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Literature summary for 1.5.8.2 extracted from

  • Steenkamp, D.J.
    Identification of the prosthetic groups of dimethylamine dehydrogenase from Hyphomicrobium X (1979), Biochem. Biophys. Res. Commun., 88, 244-250.
    View publication on PubMed
Search for more literature for 1.5.8.2

Inhibitors

Inhibitors Comment Organism Structure
diphosphate noncompetitive inhibition to 50% of initial activity with respect to trimethylamine Hyphomicrobium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
trimethylamine + H2O + electron acceptor Hyphomicrobium sp.
-
 dimethylamine + formaldehyde + reduced electron acceptor
-
 ?
trimethylamine + H2O + electron acceptor Hyphomicrobium sp. X
-
 dimethylamine + formaldehyde + reduced electron acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Hyphomicrobium sp.
-
 Hyphomicrobium X
-

Purification (Commentary)

Purification (Comment) Organism
partial Hyphomicrobium sp.

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
 Hyphomicrobium sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.6
-
-
 Hyphomicrobium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trimethylamine + H2O + electron acceptor
-
 Hyphomicrobium sp. dimethylamine + formaldehyde + reduced electron acceptor
-
 ?
trimethylamine + H2O + electron acceptor
-
 Hyphomicrobium sp. X dimethylamine + formaldehyde + reduced electron acceptor
-
 ?

Cofactor

Cofactor Comment Organism Structure
FMN 6-S-cysteinyl-FMN coenzyme-peptide Hyphomicrobium sp.