and His 182
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K16A
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loss of enzymic activity
R90A
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large decrease in ratio kcat/Km, mutant cannot be saturated in O2
R90K
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slight decrease in ratio kcat/Km
Y98F
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large decrease in ratio kcat/Km, mutant cannot be saturated in O2. Mutant produces methylphosphonate as a minor side product