Information on EC 1.5.3.10 - dimethylglycine oxidase

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

EC NUMBER
COMMENTARY hide
1.5.3.10
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RECOMMENDED NAME
GeneOntology No.
dimethylglycine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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oxidative demethylation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
N,N-dimethylglycine:oxygen oxidoreductase (demethylating)
A flavoprotein (FAD). Does not oxidize sarcosine.
CAS REGISTRY NUMBER
COMMENTARY hide
74870-79-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two dmg genes, dmg and dmg2
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Manually annotated by BRENDA team
strain M-1
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Manually annotated by BRENDA team
strain M-1
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydrofolate + reduced N,N-dimethylglycine
5,10-methylene tetrahydrofolate + oxidized N,N-dimethylglycine
show the reaction diagram
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
show the reaction diagram
additional information
?
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bifunctional enzyme catalyzing the formation of 5,10-methylene tetrahydrofolate and the oxidation of N,N-dimethylglycine, folate binding and active site, a large channel connects both active sites, the channeling is kinetically controlled by terahydrofolate binding, overview
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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,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
show the reaction diagram
additional information
?
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bifunctional enzyme catalyzing the formation of 5,10-methylene tetrahydrofolate and the oxidation of N,N-dimethylglycine, folate binding and active site, a large channel connects both active sites, the channeling is kinetically controlled by terahydrofolate binding, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
8alpha-N1-histidyl flavin
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5-dithio-bis(2-nitrobenzoic acid)
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28% inhibition at 1 mM
Ag+
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45% inhibition at 1 mM
Hg2+
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89% inhibition at 1 mM
iodoacetate
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complete inhibition at 1 mM
Mn2+
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30% inhibition at 1 mM
NaCl
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the specific activity of DMGO decreased when cells are grown in the medium with high NaCl concentration. High osmolarity inhibits the activity of the enzyme, but not in the case of the medium with glycine betaine as the sole carbon source
Zn2+
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51% inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycine betaine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.39 - 142
N,N-dimethylglycine
0.041 - 0.117
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 14.3
N,N-dimethylglycine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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DMGO1 and DMGO2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 88000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with folate compounds. N-terminal region covalently binds FAD and has dimethylglycine dehydrogenase activity
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mutant D552A in complex with tetrahydrofolate. Presence of one water molecule instead of the Asp552 side chain
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purified recombinant wild-type enzyme, sitting-drop vapour diffusion method, 0.004 ml of protein solution containing 15 mg/ml protein, mixed with 0.002 ml reservoir solution containing 15% PEG 5000 monomethylether, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.5, magnesium salt can be exchanged for acetate, for complexing the crystals are soaked in a solution containing folic or folinic acid in 15% PEG 5000 monomethylether and 0.3 M NaCl for 10 min, X-ray diffraction structure determination and analysis at 1.60 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
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40C for 15 min: stable between
394961
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography steps
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to homogeneity, recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli
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two dmg genes, dmg and dmg2, DNA and amino acid sequence determination, genetic organization, quantitative real-time pCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glycine betaine induces the expression of the dmg genes by about 300fold at 5 mM
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D552A
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mutation leads to increased formaldehyde release
additional information
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complete removal of 5,10-CH2-THF synthase domain through expression of a truncated version generates a mutant enzyme unable to avoid hydrolysis of the imine species generated following amine oxidation