EC 1.14.14.30 - Isobutylamine N-monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.14.30

Names

Accepted name:
isobutylamine N-monooxygenase
Other name:
vlmH (gene name)
Systematic name:
2-methylpropan-1-amine,FADH2:O2 N-oxidoreductase

Reactions

Comments:

The enzyme, characterized from the bacterium Streptomyces viridifaciens, is part of a two component system that also includes a flavin reductase, which provides reduced flavin mononucleotide for this enzyme. The enzyme, which is involved in the biosynthesis of the azoxy antibiotic valanimycin, has a similar activity with either FMNH2 or FADH2. It exhibits broad specificity, and also accepts propan-1-amine, butan-1-amine, butan-2-amine and benzylamine.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Parry, R. J., Li, W.
    Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens MG456-hF10.
    Arch. Biochem. Biophys. 339: 47-54 (1997). [PMID: 9056232]
  2. Parry, R. J., Li, W., Cooper, H. N.
    Cloning, analysis, and overexpression of the gene encoding isobutylamine N-hydroxylase from the valanimycin producer, Streptomyces viridifaciens.
    J. Bacteriol. 179: 409-416 (1997). [PMID: 8990292]
  3. Parry, R. J., Li, W.
    An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces viridifaciens. Cloning, analysis, and overexpression.
    J. Biol. Chem. 272: 23303-23311 (1997). [PMID: 9287340]

[EC 1.14.14.30 created 2016, modified 2017]