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Literature summary extracted from

  • Leys, D.; Basran, J.; Scrutton, N.S.
    Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase (2003), EMBO J., 22, 4038-4048.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.10 expression of wild-type and mutant enzymes in Escherichia coli Arthrobacter globiformis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.3.10 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 Arthrobacter globiformis

Protein Variants

EC Number Protein Variants Comment Organism
1.5.3.10 H225Q site-directed mutagenesis, reduced catalytic activity compared to the wild-type enzyme Arthrobacter globiformis
1.5.3.10 Y259F site-directed mutagenesis, reduced catalytic activity compared to the wild-type enzyme Arthrobacter globiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.10 2.4
-
 N,N-dimethylglycine wild-type enzyme Arthrobacter globiformis
1.5.3.10 47
-
 N,N-dimethylglycine mutant Y259F Arthrobacter globiformis
1.5.3.10 59
-
 N,N-dimethylglycine mutant H225Q Arthrobacter globiformis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.3.10 mitochondrion
-
 Arthrobacter globiformis 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.3.10 additional information Arthrobacter globiformis 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.10 Arthrobacter globiformis
-
 bifunctional enzyme
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.3.10 N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2 = sarcosine + 5,10-methylenetetrahydrofolate + 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 Arthrobacter globiformis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.10 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 Arthrobacter globiformis ?
-
 ?
1.5.3.10 N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2
-
 Arthrobacter globiformis sarcosine + 5,10-methylenetetrahydrofolate + H2O2
-
 ?
1.5.3.10 N,N-dimethylglycine + H2O + O2 In the absence of tetrahydrofolate, formaldehyde is the second product of catalysis, formed by hydrolysis of a labile iminium intermediate. In the cell, toxic formaldehyde is not produced and these enzymes catalyse the formation of 5,10-methylene-THF from THF and the labile iminium intermediate. Arthrobacter globiformis sarcosine + formaldehyde + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.3.10 DMGO
-
 Arthrobacter globiformis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.3.10 0.047
-
 N,N-dimethylglycine mutant Y259F Arthrobacter globiformis
1.5.3.10 4.35
-
 N,N-dimethylglycine mutant H225Q Arthrobacter globiformis
1.5.3.10 10.6
-
 N,N-dimethylglycine wild-type enzyme Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.10 FAD covalently bound to the N-terminus, biding site structure Arthrobacter globiformis