1.5.3.10: dimethylglycine oxidase
This is an abbreviated version!
For detailed information about dimethylglycine oxidase, go to the full flat file.
Word Map on EC 1.5.3.10
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1.5.3.10
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arthrobacter
-
globiformis
-
sarcosine
-
formaldehyde
-
tetrahydrofolate
-
amine
-
fad
-
flavoprotein
-
t-protein
-
folate-binding
-
folate
-
betaine
-
iminium
-
multiwavelength
-
half-reaction
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charge-transfer
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heterotetrameric
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folate-dependent
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folinic
-
sulfite
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stopped-flow
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methylene
-
aminomethyltransferase
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oxidases
-
tetrahydrofolate-dependent
-
l-proline
-
tetrahydrofolate-binding
- 1.5.3.10
- arthrobacter
- globiformis
- sarcosine
- formaldehyde
- tetrahydrofolate
- amine
- fad
- flavoprotein
-
t-protein
-
folate-binding
- folate
- betaine
-
iminium
-
multiwavelength
-
half-reaction
-
charge-transfer
-
heterotetrameric
-
folate-dependent
-
folinic
- sulfite
-
stopped-flow
-
methylene
- aminomethyltransferase
- oxidases
-
tetrahydrofolate-dependent
- l-proline
-
tetrahydrofolate-binding
Reaction
Synonyms
dimethylglycine dehydrogenase, dmg, DMGO, DMGO1, DMGO2, N,N-dimethylglycine:oxygen oxidoreductase (demethylating)
ECTree
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Engineering
Engineering on EC 1.5.3.10 - dimethylglycine oxidase
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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
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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
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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