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Literature summary for 1.5.8.2 extracted from

  • Shi, W.; Mersfelder, J.; Hille, R.
    The interaction of trimethylamine dehydrogenase and electron-transferring flavoprotein (2005), J. Biol. Chem., 280, 20239-20246.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant T442G enzymes in Escherichia coli strain Bl21(DE3) Methylophilus methylotrophus

Protein Variants

Protein Variants Comment Organism
Y442G site-directed mutagenesis Methylophilus methylotrophus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics, dissociation constants, thermodynamics Methylophilus methylotrophus

Organism

Organism UniProt Comment Textmining
Methylophilus methylotrophus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme, and recombinant wild-type and mutant T442G enzymes expressed in Escherichia coli strain BL21(DE3) Methylophilus methylotrophus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trimethylamine + H2O + oxidized electron-transferring flavoprotein
-
Methylophilus methylotrophus dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
-
r
trimethylamine + H2O + semiquinone electron-transferring flavoprotein
-
Methylophilus methylotrophus dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
-
r

Synonyms

Synonyms Comment Organism
TMADH
-
Methylophilus methylotrophus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
Abz-VAA
-
Methylophilus methylotrophus

Cofactor

Cofactor Comment Organism Structure
electron-transferring flavoprotein interaction with the enzyme, binding study, reaction mechanism and kinetics Methylophilus methylotrophus
FAD
-
Methylophilus methylotrophus