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Literature summary for 1.5.3.10 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
bifunctional enzyme
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2
-
Arthrobacter globiformis sarcosine + 5,10-methylenetetrahydrofolate + H2O2
-
?
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

Synonyms Comment Organism
DMGO
-
Arthrobacter globiformis

Turnover Number [1/s]

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

Cofactor

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