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CATH Superfamily 3.50.50.60

FAD/NAD(P)-binding domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
FAD/NAD(P)-binding domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 65: Dimethylaniline monooxygenase [N-oxide-forming]

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Flavin-containing monooxygenase. [EC: 1.14.13.8]
N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.
  • A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines.
  • Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate.
  • Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites.
  • For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl- 1,2,3,6-tetrahydropyridine (MPTP).
  • Formerly EC 1.13.12.11.
 28 A0A024R934 A0A024R934 A0A2J8LLM2 A0A2J8LLM2 A0A2J8LLM2 A0A2R9B464 A0A2R9B464 A0A2R9B464 A0A480Y4M1 A0A480Y4M1
(18 more...)
Trimethylamine monooxygenase. [EC: 1.14.13.148]
N,N,N-trimethylamine + NADPH + O(2) = N,N,N-trimethylamine N-oxide + NADP(+) + H(2)O.
  • The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy.
  • The mammalian enzyme is involved in detoxification of trimethylamine.
  • Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome).
 2 Q8HYJ9 Q95LA1
Albendazole monooxygenase (sufoxide-forming). [EC: 1.14.14.73]
(1) Albendazole + [reduced NADPH--hemoprotein reductase] + O(2) = albendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O. (2) Fenbendazole + [reduced NADPH--hemoprotein reductase] + O(2) = fenbendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O.
  • This is one of the activities carried out by some microsomal cytochrome P450 monooxygenases.
  • A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32), but it is estimated that cytochrome P450s are responsible for 70% of the activity.
 2 Q8HYJ9 Q95LA1
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