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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
dimethylglycine oxidase,
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dimethylglycine dehydrogenase
dimethylglycine dehydrogenase
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dimethylglycine dehydrogenase
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dimethylglycine dehydrogenase
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DMGO
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DMGO1
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DMGO2
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N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
a flavoprotein, FAD
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N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
A flavoprotein, FAD. Does not oxidize sarcosine
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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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oxidative demethylation
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N,N-dimethylglycine:oxygen oxidoreductase (demethylating)
A flavoprotein (FAD). Does not oxidize sarcosine.
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5,10-methenyltetrahydrofolate + reduced N,N-dimethylglycine
5,10-methylene tetrahydrofolate + oxidized N,N-dimethylglycine
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
involved in tetrahydrofolate-dependent assimilation of methyl groups
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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
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
involved in tetrahydrofolate-dependent assimilation of methyl groups
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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N,N-dimethylglycine + H2O + O2
sarcosine + formaldehyde + H2O2
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?
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flavin
8alpha-N1-histidyl flavin
FAD
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FAD
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covalently bound to the N-terminus, biding site structure
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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
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1.39 - 142
N,N-dimethylglycine
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
2.4
N,N-dimethylglycine
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wild-type enzyme
2.4
N,N-dimethylglycine
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wild-type, pH 8.5, 25°C
9.1
N,N-dimethylglycine
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47
N,N-dimethylglycine
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mutant Y259F
47
N,N-dimethylglycine
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mutant Y259F, pH 8.5, 25°C
59
N,N-dimethylglycine
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mutant H225Q
142
N,N-dimethylglycine
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mutant H225Q, pH 8.5, 25°C
0.041
O2
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wild-type, pH 8.5, 25°C
0.117
O2
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mutant H225Q, pH 8.5, 25°C
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0.047 - 14.3
N,N-dimethylglycine
0.047
N,N-dimethylglycine
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mutant Y259F
0.047
N,N-dimethylglycine
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mutant Y259F, pH 8.5, 25°C
4.35
N,N-dimethylglycine
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mutant H225Q
10.6
N,N-dimethylglycine
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wild-type enzyme
10.6
N,N-dimethylglycine
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wild-type, pH 8.5, 25°C
13.6
N,N-dimethylglycine
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mutant H225Q, pH 8.5, 25°C
14.3
N,N-dimethylglycine
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two dmg genes, dmg and dmg2
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brenda
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brenda
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brenda
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SwissProt
brenda
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brenda
bifunctional enzyme
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brenda
two dmg genes, dmg and dmg2
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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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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DMGO_ARTGO
830
0
89985
Swiss-Prot
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A0A2Z3YMY5_9CORY
883
0
94241
TrEMBL
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A0A1J5PJV6_9ZZZZ
82
0
8855
TrEMBL
other Location (Reliability: 1 )
A0A2S6X035_9ACTN
817
0
88876
TrEMBL
-
A0A563VME4_9CYAN
806
1
88967
TrEMBL
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A0A2S6T6P9_9PROT
443
0
48694
TrEMBL
-
F5XJW8_MICPN
Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1)
825
0
89339
TrEMBL
-
A0A653UF96_9MICC
830
0
90666
TrEMBL
-
I4EY51_9ACTN
820
0
88783
TrEMBL
-
L0JY53_9EURY
843
0
93051
TrEMBL
-
A0A3G8JQ00_9ACTN
812
0
88292
TrEMBL
-
A0A177HTH3_9ACTN
812
0
89088
TrEMBL
-
J9Z076_9PROT
824
1
92650
TrEMBL
-
A0A1W6KC48_9ALTE
856
0
96218
TrEMBL
-
A0A1V0RN77_9RHOB
806
0
88387
TrEMBL
-
A0A1F2PE72_9FIRM
458
0
51959
TrEMBL
-
A0A6A7SHT2_9ZZZZ
855
0
94605
TrEMBL
other Location (Reliability: 3 )
A0A653UT26_9MICC
