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Enzyme Nomenclature
Information on EC 1.5.3.10 - dimethylglycine oxidase
for references in articles please use BRENDA:EC1.5.3.10
Word Map on EC 1.5.3.10
- 1.5.3.10
- arthrobacter
- globiformis
- sarcosine
-
t-protein
- flavoprotein
- tetrahydrofolate
- formaldehyde
- amine
- fad
- betaine
-
folate-binding
- folate
-
methylene
-
heterotetrameric
-
multiwavelength
-
oxidases
-
folate-dependent
- aminomethyltransferase
-
half-reaction
-
folinic
-
tetrahydrofolate-dependent
-
charge-transfer
- l-proline
-
stopped-flow
- sulfite
-
iminium
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.5.3.10
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RECOMMENDED NAME
GeneOntology No.
dimethylglycine oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
a flavoprotein, FAD; A flavoprotein, FAD. Does not oxidize sarcosine
-
-
-
N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
reaction mechanism, substrate binding structures, bifunctional enzyme catalyzing the formation of 5,10-methylne tetrahydrofolate and the oxidation of N,N-dimethylglycine, active site structures, Tyr259 and His225 are involved in catalysis
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N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
tetrahydrofolate-binding site of enzyme is highly specific for reduced folate compounds and enhances the nucleophilic character of the tetrahydrofolate N10 position
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative demethylation
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-
-
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redox reaction
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-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
74870-79-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
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in high-salinity media with 1 M NaCl, Arthrobacter globiformis accumulates 360 mM of glycine betaine when the main source of carbon is glucose and 180 mM glycine betaine when the sole carbon source is glycine betaine
metabolism
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in high-salinity media with 1 M NaCl, Arthrobacter globiformis accumulates 360 mM of glycine betaine when the main source of carbon is glucose and 180 mM glycine betaine when the sole carbon source is glycine betaine
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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
5,10-methenyltetrahydrofolate + reduced N,N-dimethylglycine
5,10-methylene tetrahydrofolate + oxidized N,N-dimethylglycine
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-
-
-
-
additional information
?
-
-
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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-
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
-
-
-
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
involved in tetrahydrofolate-dependent assimilation of methyl groups
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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the oxidation of dimethylglycine is coupled to the synthesis of 5,10-methylenetetrahydrofolate through an unusual substrate channeling mechanism. Uncoupling of the active sites can be achieved by mutagenesis or deletion of the 5,10-methylenetetrahydrofolate synthase site and this leads to accumulation of intracellular formaldehyde. Channeling occurs by nonbiased diffusion of the labile intermediate through a large solvent cavity connecting both active sites
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-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
-
-
-
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
-
-
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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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
additional information
?
-
-
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
-
-
-
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
-
-
-
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
Q9AGP8
involved in tetrahydrofolate-dependent assimilation of methyl groups
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
-
-
-
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
-
-
-
?
N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.39
N,N-dimethylglycine
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DMGO1, pH 9.0, temperature not specified in the publication
1.86
N,N-dimethylglycine
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DMGO2, pH 9.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
glycine betaine induces the expression of the dmg genes by about 300fold at 5 mM
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glycine betaine induces the expression of the dmg genes by about 300fold at 5 mM
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-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H225Q
Y259F
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
H225Q
-
site-directed mutagenesis, reduced catalytic activity compared to the wild-type enzyme
H225Q
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modest changes in kinetic parameters, no stabilization of FADH2-iminium charge-transfer complex
Y259F
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site-directed mutagenesis, reduced catalytic activity compared to the wild-type enzyme
Y259F
-
able to oxidize substrate, steady-state turnover is attenuated 200fold, rate of FAD reduction is substantially impaired, no stabilization of FADH2-iminium charge-transfer complex
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.3.10)
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