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Literature summary for 1.5.3.10 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
Search for more literature for 1.5.3.10

Protein Variants

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

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

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N,N-dimethylglycine + H2O + O2
-
 Arthrobacter globiformis sarcosine + formaldehyde + H2O2
-
 ?

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, pH 8.5, 25°C Arthrobacter globiformis
10.6
-
 N,N-dimethylglycine wild-type, pH 8.5, 25°C Arthrobacter globiformis
13.6
-
 N,N-dimethylglycine mutant H225Q, pH 8.5, 25°C Arthrobacter globiformis