832
0
90101
TrEMBL
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A0A143QI07_9NOCA
821
0
89325
TrEMBL
-
A0A2H5WC39_9BACT
839
0
92981
TrEMBL
-
A0A3Q9JIN4_9MICO
379
0
40136
TrEMBL
-
A0A385ZVE1_9ACTN
812
0
88600
TrEMBL
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A0A2H6AYV8_9BACT
390
0
42335
TrEMBL
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A0K1C3_ARTS2
Arthrobacter sp. (strain FB24)
835
0
90919
TrEMBL
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A0A165MSB2_RHOFA
382
1
40203
TrEMBL
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A0A1F2PRC6_RHOER
375
0
40684
TrEMBL
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A0A395L844_9RHIZ
853
0
95428
TrEMBL
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A0A5J4E486_9BACT
447
0
49035
TrEMBL
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A0A2P5VKQ9_9PROT
260
0
28977
TrEMBL
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J7LLR7_9MICC
830
0
90671
TrEMBL
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A0A161GLT5_RHOFA
821
0
89355
TrEMBL
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A0A653UDH4_9MICC
835
0
90984
TrEMBL
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C1AXN5_RHOOB
Rhodococcus opacus (strain B4)
821
0
89456
TrEMBL
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A0A2R8B6N5_9RHOB
811
0
89088
TrEMBL
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A0A5E7YLE2_9RHOB
806
0
88328
TrEMBL
-
A0A2P8AVQ3_9ACTN
435
0
46696
TrEMBL
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A0A5B8RH90_9ZZZZ
855
0
94605
TrEMBL
other Location (Reliability: 3 )
A0A1F2Q2P9_RHOER
341
0
36426
TrEMBL
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A0A5S9R9E3_MYCVN
814
0
88494
TrEMBL
-
A0A2Z2P2R9_9GAMM
855
0
95279
TrEMBL
-
A0A1J5PCX8_9ZZZZ
219
0
23744
TrEMBL
other Location (Reliability: 3 )
A0A2H5VES4_9ARCH
806
1
91053
TrEMBL
-
A0A2R8CBU5_9RHOB
806
1
87719
TrEMBL
-
A0A6I1ZEN3_9ACTN
811
0
88737
TrEMBL
-
A0A2S6S9T6_9PROT
448
0
49724
TrEMBL
-
A0A177HSJ2_9ACTN
815
0
89227
TrEMBL
-
A0A653ME92_9ALTE
856
0
96162
TrEMBL
-
F0M736_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
835
0
90838
TrEMBL
-
A0A2P5VKU8_9PROT
141
0
15518
TrEMBL
-
K9EQX0_9CYAN
805
1
87578
TrEMBL
-
A0A653TVY4_9MICC
835
0
90320
TrEMBL
-
A0A2H5WFM7_9BACT
271
0
29747
TrEMBL
-
A0A2R8ALT3_9RHOB
430
0
47205
TrEMBL
-
A0A653XHP4_9MICC
830
0
90701
TrEMBL
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82000
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2 * 82000, SDS-PAGE
88000
x * 88000, SDS-PAGE
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dimer
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2 * 82000, SDS-PAGE
dimer
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2 * 82000, SDS-PAGE
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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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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
H225Q
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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
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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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6 - 7.5
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40°C for 15 min: stable between
394961
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to homogeneity, chromatography steps
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to homogeneity, recombinant enzyme
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expression in Escherichia coli
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 in Escherichia coli
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expression in Escherichia coli
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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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Meskys, R.; Harris, R.J.; Casaite, V.; Basran, J.; Scrutton, N.S.
Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp. Implications for glycine betaine catabolism
Eur. J. Biochem.
268
3390-3398
2001
Arthrobacter globiformis (Q9AGP8), Arthrobacter globiformis
brenda
Mori, N.; Kawakami, B.; Tani, Y.; Yamada, H.
Purification and properties of dimethylglycine oxidase from Cylindrocarpon didymum M-1
Agric. Biol. Chem.
44
1383-1389
1980
Cylindrocarpon didymum, Cylindrocarpon didymum M-1
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brenda
Leys, D.; Basran, J.; Scrutton, N.S.
Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase
EMBO J.
22
4038-4048
2003
Arthrobacter globiformis
brenda
Scrutton, N.S.; Leys, D.
Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold
Biochem. Soc. Trans.
33
776-779
2005
Arthrobacter globiformis
brenda
Basran, J.; Fullerton, S.; Leys, D.; Scrutton, N.S.
Mechanism of FAD reduction and role of active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylglycine oxidase: analysis of mutant structure and catalytic function
Biochemistry
45
11151-11161
2006
Arthrobacter globiformis
brenda
Tralau, T.; Lafite, P.; Levy, C.; Combe, J.P.; Scrutton, N.S.; Leys, D.
An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde
J. Biol. Chem.
284
17826-17834
2009
Arthrobacter globiformis
brenda
Casaite, V.; Poviloniene, S.; Meskiene, R.; Rutkiene, R.; Meskys, R.
Studies of dimethylglycine oxidase isoenzymes in Arthrobacter globiformis cells
Curr. Microbiol.
62
1267-1273
2011
Arthrobacter globiformis, Arthrobacter globiformis NRRL B-2979
brenda
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1.5.3.10 dimethylglycine oxidase
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