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Literature summary extracted from

  • 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 (2006), Biochemistry, 45, 11151-11161.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.5.3.10 H225Q modest changes in kinetic parameters, no stabilization of FADH2-iminium charge-transfer complex Arthrobacter globiformis
1.5.3.10 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 Arthrobacter globiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.10 0.041
-
O2 wild-type, pH 8.5, 25°C Arthrobacter globiformis
1.5.3.10 0.117
-
O2 mutant H225Q, pH 8.5, 25°C Arthrobacter globiformis
1.5.3.10 2.4
-
N,N-dimethylglycine wild-type, pH 8.5, 25°C Arthrobacter globiformis
1.5.3.10 47
-
N,N-dimethylglycine mutant Y259F, pH 8.5, 25°C Arthrobacter globiformis
1.5.3.10 142
-
N,N-dimethylglycine mutant H225Q, pH 8.5, 25°C Arthrobacter globiformis

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.10 N,N-dimethylglycine + H2O + O2
-
Arthrobacter globiformis sarcosine + formaldehyde + H2O2
-
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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, pH 8.5, 25°C Arthrobacter globiformis
1.5.3.10 10.6
-
N,N-dimethylglycine wild-type, pH 8.5, 25°C Arthrobacter globiformis
1.5.3.10 13.6
-
N,N-dimethylglycine mutant H225Q, pH 8.5, 25°C Arthrobacter globiformis